CCR8 antibodies for therapeutic applications

Abstract

The present invention relates to tools and methods for the generation of antibodies which specifically bind chemokine receptors, such as CC or CXC chemokine receptors. Provided are isolated sulfated polypeptides and conjugates thereof, which can be used for example as antigens or for off target panning to facilitate the generation of anti-human, anti-cynomolgus, and / or anti-mouse chemokine receptor antibodies, e.g. for the generation of antibodies with fully human CDRs and / or other favorable properties for therapeutic use. The present invention furthermore relates to antibodies and conjugates thereof which can be obtained by applying the aforementioned tools and methods. Provided are antibodies specifically binding to human, cynomolgus and / or murine CCR8 with favorable properties for therapeutic use, such as cross-reactive antibodies, fully human antibodies, low internalizing (including non- internalizing) antibodies, and antibodies efficiently inducing ADCC and / or ADCP in Treg cells. Also provided are medical uses of the disclosed antibodies or conjugates and / or treatment methods comprising the administration of these antibodies to a patient or subject, either alone or in combination. Biomarkers, stratification methods and diagnostic methods are finally provided to predict or evaluate responsiveness to anti-CCR8 antibody monotherapy or combination therapy. The invention furthermore provides tools and methods for producing the foregoing antibodies, pharmaceutical compositions, diagnostic uses of the antibodies, and kits with instructions for use.

Description

CCR8 ANTIBODIES FOR THERAPEUTIC APPLICATIONS DESCRIPTION Technical Field The present invention relates to tools and methods for the generation of antibodies which specifically bind chemokine receptors, such as CC or CXC chemokine receptors. Provided are isolated sulfated polypeptides and conjugates thereof, which can be used for example as antigens or for off target panning to facilitate the generation of anti-human, anti-cynomolgus, and / or anti-mouse chemokine receptor antibodies, e.g. for the generation of antibodies with fully human CDRs and / or other favorable properties for the rapeutic use. The present invention furthermore relates to antibodies and conjugates thereof which can be obtained by applying the aforementioned tools and methods. Provided are antibodies specifically binding to human, cynomolgus and / or murine CCR8 with favorable properties for therapeutic use, such as cross-reactive antibodies, fully human antibodies, low internalizing (including non-internalizing) antibodies, and antibodies efficiently inducing ADCC and / or ADCP in Treg cells. Also provided are medical uses of the inventive antibodies or conjugates and / or treatment methods comprising the administration of these antibodies to a patient or subject, either alone or in combination. Biomarkers, stratification methods and diagnostic methods are finally provided to predict or evaluate responsiveness to anti-CCR8 antibody monotherapy or combination therapy. The invention furthermore provides tools and methods for producing the foregoing antibodies, pharmaceutical compositions, diagnostic uses of the antibodies, and kits with instructions for use. Technical Problem Antibody generation for CC and CXC chemokine receptors CXC and CC chemokine-receptors are specific seven-transmembrane G-protein-coupled receptors that mediate cell migration in chemotactic gradients. Chemokine receptors are a challenging target class for antibody generation due to their inherent structural, biophysical and biological properties. There are multiple reasons for the difficulties to obtain optimal antibodies against chemokine receptors which shall be discussed in an exemplary fashion, with an emphasis on human CCR8. Chemokine receptors are characterized by seven domains embedded in the cell membrane and therefore cannot be easily purified in their native confirmation. A purified, native chemokine receptor will have been removed from the membrane environment and is therefore likely to be conformationally compromised. These corrupted structures are typically not suitable for antibody generation, because antibodies are required to recognize the intact antigen as it is presented at the cell surface. Although some chemokine receptors, such as CXCR4 and CCR5, possess some inherent stability that allows for purification in mild detergents, this does not apply to most chemokine receptors (Hutchings, Catherine J., et al. "Opportunities for therapeutic antibodies directed at G-protein-coupled receptors." Nature reviews Drug discovery 16.11 (2017): 787.). This is emphasized by the fact, that until today, no X-ray crystal structure is available for CCR8 in the Protein Data Bank PDB (rcsb.org). In consequence, solubilization for obtaining the required amounts of protein in the native conformation as well as correct orientation and folding for use as immunogen is difficult for chemokine receptors (cf. Klarenbeek, Alex, et al. "Targeting chemokines and chemokine receptors with antibodies." Drug Discovery Today: Technologies 9.4 (2012): e237-e244.). A schematic representation of the overall structure of human CCR8 is shown in Fig. 2 b. Of the 355 amino acids, residues 1-35 (N term), 94-107 (ECL1), 172-202 (ECL2) and 264-280 (ECL3) have been predicted as extracellular domains (uniprot.org). These extracellular domains are assumed to adopt a tertiary structure, stabilized by disulfide bonds. On average, less than 30 % of a chemokine receptor is thus exposed at the cell surface. In consequence, chemokine receptors and particularly CCR8 are not easily accessible for antibody binding, as described also in WO200744756. Furthermore, antibodies generated against peptides corresponding to extracellular domains of chemokine receptors often fail to recognize the intact receptor on the cell, possibly due to differences in secondary structure. In consequence, researchers in this field have had a low success rate in developing antibodies (Tschammer, Nuska, ed. Chemokines: chemokines and their receptors in drug discovery. Vol. 14. Springer, 2015, Chapter by J.E. Pease & R. Horuk, section 6, page 12, 2nd para). Antibody generation to obtain anti-murine CCR8 antibodies seems slightly less difficult and conventional approaches such as the one described by Kremer and Márquez could be reproduced by the inventors (D'Ambrosio, Daniele, and Francesco Sinigaglia. Cell Migration in Inflammation and Immunity. Springer, 2004., Chapter by Kremer and Márquez p. 243 – 260). Murine and human CCR8 have a sequence identity of <com:Math><semantics>∼70<annotation encoding="application / x-tex">\sim 70< / annotation>< / semantics>< / com:Math> %, which is even lower for the extracellular domains, as described in more detail in example 2. Nevertheless, Kremer and Márquez discuss, that production of anti-mouse chemokine- receptor monoclonal antibodies is a demanding challenge and that antibodies against murine chemokine receptors are comparably scarce, despite the time that has passed since their amino acid sequences were first reported. Therapeutic antibodies for CCR8 and medical uses thereof Despite the difficulties associated with their generation, antibodies targeting CC chemokine receptors have been suggested as promising therapeutic tools in various diseases, e.g. based on mechanistic insights in diseases with involvement of immune cells or in various cancer indications characterized by aberrant expression of chemokine receptors. In 2004, Curiel et al. could show for CD4+CD25+FOXP3+ regulatory T cells (Treg cells or Tregs) in 104 individuals affected with ovarian carcinoma, that human tumor Treg cells suppress tumor-specific T cell immunity and contribute to growth of human tumors in vivo (Curiel, Tyler J., et al. "Specific recruitment of regulatory T cells in ovarian carcinoma fosters immune privilege and predicts reduced survival." Nature medicine 10.9 (2004): 942-949.). Tumor cells and microenvironmental macrophages produce chemokines such as CCL22, which mediates trafficking of Treg cells to the tumor. High level of Tregs in the tumor microenvironment are not only associated with poor prognosis in many cancers, such as ovarian, breast, renal, and pancreatic cancer, but cause the suppression of the immune response against these cancers, e.g. by suppressing the action of the effector cells of the immune system. This specific recruitment of Treg cells thus represents a mechanism by which tumors may foster immune privilege. It has therefore been suggested to block Treg cell migration or function to defeat human cancer. Being aware of the finding of Curiel, two independent teams around Plitas / Rudensky and De Simone / Abrignani / Pagani found that tumor infiltrating Treg cells are characterized by selective expression of CCR8. Indeed, selectivity of Treg cell depletion for the tumor infiltrating Tregs is important because systemic depletion of Treg cells may cause severe autoimmunity (Nishikawa, Hiroyoshi, and Shimon Sakaguchi. "Regulatory T cells in tumor immunity." International journal of cancer 127.4 (2010): 759- 767.). The search for a specific Treg marker is complicated by the fact, that Treg cells show a molecular pattern which resembles effector lymphocytes, cf. example 11.2. Both peripheral Tregs and tumor- specific effector cells should not suffer from friendly fire during depletion of intra-tumoral Tregs, because peripheral Tregs are important to avoid autoimmunity while tumor-specific effector cells assist in keeping the tumor under control. Based on these findings various teams have suggested to use CCR8 antibodies for selective depletion of tumor-infiltrating regulatory T cells. While some have presented data confirming tumor reduction in tumor models using anti-human CCR4 or anti-murine CCR8 antibodies, thereby confirming the mechanistic concept of Treg depletion, there is a need for therapeutic anti-human CCR8 antibodies, e.g. with superior properties in therapeutic applications. Prior art 1.1 Antigens, methods & antibodies The selection of an antigen in antibody generation is crucial for the properties of the resulting antibodies and may pose serious problems as discussed elsewhere herein for chemokine receptors such as CCR8. In some cases, antibodies have been obtained using whole cells as antigens, which were engineered for overexpression of chemokine receptors. At least for some chemokine receptors, these approaches seem to suffer from low numbers of resulting binders. Furthermore, antibodies obtained with these antigens are often characterized by off-target binding and low specificity for the chemokine receptor. If whole cells are used as antigens, immunodominant epitopes can mask other less antigenic ones, where the less antigenic would otherwise have the potential of generating the desired selective and specific antibodies. For CCR8, a successful "whole cell" approach has been described in WO2007044756 (ICOS). In brief, anti-CCR8 monoclonal antibodies were developed by immunizing Balb / c mice with irradiated cells transfected with CCR8 which had high levels of CCR8 expressed on the cell surface. Spleen cells from these mice were fused by standard methods to create hybridomas producing the antibodies. Positive pools were identified by FACS and were cloned by limiting dilution. Two of the antibodies, 433H and 459M, showed a specific reactivity to human CCR8 in immunohistochemistry. Antibody 433H is still available and can be purchased from BD. Biolegend distributes clone L263G8, a purified mouse IgG2a anti-human CCR8 antibody which has been generated using human CCR8 transfectants as immunogen. Kremer and Márquez have described the generation of monoclonal antibodies against murine CCR8 (D'Ambrosio, Daniele, and Francesco Sinigaglia. Cell Migration in Inflammation and Immunity. Springer, 2004., Chapter by Kremer and Márquez p. 243 – 260). In brief, Kremer and Márquez describe the use of peptides derived from the extracellular domains of murine CCR8 as immunogens, but do not suggest sulfation of the tyrosines. Indeed, the inventors found that the approach described by Kremer and Márquez can be successfully applied for antibodies recognizing murine CCR8 but has low success rates for antibodies recognizing human CCR8. Schaerli et al. have generated anti-human CCR8 antibodies by immunizing rabbits with a human CCR8 peptide conjugate, corresponding to positions 1–34 of the N-terminal region of CCR8 coupled to either KLH or BSA, but again, do not suggest sulfation of the tyrosines (Schaerli, Patrick, et al. "A skin-selective homing mechanism for human immune surveillance T cells." The Journal of experimental medicine 199.9 (2004): 1265-1275.). A murine monoclonal antibody binding to a 26–amino acid–containing peptide from the extracellular N- terminal portion of CCR8 has been described by Haque et al. (Haque, Nasreen S., et al. "The chemokine receptor CCR8 mediates human endothelial cell chemotaxis induced by I-309 and Kaposi sarcoma herpesvirus-encoded vMIP-I and by lipoprotein (a)-stimulated endothelial cell conditioned medium." Blood, The Journal of the American Society of Hematology 97.1 (2001): 39-45.). None of these methods for antibody generation uses an isolated sulfated polypeptide comprising the tyrosine rich domain (TRD) of a chemokine receptor or transmembrane protein as antigen. Use of an isolated sulfated polypeptide comprising the TRD of a chemokine receptor or transmembrane protein as antigen influences both, structural and functional features of the set of obtained antibodies, as discussed elsewhere herein. In consequence, the antibodies according to the current invention are assumed do deviate in structure and function from the aforementioned prior art antibodies, e.g. at least in their affinity for sulfated CCR8, in their affinity for unsulfated CCR8, in their way and degree of modulating receptor signaling, in their internalization behavior, in cross reactivity, in clearance and pharmacokinetic behavior and finally in Treg depletion and / or efficacy for therapeutic applications. Furthermore, the use of the antigens disclosed herein enabled the generation of fully human antibodies. In contrast, the discussed prior art antibodies for CCR8 are of non-human origin and deviate from some of the inventive antibodies at least because they do not comprise human CDRs. 1.2 Medical uses and mode of action Cancer immunotherapy involves the use of a subject's immune system to treat or prevent cancer. Immunotherapies typically exploit the fact that cancer cells often have subtly different molecules on their surface that can be detected by the immune system, the cancer antigens. Immunotherapy thus involves provocation of the immune system into attacking tumor cells via these cancer antigens. However, some cancers, such as solid tumors or hematological cancers can escape immune surveillance. For example, tumor infiltration by regulatory T cells (Treg cells or Tregs) and, more specifically, low ratio of effector T cells (Teff) to Tregs have been proposed as critical factors for hiding the tumor from the immune system (Smyth, Mark J., Shin Foong Ngiow, and Michele WL Teng. "Targeting regulatory T cells in tumor immunotherapy." Immunology and cell biology 92.6 (2014): 473-474.). Foxp3-expressing regulatory T cells, which are indispensable for preventing autoimmunity, are known to effectively suppress tumor immunity. Treg cells abundantly infiltrate into tumor tissues, which is often associated with poor prognosis in cancer patients. Removal of Treg cells enhances anti-tumor immune responses but may also elicit autoimmunity. A key issue for tailoring Treg-targeting cancer immunotherapy resides in specific depletion of Treg cells infiltrating into tumor tissues without affecting tumor-reactive effector T cells, while suppressing autoimmunity. Back in 2010 various groups had already investigated that Treg removal, e.g. by depletion with anti-CD25 antibodies, could improve antitumor immunity in mice. It had been shown that depletion of Tregs before the inoculation of tumor cells led to their efficient rejection while Treg depletion occurring simultaneously with or after tumor inoculation resulted in no tumor regression. It had furthermore been suggested, that this was due to the fact, that the administered depleting antibodies also removed CD25-expressing effector T cells, while CD25–Foxp3+ Tregs persisted (Klages, Katjana, et al. "Selective depletion of Foxp3+ regulatory T cells improves effective therapeutic vaccination against established melanoma." Cancer research 70.20 (2010): 7788-7799.). In 2015, the afucosylated humanized anti-human CCR4 monoclonal antibody mogamulizumab (KW- 0761) was evaluated in a clinical study for patients with CCR4-positive cancers (Kurose, Koji, et al. "Phase Ia study of FoxP3+ CD4 Treg depletion by infusion of a humanized anti-CCR4 antibody, KW- 0761, in cancer patients." Clinical Cancer Research 21.19 (2015): 4327-4336.). CCR4 is expressed on regulatory T cells. Indeed, mogamulizumab efficiently depleted Treg cells and an augmentation or induction of specific immune responses to cancer antigens was observed. However, mogamulizumab targets both, peripheral as well as intra-tumoral Tregs and further effector cell polulations, thereby leading to immunological side effects such as skin rashes or Stevens Johnson syndrome. Thus, although the great potential for Treg depletion in cancer therapies was obvious, a concept to selectively target the Tregs and to avoid overt autoimmunity was missing. This was changed with the work of two teams around Plitas / Rudensky and De Simone / Abrignani / Pagani in 2015 and 2016. Plitas et al. demonstrated that CCR8 is selectively expressed by human breast cancer infiltrating Treg cells and immediately concluded that targeting CCR8 represents a promising immunotherapeutic approach for the treatment of patients with breast cancer and further tumors (Plitas, G., et al. "Abstract P4-04-11: Preferential expression of the chemokine receptor 8 (CCR8) on regulatory T cells (Treg) infiltrating human breast cancers represents a novel immunotherapeutic target." (2016): P4-04.; Plitas, George, et al. "Regulatory T cells exhibit distinct features in human breast cancer." Immunity 45.5 (2016): 1122-1134.; US10087259). Only shortly after publication of the initial work of Plitas et al., De Simone et al. published an analysis on the transcriptional landscape of tumor infiltrating T regulatory cells and found that tumor-infiltrating Treg cells were highly immune suppressive and expressed CCR8 on their cell surface as a specific signature molecule (De Simone, Marco, et al. "Transcriptional landscape of human tissue lymphocytes unveils uniqueness of tumor-infiltrating T regulatory cells." Immunity 45.5 (2016): 1135-1147., WO2017198631). The authors described that CCR8 correlated with poor prognosis and concluded that CCR8 could be an interesting therapeutic target to inhibit Treg cells trafficking to tumor sites, without disturbing recruitment of other effector T cells that do not express CCR8. WO2018112032 and WO2018112033 describe methods of decreasing the number or activity of tumor infiltrating T regulatory cells (TITR) in a tumor comprising administering an agent that induces cytotoxicity in cells that express a product of a gene, e.g. CCR8. WO2018112033 and EP3431105 describe a molecule which can modulate the expression and / or function of at least one marker that is selectively deregulated in tumor-infiltrating regulatory T cells for use in the prevention and / or treatment of this tumor. WO2018181425 relates to an antibody against CCR8 having ADCC activity, for use in a method of treating a cancer, wherein the antibody against CCR8 is a CCR8-neutralizing antibody. WO2018181425 does not disclose specific antibody sequences but refers to rat anti-mouse CCR8 clone SA214G2 distributed by BioLegend under Cat. No. 150302. This antibody was used as a tool antibody to recapitulate the previously described anti-tumorigenic effects of Treg depletion in mice. According to the current invention, a method is provided which facilitates the generation of anti-CCR8 antibodies and yields antibodies having superior properties for therapeutic uses. The antibodies according to the current invention were compared with the prior art antibodies and were found to deviate in structure, function and therapeutic efficacy, as discussed elsewhere herein. Solution to Problem 1.1 Antibody generation for CC and CXC chemokine receptors Because prior art approaches to generate antibodies for CC chemokine receptors suffer from low success rates, and resulting antibodies often show a poor performance (cf. e.g. example 3), the inventors developed a novel method to generate antibodies for chemokine receptors in general and, in particular, to generate anti-CCR8 antibodies. The use of a specifically modified isolated polypeptide as antigen for the selection of human anti-human CCR8 antibodies solved the problem to provide an improved method for antibody generation against CC and CXC chemokine receptors, such that e.g. fully human anti-CCR8 antibodies could be obtained for the first time, cf. example 6. In more detail, a polypeptide comprising the tyrosine rich domain of human CCR8, optionally including the LID domain, was modified by introduction of sulfate modifications at specific positions in order to form the antigen, cf. example 4, Table 4.1. A phage display approach was optionally used together with this specifically modified antigen to select fully human anti-human CCR8 antibodies. In the alternative, the sulfated antigens can be used in various further methods, e.g. in conventional immunization approaches. The obtained antibodies showed an excellent binding profile for the sulfated antigen and the biological target expressed under physiological conditions, cf. examples 6, 10.1.1, but a comparably low or no affinity for the unmodified antigen, cf example 10.1.2, example 10.1.3, demonstrating that the sulfated residues were indeed crucial for antigen antibody binding. The inventive antibodies furthermore showed an excellent and also specific binding on cell lines engineered to express human, cynomolgus or murine CCR8, and also on activated human Tregs, cf. example 10.1.1. Out of the six CDR loops of an antibody, the H3 loop shows the greatest structural diversity and is located in the center of the binding site. It also gains the most mutations through affinity maturation and has on average the largest number of contacts with the antigen. It therefore plays a crucial role in antigen binding. Upon analysis of the specific structure of the antibodies obtained with the method according to the current invention, it was surprisingly found that the composition of the HCDR3 was structurally different from usual human HCDR3 domains, cf. example 9. In particular, the HCDR3 domains of the antibodies with the therapeutically most beneficial properties and specific binding to CCR8 were characterized by an average frequency of <com:Math><semantics>∼21<annotation encoding="application / x-tex">\sim 21< / annotation>< / semantics>< / com:Math> % tyrosine residues and an average histidine content of <com:Math><semantics>∼10<annotation encoding="application / x-tex">\sim 10< / annotation>< / semantics>< / com:Math> %, emphasizing a beneficial impact of these residues on the recognition of the specific sulfated antigen (cf. Table 9.2). Without being bound by theory, the inventors believe that these structural features translate into certain functional characteristics which make the obtained antibodies more suitable for therapeutic applications. For example, and in contrast to the tested prior art antibodies, several antibodies according to the invention block G protein dependent signaling, cf. example 10.4.3, but do not impact G protein independent pathways, cf. examples 10.4, 10.4.1, 10.4.2, and do not substantially internalize into cells with endogenous expression of the target chemokine receptor, cf. example 10.5. In addition, particularly preferred antibodies according to the current invention were specific for the target receptor and target cells, cf. example 10.2, 11, and are especially suitable / showed superior properties in methods of treatment for cancer, cf. examples 12 ff. Furthermore, use of these synthetic polypeptides either as antigens or for off target panning facilitated or enabled the generation of cross-reactive antibodies, such as antibodies specifically binding to human CCR8 and / or cynomolgus CCR8, cf. example 10.1.1. 1.2 Provision of therapeutic antibodies specifically binding chemokine receptors 1.2.1 Obtaining chemokine receptor antibodies with human CDRs While humanization of antibodies with murine CDRs may improve the immunogenicity of an antibody, residual immunogenicity resides in the CDR regions (Harding, Fiona A., et al. "The immunogenicity of humanized and fully human antibodies: residual immunogenicity resides in the CDR regions." MAbs. Vol. 2. No. 3. Taylor & Francis, 2010.). Antibodies comprising human CDRs are thus assumed to have a superior suitability as therapeutic agents for humans compared with antibodies comprising CDRs from other species. For example, antibodies with human CDRs can be produced via phage display technologies or using transgenic animals capable of generating fully human antibodies. However, it is not always trivial to obtain fully human antibodies. While, in theory, the diversity of HCDR3 regions is almost unlimited, in practice the generation of the antibody repertoire diversity appears to be carefully regulated by multiple mechanisms, which yield an in vivo repertoire that is restricted in its diversity and constrained in its range of antigen-binding sites. This is also the case for human phage display libraries, which are often designed to reflect the in vivo repertoire. Thus, in some cases, the structural requirements of a "complicated" antigen may be fulfilled by rodent CDRs, while the same structure cannot be readily recognized by human CDRs. Based on the observation that tyrosine representation is on average approximately 50 % lower in human HCDR3 than in murine HCDR3, it can be assumed that it is clearly more challenging to find a human anti-human antibody in cases, where the unique binding abilities of tyrosine and histidine are required to enable the target binding. Indeed, the inventors are not aware of fully human anti-human CCR8 prior art antibodies. According to the current invention there are provided CCR8 antibodies comprising human derived CDRs, and also fully human antibodies, cf. examples 6, 7, 8. 1.2.2 Obtaining cross reactive chemokine receptor antibodies Cross reactive anti-chemokine receptor antibodies such as cross reactive anti-CCR8 antibodies are advantageous for the development of a therapeutic antibody, because they can be used in non-human animal models to characterize the therapeutic agents with regards to pharmacological data and safety, before the antibodies are administered to humans. However, cross reactive antibodies e.g. with similar binding behavior in two species are difficult to generate and cannot be easily affinity maturated, e.g. because the extracellular parts of chemokine receptors such as CCR8 have a low homology between species (see example 2). According to the current invention, cross reactive antibodies for CCR8 can be generated in particular by using small sulfated tyrosine comprising motifs which have a higher conservation between species, such that cross reactive antibodies binding a chemokine receptor such as CCR8 from two or more species, e.g. with affinities in the same order of magnitude can be obtained in an easy and convenient way, cf. examples 6, 7, 10.1.1. 1.2.3 Obtaining chemokine receptor antibodies for therapy To induce the killing of cells expressing a target chemokine receptor or CCR8, multiple modes of action can be envisioned. One mode of action is the conjugation of an antibody targeting the chemokine receptor or CCR8 to a drug in the form of an antibody drug conjugate (ADC). Other possible modes of action are induction of antibody-dependent cellular cytotoxicity (ADCC), antibody-dependent cellular phagocytosis (ADCP) and / or complement-dependent cytotoxicity (CDC). For ADCC, CDC and ADCP, a two-step mechanism is involved: On the one hand, the antibody or fragment is required to effectively bind the target cell, e.g. the Treg via CCR8, on the other hand, the FC part of the antibody (or an alternative binding moiety which can be conjugated to the antibody or fragment as described elsewhere herein) has to bind to an effector cell, which will then mediate the killing of the target cell. For ADCP, binding to macrophages as effector cells typically occurs via the interaction of the antibodies FC part with FcγRIIa (CD32a) expressed by macrophages. In contrast, ADCC is mediated via interaction of the antibody or fragment with FcyRIIIa. In humans, FcyRIII exists in two different forms: FcyRIIIa (CD16a) and FcyRIIIb (CD16b). While FcyRIIIa is expressed on mast cells, macrophages, and natural killer cells as a transmembrane receptor, FcyRIIIb is only expressed on neutrophils. These receptors bind to the Fc portion of IgG antibodies, which then activates antibody-dependent cell-mediated cytotoxicity (ADCC) mediated by the human effector cells. 1.2.4 Obtaining low internalizing (including non-internalizing) chemokine receptor antibodies When the inventors analyzed known anti-human CCR8 prior art antibodies, they found that these antibodies readily internalized into a cell with endogenous target expression but did not reside on the cell surface for extended periods of time. The internalization behavior of an antibody does not only influence its clearance and pharmacological behavior but also its suitability for a specific mode of action for therapeutic uses. While high internalization is desirable for the generation of certain antibody drug conjugates, it is undesirable for ADCC induced depletion of tumor cells or Treg cells. In more detail, an antibody drug conjugate is required to transport the drug into the cell to achieve an efficient and specific depletion of the target cell. In contrast, the ADCC mode of action requires the exposure of the antibody and its Fc domain at the outside of the target cell, where the immune effector cells can bind the FC domain for the lysis of the target cell. A low or even absent internalization rate thereby increases the time of effect for an ADCC / ADCP inducing antibody. Upon characterization of the antibodies obtained with the novel method, the inventors surprisingly found, that several of the antibodies according to the current invention showed a particularly low or even absent internalization profile in cells with endogenous expression levels of CCR8, cf. example 10.5, while the prior art antibodies recognizing the same target had a higher internalization rate. For example, prior art antibodies 433H and L263G8 readily internalized into the targeted cell and did not reside on the cell surface for extended periods of time. Due to their low internalization properties, some of the antibodies according to the current invention are thus particularly useful in an ADCC, ADCP, CDC or a mixed approach, such as a combined ADCC / ADCP approach. Typically, the selection of a target is an important factor which strongly influences the internalization of an antibody into a cell. According to Islam SA et al, CCL1 ligand binding induces Ca2+ flux and rapid receptor internalization of CCR8 (Islam, Sabina A., et al. "Identification of human CCR8 as a CCL18 receptor CCR8 is a CCL18 receptor." The Journal of experimental medicine 210.10 (2013): 1889-1898.). The inventors found it surprising that the antibody itself was able to influence the internalization properties in such a substantial degree. However, when they characterized the ability of the inventive antibodies to modulate G protein independent signaling pathways of their target chemokine receptor, they found that all tested prior art antibodies not only blocked G protein dependent signaling, but also modulated G protein independent signaling, cf. examples 10.4 ff.. G protein independent signaling has been previously linked to internalization behavior, cf. Fox, James M., et al. "Structure / function relationships of CCR8 agonists and antagonists: Amino-terminal extension of CCL1 by a single amino acid generates a partial agonist." Journal of Biological Chemistry 281.48 (2006): 36652-36661. 1.2.5 Obtaining chemokine receptor antibodies modulating target receptor signaling There are multiple different ways how an antibody can modulate a chemokine receptor. For example, an antibody can a) block G-protein independent signaling, b) block G-protein dependent signaling, c) block G-protein dependent and G-protein independent signaling, d) increase G-protein independent signaling, e) increase G-protein dependent signaling, f) increase G-protein dependent and G-protein independent signaling. Without being bound by theory, the inventors hypothesize that the sulfated TRD of the respective chemokine receptor may be relevant for the ligand induced signaling of the chemokine receptor. Interestingly, most of the inventive antibodies efficiently blocked ligand induced G-protein dependent signaling but did not influence G protein independent signaling, cf. examples 10.4 ff. In contrast, all prior art antibodies likewise blocked ligand induced G-protein dependent signaling but agonized G-protein independent signaling. Without being bound by theory, these differences may contribute to the differences in internalization behavior. Avoiding induction of G protein independent signaling by a therapeutic antibody might also be advantageous, because unspecific signaling may result in uncontrollable downstream effects such as an increased cell proliferation, cf. Hutchings, Catherine J., et al. (2017); Webb, David R., et al. "Opportunities for functional selectivity in GPCR antibodies." Biochemical pharmacology 85.2 (2013): 147-152.; Fox, James M., et al. (2006). 1.2.6 Obtaining ADCC / ADCP inducing chemokine receptor antibodies The antibodies according to the current invention are characterized by a superior induction of ADCC and ADCP, as shown e.g. in example 10.3.3, 10.3.4. In some preferred embodiments, the antibodies were engineered by elimination of the fucose at N297 (afucosylation) to obtain the high ADCC rates, cf. examples 10.3.1. Interestingly, many of the inventive anti-CCR8 antibodies seemed to induce target cell depletion via a combined mode of action using both mechanisms, i.e. ADCC and ADCP. 1.3 Methods for treatment While it has been suggested by several research groups to use antibodies binding CCR8 in methods of treatment based on mechanistic insights, the way to the provision of antibodies with optimal therapeutic properties has been tedious. By providing a method for antibody generation according to the current invention, antibodies for chemokine receptors with superior therapeutic properties can now be easily obtained. According to the current invention, various sequence defined antibodies with favorable properties are disclosed, which can be used in a method of treatment, e.g. as part of a conjugate, in an ADCC based approach, in an ADCP based approach, in a CDC based approach, or in a mixed ADCC / ADCP based approach. Examples 12 ff. show remarkable efficacies in Treg depletion, Overall Response Rate and Tumor-to-Control ratio for surrogate antibodies generated with a method according to the current invention. 1.4 Combination treatment While remarkable response rates were obtained in monotherapy with the inventive anti-CCR8 antibodies, it was surprisingly found that the therapeutic benefit could be further increased by combining the antibodies with immune checkpoint inhibitors, with further targeted therapies, and even with unspecific chemotherapeutics or radiation therapy. These combination treatments were particularly beneficial in challenging tumor models. In particular, a specific combination treatment scheme was found effective, where the second therapeutic agent or therapy was administered only after the anti-CCR8 antibody had caused substantial Treg depletion (see examples 12.6 ff.). Furthermore, it was observed that even a single anti-CCR8 antibody treatment showed a substantial therapeutic effect (see example 12.4.2). 1.5 Stratification schemes and diagnostic methods When evaluating the responsiveness of different syngeneic mouse models to anti-CCR8 antibody treatment, the inventors could identify several mechanisms, biomarkers and biomarker combinations that were predictive for treatment efficacy and overall response. For example, it was surprisingly found that the degree of responsiveness to immune checkpoint inhibitors such as PD-1, PD-L1 or CTLA4 antibodies was also predictive for the response to anti-CCR8 antibody treatment. Because PD-L1 expression is sometimes used as a surrogate marker to predict the responsiveness for immune checkpoint inhibitors, the inventors evaluated if PD-L1 could also be used to predict the responsiveness for anti-CCR8 antibody treatment. This hypothesis could finally be confirmed by correlation data, see example 12.7.1. In a further attempt to identify those subjects that would most likely benefit from anti-CCR8 treatment, further marker genes, such as immune cell and Treg markers were evaluated as biomarkers (see examples 12.1.2., 12.7.2, 12.8). BRIEF DESCRIPTION OF THE DRAWINGS Fig. 1: Alignment of human CC chemokine receptors and CXC chemokine receptors. Fig. 2: a. Human CCR8, cynomolgus CCR8 and murine CCR8 sequences were retrieved from Uniprot and aligned with Clustal Omega. b. Schematic representation of CCR8 receptor structure which contains 7 transmembrane domains (black boxes), three extracellular loops (ECL), several disulfide bridges (SS), and an intracellular C-terminal part as well as the extracellular N-terminal domain composed of the "LID" domain and the tyrosine rich domain (TRD). Fig. 3: Evaluation of three prior art antibodies by FACS staining in CCR8 positive target cells. None of the shown prior art antibodies showed a shift in FACS staining compared with the isotype control. hAP- 0068 and MAB1429-100 were tested on 293T cells stably transfected with human CCR8 while MAB8324 was tested on BW5147.3 cells expressing murine CCR8. Fig. 4: Panning strategy for lead finding: Two major strategies for selections on sulfated peptides are depicted. In all strategies, prior to each round of selection a depletion step on a relevant or an irrelevant biotinylated protein was included. Fig. 5: Panning strategy to obtain anti-murine CCR8 antibodies: The main strategy for selection based on a mix of sulfated / non-sulfated peptides is depicted. Prior to each round of selection, a depletion step on a relevant biotinylated protein was performed. Fig. 6: FACS data of inventive antibodies binding to CHO cells expressing human CCR8. Fig. 7: FACS data of inventive antibodies binding to CHO cells expressing cynomolgus CCR8. Fig. 8: FACS data of candidates binding to activated human Tregs (donor 1). Right side: Percent of CCR8 expression determined using BioLegend Clone L263G8. Fig. 9: FACS data of inventive antibodies TPP-21181 and TPP-23411 binding to CHO cells expressing human CCR8. Fig. 10: FACS data of inventive antibodies TPP-21181 and TPP-23411 binding to CHO cells expressing cynomolgus CCR8. Fig. 11: Binding of TPP-21360, L263G8, and 433H to CHO cells expressing human CCR8. Fig. 12: Binding of TPP-21360, L263G8, and 433H to CHO cells expressing cynomolgus CCR8. Prior art antibodies showed only very low overall binding to cynomolgus CCR8 (low saturation). Nevertheless, EC50 values could be determined for each antibody. Fig. 13: Activated human Treg staining with inventive antibody TPP-23411, gating strategy. CD4+ and CD25+ sorted cells from peripheral blood mononuclear cells (PBMC) were activated with anti-CD3 and anti-CD28 beads (Treg expansion kit, Miltenyi). Middle pane: Cells that are CD4+ CD25+CD127low and Foxp3+. Lower panel: CCR8 expression on Tregs after staining with TPP-23411 or L263G8. Fig. 14: Binding of TPP-21360 to CHO cells with mock transfectants. No unspecific binding was observed. Fig. 15: Off target binding in HEK cells transiently transfected with human CCR1. Most inventive candidates showed only low off target binding for CCR1. Fig. 16: Off target binding in HEK cells transiently transfected with human CCR4. Most inventive candidates showed only low off target binding for CCR4. Figure 17: Staining for CCR8 expression on different immune cell populations from healthy donor PBMCs (CD4+ T cells, CD8+ T cells, B cells as marked by CD19+ expression, Myeloid cells as marked by CD11b+ expression, CD4 T cells activated with anti-CD3 and anti-CD28 beads for 4 days, CD8+ T cells activated with anti-CD3 and anti-CD28 beads for 4 days). Figure 18: CCR8 is upregulated on human Tregs after activation. After activation, the percentage of CCR8+ cells increased significantly in CD4+CD25+ purified cells with increased MFI while % of CCR8+ cells increased slightly in PBMC population. Anti-CCR8 antibody from BioLegend was used for these experiments. N=4 donors. Fig. 19: ADCC induced by wild type or afucosylated inventive antibodies TPP-19546, TPP-21360 or TPP-23411 in HEK cells expressing human CCR8 as target cells. Isotype control: TPP-9808. Fig. 20: Left: Percent CCR8+ expression on day 3 for activated human Tregs as target cells. Right: ADCC induced by wild type or afucosylated inventive antibody TPP-21360, TPP-23411 in activated human Tregs as target cells. Isotype control: TPP-9808. Results were reproducible in different donors (data not shown). Fig. 21: Protocol for ADCP assay. Fig. 22: ADCP assay for wild type and afucosylated versions of inventive antibodies shows induction of phagocytosis in HEK cells expressing human CCR8 as target cells with in vitro differentiated M2c macrophages as effector cells. Wild type and afucosylated versions of inventive antibodies TPP-19546, TPP-21360 and TPP-23411 induced ADCP. TPP-9808 is the isotype control. Mogamulizumab is a marketed anti-CCR4 antibody. Fig. 23: ADCP assay for wild type and afucosylated versions of inventive antibodies TPP-21360, and TPP-23411 shows induction of phagocytosis in activated human Tregs from two different donors as target cells (upper or lower panel) and M2c macrophages as effector cells. TPP-9808 is the isotype control. Fig. 24: ADCP assay for wild type and afucosylated versions of inventive antibodies TPP-21360, and TPP-23411 shows induction of phagocytosis in activated human Tregs as target cells and M1 macrophages as effector cells. Fig. 25: Activation of β-arrestin signaling measured with the DiscoverX assay for CCL1, TPP-23411, L263G8, or 433H on CHO cells co-expressing human CCR8 tagged with ProLink and EA. As expected, CCR8 ligand CCL1 (human) induces β-arrestin signaling. An extra timepoint was analyzed for TPP-23411 to ensure that no <com:Math><semantics>β<annotation encoding="application / x-tex">\beta< / annotation>< / semantics>< / com:Math>-arrestin activation happened at earlier time points. None of the analyzed antibodies induced <com:Math><semantics>β<annotation encoding="application / x-tex">\beta< / annotation>< / semantics>< / com:Math>-arrestin signaling activation. Fig. 26: Evaluation of blocking of CCL1 induced β-arrestin signaling by TP-23411, L263G8, or 433H, measured with the DiscoverX assay. CCL1 was used at its EC80 (20ng / ml). Prior art antibodies L263G8, and 433H both blocked β-arrestin signaling induced by CCL1 at low antibody concentration, while inventive antibody TPP-23411 showed no effect at these concentrations. β-arrestin signaling has been suggested to play a role in internalization. Fig. 27: Phospho Erk 1 / 2 ELISA assay. CHO cells expressing human CCR8 were treated with CCL1, TPP- 23411, Biolegend L263G8 or BD antibody 433H and cell lysates were collected at the respective time point. Fig. 28: Phospho Erk 1 / 2 ELISA assay. Activated human Treg cells expressing CCR8 were treated with CCL1, TPP-23411, Biolegend L263G8 or BD antibody 433H, and cell lysates were collected at the respective time point. Prior art antibodies Biolegend L263G8 and BD antibody 433H both induced a significant increase of phosphorylated Erk 1 / 2 levels, e.g. after 15 minutes in activated human Tregs, while this was not the case for inventive antibody. Fig. 29: Phospho AKT ELISA assay. CHO cells expressing human CCR8 were treated with CCL1, TPP- 23411, Biolegend L263G8 or BD antibody 433H and cell lysates were collected at the respective time point. Fig. 30: Phospho AKT ELISA assay. Activated human Treg cells expressing CCR8 were treated with CCL1, TPP-23411, Biolegend L263G8 or BD antibody 433H, and cell lysates were collected at the respective time point. Prior art antibodies Biolegend L263G8 and BD 433H both induced a significant increase of phospho AKT levels in activated human Tregs, e.g. after 15 minutes, while this was not the case for inventive antibodies. Fig. 31: Internalization studies. a. FACS analysis of commercial anti-human CCR8 antibodies Biolegend L263G8 or BD antibody 433H with endogenously CCR8-expressing cell line HuT78. b. Internalization studies of commercial anti-human CCR8 antibodies with endogenously CCR8-expressing cell line HuT78 based on cytoplasmic-intensity spots. TPP-5657: Isotype control. Fig. 32: Internalization studies. a. FACS analysis of commercial anti-murine CCR8 antibody SA214G2 with murine endogenously CCR8-expressing cell line BW5147.3. b. Internalization study of commercial anti-murine CCR8 antibody SA214G2 with murine endogenously CCR8-expressing cell line BW5147.3. The anti-murine CCR8 prior art antibody SA214G2 elicits internalization. Fig. 33: Internalization study of inventive anti-human CCR8 antibodies TPP-21360 and TPP-23411 with endogenously CCR8-expressing cell lines TALL-1 (a) and HuT78 (b). Both antibodies reveal identical internalization behavior, comparable with the isotype control TPP-5657. Fig. 34: FACS analysis of inventive anti-human CCR8 antibodies TPP-21360 and TPP-23411 with endogenously CCR8-expressing cell lines TALL-1 (a) and HuT78 (b). Both antibodies reveal same binding potency to the cell lines. Fig. 35: CCR8 mRNA expression across 11642 samples representing a comprehensive set of human tissues and cell types as measured by affymetrix probe 208059 at. All samples were co-normalized using the refRMA method (Katz, Simon, et al. "A summarization approach for Affymetrix GeneChip data using a reference training set from a large, biologically diverse database." BMC bioinformatics 7.1 (2006): 1- 11.). Dark grey box coloring indicates that the median sample in the corresponding group has a probe signal intensity significantly above background noise (as estimated by affymetrix' MAS5 algorithm, cf. Pepper, Stuart D., et al. "The utility of MAS5 expression summary and detection call algorithms." BMC bioinformatics 8.1 (2007): 1-12.). Median CCR8 expression significantly above background noise is only observed in activated regulatory T cells as well as tumor infiltrating lymphocytes. Groups are sorted based on decreasing mean expression. Fig. 36: CCR8 mRNA expression, as measured by RNA-seq, across 50 different TCGA (https: / / www.cancer.gov / tcga) tumor indications (dark grey boxes), corresponding normal tissues (white boxes), as well as across the CCLE tumor cell line panel (Barretina, Jordi, et al. "The Cancer Cell Line Encyclopedia enables predictive modelling of anticancer drug sensitivity." Nature 483.7391 (2012): 603- 607.) also grouped by tumor indications (light grey boxes). Groups are sorted based on mean expression. Indications with highest CCR8 expression are breast cancer, lung adenocarcinoma (ADC) and squamous cell carcinoma (SCC), head and neck malignancies, as well as esophageal tumors. In all indications except pancreatic adenocarcinoma and melanoma, expression appears higher in the tumor compared to the corresponding normal tissue. Little to no expression is observed in corresponding tumor cell lines of epithelial origin indicating that CCR8 is not expressed by tumor cells but exclusively by tumor infiltrating T cells. In principle, each tumor indication with CCR8+ Treg cell infiltration is supposed to be eligible for anti-CCR8 antibody treatment. Fig. 37: Immunohistochemistry with staining of Treg markers FOXP3 and CCR8 (clone 433H) in human Non-small-cell lung cancer tissue (NSCLC) or human melanoma tissue. Fig. 38: Staining of FACS sorted T cell populations based on CCR4, CCR8, OX40, GITR, and CD25. Only CCR8 is specific for activated Tregs. OX40, GITR, and CD25 are significantly expressed on stimulated CD8+ Teff cells and CD4+ T cells (CD4+CD25+Foxp3-). Dark grey: isotype control, light grey: target staining. Fig. 39: Expression of CCR8 across different T cell subsets extracted from different tumor entities as measured by single cell RNA-seq. For these tumors, CCR8 mRNA expression is largely restricted to regulatory T cells (light grey boxes) residing in tumor tissue while largely being absent in regulatory T cells from normal tissues as well as from CD4 helper T and CD8 cytotoxic T cells (medium and dark gray boxes, respectively). Upper panel: Colorectal tumor tissue (Tumor) or adjacent normal tissue (Normal). Middle panel: Liver cancer tissue (Tumor) or adjacent normal tissue (Normal). Lower panel: Lung cancer tissue (Tumor) or adjacent normal lung tissue and peripheral blood (Normal). Sample sizes, N, indicate the number of cells in each category. Cells were designated as regulatory T cells, T helper cells, or cytotoxic T cells based on expression of marker genes FOXP3, CD4 (but no FOXP3), and CD8A / B, respectively. Fig. 40: Treg, macrophage, T cell or tumor cell populations from NSCLC, CRC (colorectal cancer) or RCC (renal carcinoma) were stained with anti-CCR8 antibody or isotype control and were analyzed by flow cytometry. X axis: Log shift up to 10<com:Sup>5< / com:Sup>; Y axis: Intensity normalized to mode. Lighter grey: isotype control. Darker grey: CCR8. Specific CCR8 expression on intra-tumoral human Tregs is indicated by arrows. Fig. 41: CT26 tumor growth after treatment with different doses of anti-CCR8 antibodies or anti-PDL1 antibody. Fig. 42: Spider plots of CT26 tumor bearing mice after treatment with different doses of anti-CCR8 antibodies, anti-PDL1 antibody or isotype controls. Fig. 43: FACS analysis of intra-tumoral immune cells 24 hours after second antibody treatment. Analysis of intra-tumoral Tregs. Anti-CCR8 antibody TPP15285 leads to an average decrease of intra-tumoral Tregs to 13 %, 33 %, or 47 % of the Tregs in the isotype control, for 10 mg / kg, 1 mg / kg or 0.1 mg / kg, respectively. Anti-CCR8 antibody TPP15286 leads to an average decrease of intra-tumoral Tregs to 10 %, 9 % or 14 % of the Tregs in the isotype control, for 10 mg / kg, 1 mg / kg or 0.1 mg / kg, respectively, cf. Table 12.2.1. Analysis of intra-tumoral CD8+ T cells. Mean increase in % of isotype control is shown in Table 12.2.1. Analysis of ratio of CD8+ T cells to Treg cells. Anti-CCR8 antibody TPP15286 leads to an average increase of the CD8+ cell to Treg cell ratio of 44 (10 mg / kg), 87 (1 mg / kg) or 68 (0.1 mg / kg). Anti-CCR8 antibody TPP15285 leads to an average increase of the CD8+ cell to Treg cell ratio of 64 (10 mg / kg), 16 (1 mg / kg) or 10 (0.1 mg / kg). Analysis of ratio of CD4+ conv T cells to Treg cells. Fig. 44: CT26 tumor growth after treatment with glycosylated (TPP-14095, TPP-14099, TPP-15285, TPP- 15286) or aglycosylated (TPP-18208, TPP-18209) anti-CCR8 antibodies. Aglycosylation largely abolished the anti-tumor effect. Fig. 45: Spider plots of CT26 tumor bearing mice after treatment with glycosylated (TPP-14095, TPP- 14099, TPP-15285, TPP-15286) or aglycosylated (TPP-18208, TPP-18209) anti-CCR8 antibodies. Aglycosylation largely abolished the anti-tumor effect, suggesting an ADCC / ADCP dependent mechanism of anti-tumor efficacy. Fig. 46: FACS analysis of immune cells 24 hours after second antibody treatment. Absolute numbers of intra-tumoral CD45+ cells. Absolute numbers of intra-tumoral CD45+CD8+ T cells. Absolute numbers of intra-tumoral CD8+ T cells. Absolute numbers of intra-tumoral CD4+ conv cells. Analysis of intra- tumoral Treg depletion by flow cytometry showing absolute cell numbers. Average percentage of residual Tregs relative to the respective isotype control after antibody administration was 15.6 % for TPP-14095, 28.2 % for TPP-14099, 8.7 % for TPP-15285 and 36.5 % for TPP-15286. For the aglycosylated antibodies no reduction in Tregs was observed. % CD8+ T cells of intra-tumoral CD45+ cells. CD8+ T cells: Treg ratio. CD4+ conv: Treg ratio. Percentage Treg cells of CD4+ T cells. Absolute numbers of intra-tumoral 4-1BB+ Treg cells. Absolute numbers of intra-tumoral 4-1BB+ CD4+ conv cells. Fig. 47: EMT6 tumor growth after treatment with different doses of anti-CCR8 antibody TPP-15285. Significance was determined by 1-Way ANOVA plus Sidak's post-test after log transform. Fig. 48: EMT6 tumor growth at day 19 after treatment with different doses of anti-CCR8 antibody TPP- 15285 or anti-CTLA4 antibody. Fig. 49: Spider plots of EMT6-tumor bearing mice after treatment with different doses of anti-CCR8 antibody TPP-15285 or anti-CTLA4 antibody. Fig. 50: FACS analysis of immune cells of EMT6-tumor bearing mice after treatment with different doses of CCR8-antibody TPP-15285 or anti-CTLA4 antibody, 24 hours after second treatment or at the end of the study. Absolute numbers of intra-tumoral Treg cells. Significant differences were observed e.g. for 10 mg / kg of anti-CCR8 antibody at both timepoints. CD8 positive cells to Treg ratio. CD4+ conv cells to Treg ratio. Percentage Treg cells of CD4+ T cells. Fig. 51: FACS analysis of immune cells of EMT6-tumor bearing mice after treatment with different doses of anti-CCR8 antibody TPP-15285 or anti-CTLA4 antibody, 24 hours after second treatment or at the end of the study. Absolute numbers of intra-tumoral CD45+ cells. Absolute numbers of intra-tumoral CD4+ conv cells. Absolute numbers of intra-tumoral CD4+ T cells. Absolute numbers of intra-tumoral activated CD8+ T cells. Absolute numbers of intra-tumoral NK cells. Absolute numbers of intra-tumoral CD8+ T cells. Differences were observed e.g. for 10 mg / kg of anti-CCR8 antibody at the end of the study. Fig. 52: F9 tumor growth after treatment with different doses of anti-CCR8 antibody TPP-15285 or anti- PDL1 antibody. Fig. 53: F9 tumor volume at day 16 after treatment start with different doses of anti-CCR8 antibody TPP- 15285 or anti-PDL1 antibody. Significant improvement was observed at least for an antibody dose of 10 mg / kg. Fig. 54: Spider plots of F9 tumor bearing mice after treatment with different doses of anti-CCR8 antibodies or anti-PDL1 antibody. Fig. 55: Effects of anti-CCR8 antibodies or anti-PDL1 antibody on immune cell populations and their ratios in F9 tumors analyzed by FACS 24 hours after second antibody treatment. Anti-CCR8 antibody increased absolute numbers of intra-tumoral CD45+ T cells, intra-tumoral CD4+ T cells, intra-tumoral CD8+ T cells, intra-tumoral CD4+conv T cells and intra-tumoral NK cells compared with the matched isotype control. Anti-CCR8 antibody at 10 mg / kg decreased absolute numbers of intra-tumoral Treg cells <com:Math><semantics>(CD4+,CD25+,FoxP3+).<annotation encoding="application / x-tex">(CD4+, CD25+, FoxP3+).< / annotation>< / semantics>< / com:Math> Fig. 56: Effects of anti-CCR8 antibodies or anti-PDL1 antibody on immune cell populations and their ratios in F9 tumors analyzed by FACS 24 hours after second treatment plotted as CD8+ T cell to Treg ratio, frequency of Treg to CD4+ T cells, frequency of 4-1BB+ cells of CD8+ T cells, frequency of 4- 1BB+ cells of Tregs and frequency of 4-1BB+ cells of conventional CD4+ T cells. At 10 mg / kg anti- CCR8 antibody increased the CD8+ cell to Treg cell ratio to approximately 54 or higher, cf. Table 12.5.1. Fig. 57: Efficacy of combination treatments in C38 tumor bearing mice. a. C38 tumor growth after treatment with anti-CCR8 surrogate antibodies TPP-14099 or TPP-15285 or anti-PD-L1 antibody or after combination treatment with 3 mg / kg anti-PDL1 antibody, 10 mg / kg TPP-15285. Significance as determined by 1-Way ANOVA plus Sidak's post-test after log transform. b. Survival plot of C38-tumor bearing mice after treatment with anti-murine CCR8 antibody TPP-15285 (10 mg / kg), anti-murine PD- L1 antibody (PDL1, 3 mg / kg) or a combination of TPP-15285 (10 mg / kg) and anti-murine PD-1 antibody <com:Math><semantics>(3 mg / kg).<annotation encoding="application / x-tex">(3 \text{ mg / kg}).< / annotation>< / semantics>< / com:Math> Fig. 58: Analysis of tumoral Treg depletion in C38 tumors by flow cytometry (sampling 24 hours after second antibody treatment). C38 tumor bearing mice were treated with anti-CCR8 surrogate antibodies TPP-14099 or TPP-15285 or anti-PD-L1 antibody in monotherapy, or with TPP-15285 in combination with anti-PD-L1 antibody. Absolute Treg depletion. CD8+ T cell / Treg cell ratios. Fig. 59: CD11+ F4 / 80+ macrophages in C38 tumors as analyzed by flow cytometry (sampling at study end). Fig. 60: B16F10-OVA tumor growth after treatment with TPP-15285, anti-CTLA4 antibody or both. Fig. 61: EMT-6 tumor growth after treatment with anti-murine CCR8 antibody TPP-15285 (1 mg / kg), anti-murine PD-1 antibody (CDRs: atezolizumab, 10 mg / kg) or a combination of TPP-15285 (1 mg / kg) and anti-murine PD-1 antibody (10 mg / kg), (twice weekly i.p.). Mean with standard deviation. Fig. 62: FACS analysis of immune cell populations in EMT-6-tumors analyzed by flow cytometry, sampling 24 hours after second antibody treatment. CD4+ T cells, Tregs, CD8+ T cells, NK cells, Ratios of CD8+ T cells to Tregs. Box and whiskers, min to max with median (GraphPad). Fig. 63: a. Analysis of C38 tumor bearing mice after treatment with anti-murine CCR8 antibody TPP- 15285 (5 mg / kg), anti-murine PD-1 antibody (CDRs: atezolizumab, 5 mg / kg) or a combination of TPP- 15285 (5 mg / kg) and anti-murine PD-1 antibody (5 mg / kg), (each twice weekly i.p.). a. Tumor volume. Mean with standard deviation. b. Survival plot. Fig. 64: Analysis of tumoral CD4+ T cells, Tregs, CD8+ T cells, NK cells or ratios of CD8+ T cells to Tregs in C38-tumors by flow cytometry (sampling 24 hours after second antibody treatment). Fig. 65: MB49 tumor growth after treatment with anti-CCR8 antibody TPP-15285 (10 mg / kg) alone, anti- PD-1 antibody (aPD-1, CDRs: atezolizumab, 10 mg / kg) alone or sequential combination treatment of TPP-15285 (10 mg / kg) and anti-PD-1 antibody (10 mg / kg) (both twice weekly i.p.). Fig. 66: Analysis of tumoral CD45+ cells, Tregs, CD8+ T cells, NK cells and ratio of CD8 to Tregs in MB49-tumors by flow cytometry (sampling at study end). Fig. 67: EMT-6 tumor growth after treatment with anti-CCR8 antibody TPP-15285 (5 mg / kg, q3 / 4d i.p.), Oxaliplatin (5 mg / kg, q4d i.p.), Doxorubicin (6 mg / kg, i.v. SD), Docetaxel (10 mg / kg, q2dx5, i.v.) or a combination of TPP-15285 with either Oxaliplatin, Doxorubicin or Docetaxel. Fig. 68: MB49 tumor growth after treatment with anti-CCR8 antibody TPP-15285, gemcitabine or a combination of TPP-15285 with gemcitabine. Fig. 69: Lewis lung tumor growth after treatment with anti-CCR8 antibody TPP-15285 (10 mg / kg) alone, anti-PD-1 antibody (aPD-1, CDRs: atezolizumab, 10 mg / kg) alone, anti-PD-L1 antibody (10 mg / kg) alone, anti-CTLA4 antibody alone, TPP-15285 (10 mg / kg) and anti-murine PD-1 antibody (10 mg / kg) in combination, or TPP-15285 (10 mg / kg) and anti-PD-L1 antibody (10 mg / kg) in combination. Fig. 70: EMT-6 tumor growth after treatment with anti-CCR8 antibody TPP-15285 (3 mg / kg) or radiotherapy (RT, 3 x 2 Gy) alone or in combination. Significance was determined by 1-Way ANOVA plus Sidak's post-test after log transform. Fig. 71: mRNA expression levels of different immune cell markers in different syngeneic tumor models treated with either isotype control (TPP-9809) or anti-CCR8 antibody (TPP-14099). Median expression in the isotype treated control groups is set to zero. Gene expression is measured in transcripts per million (TPM) as estimated by the RSEM algorithm. Treg marker Foxp3. Significantly higher Foxp3 levels are observed in the CT26, H22, Hepa1-6, and RM1 models treated with TPP-14099, indicating increased Treg infiltration, after administration of at least three doses of TPP-14099. Fig. 72: Inflammation marker lfng. Signficantly higher lfng levels are observed in the H22, CT26, and RM1 models treated with TPP-14099 pointing towards a strong pro inflammatory activity induced by TPP-14099. Fig. 73: Macrophage marker Ms4a7. Significantly higher Ms4a7 levels are observed in the CT26, H22, and Hepa1-6 models treated with TPP-14099, indicating increased infiltration of macrophages caused by TPP-14099. Fig. 74: Cytotoxic T cell markers Cd8a and Cd8b1. Significantly higher cytotoxic T cell levels are observed in the CT26, H22, RM1, and Hepa1-6 models treated with TPP-14099 indicating the induction of cytotoxic T cell infiltration and / or proliferation by TPP-14099. Fig. 75: Natural killer (NK) cell marker Ncr1. Significantly higher NK cell levels are observed in the CT26, H22, and Hepa1-6 models treated with TPP-14099. Fig. 76: Pan T cell markers Cd3e / d / g. Significantly higher T cell levels are observed in the CT26, H22, and Hepa1-6 models treated with TPP-14099. Fig. 77: Activated Treg marker and antibody target Ccr8. Significantly higher Ccr8 levels are observed in the CT26, H22, and Hepa1-6 models treated with TPP-14099. Fig. 78: Highly specific pro-inflammatory M1 macrophage marker Acod1 (a) and highly specific anti- inflammatory M2 macrophage marker Mrc1 (b). Markedly higher M1 macrophage levels are observed in the CT26, 4T1, H22, Hepa1-6, and RM1 models treated with TPP-14099, while no markedly higher M2 macrophage levels are observed across all models treated with TPP-14099. Fig. 79: Ratio of highly specific pro-inflammatory M1 macrophage marker Acod1 and highly specific anti-inflammatory M2 macrophage marker Mrc1. Taken together, multiple doses of anti-CCR8 antibody TPP-14099 increased the M1 / M2 macrophage ratio in these tumor models. Fig. 80: B cell markers Cd19 and Cd22. Markedly higher B cell levels are observed in the CT26, H22, RM1, and Hepa1-6 models treated with TPP-14099. Anti-CCR8 antibody seems to recruit B cells to the tumor. Without being bound by theory, recruitment of B cells may affect the anti-tumor response elicited by TPP-14099. Fig. 81: Expression levels for LTta / b as well as Cxcr5 and its ligand Cxcl13. These markers are crucial for the development of lymph nodes as well as tertiary lymphoid structures (cf. Cyster, Jason G. "Blown away: the unexpected role of lymphotoxin in lymphoid organ development." The Journal of Immunology 192.5 (2014): 2007-2009., and Cupedo, Tom, et al. "Induction of secondary and tertiary lymphoid structures in the skin." Immunity 21.5 (2004): 655-667.) which are key drivers of an anti-tumor effect in humans (cf. Dieu-Nosjean, Marie-Caroline, et al. "Tertiary lymphoid structures, drivers of the anti-tumor responses in human cancers." Immunological reviews 271.1 (2016): 260-275.). Fig. 82: Spider plots of tumor growth (measured in mm<com:Sup>3< / com:Sup>) over time in the TPP-14099 treatment group (shown as triangles) and isotype control treated group (shown as circles) for different tumor models. Levels of T cell infiltration at the end of the study, as judged by Cd8a mRNA levels in corresponding bulk tumor samples, are indicated by grey shades (black and light grey correspond to highest and lowest Cd8a levels, respectively). In H22 and CT26, tumor size showed an excellent anti-correlation with Cd8a levels. Fig. 83: Correlation between infiltration of the tumor by different immune cell populations as judged by mRNA levels of different immune cell markers and tumor size. TPP-14099 treated tumors are shown as triangles and isotype treated tumors are shown as circles. Tumor size is measured in mm<com:Sup>3< / com:Sup>. Strong negative correlation between cytotoxic T cell infiltration (as judged by Cd8a+Cd8b1 mRNA levels) and CT26 tumor sizes. TPP-14099 treated tumors are smaller in size and show higher Cd8a+Cd8b1 T cell infiltration levels than controls, indicating that increased T cell infiltration upon TPP-14099 treatment causes reduced tumor growth. Strong negative correlation between T cell infiltration (as measured by Cd3 mRNA levels) and CT26 tumor sizes in the TPP-14099 treated tumors. TPP-14099 treated tumors are smaller in size and show higher T cell infiltration levels, i.e. the higher the level of Cd3 mRNA the smaller the tumors. Negative correlation between NK cell infiltration (as judged by NK marker Ncr1 expression) and CT26 tumor sizes. TPP-14099 treated tumors are smaller in size and show higher NK cell infiltration. Tumor size is strongly negatively correlated with NK infiltration, the higher the level of NK, the smaller the tumors. Correlation between postulated induction of tertiary lymphoid structures as judged by Lta / Ltb / Cxcr5 and Cxcl13 mRNA levels and CT26 tumor sizes in the TPP-14099 treated tumors. For each of the four markers, the level is strongly increased after TPP-14099 treatment, and tumor size is strongly negatively correlated with the expression level, indicating that increased formation of tertiary lymphoid structures upon TPP-14099 treatment causes reduced tumor growth. Fig. 84: Correlation between Cd8a infiltration levels, as judged by Cd8a mRNA expression, and tumor sizes in the TPP-14099 treated tumors (shown as triangles) and in the isotype treated control group (shown as circles) for different tumor models. TPP-14099 treated tumors are smaller in size and show higher Cd8a infiltration levels. Tumor size is strongly negatively correlated with Cd8a infiltration, the higher the level of Cd8a, the smaller the tumors. Fig. 85: Efficacy of CCR8-antibody TPP-15285 in EMT6-tumor bearing mice treated with four different treatment schemes: single treatment, two times BIW treatment, three times BIW treatment, or four times BIW treatment. Each group was treated with vehicle control or 0.1 mg / kg, 1 mg / kg, or 5 mg / kg of TPP- 15285. Fig. 86: Therapeutic efficacies of inventive anti-CCR8 antibody, anti-PD-1 antibody, anti-PD-L1 antibody, or Paclitaxel tested alone or in combination in MBT2 syngeneic tumor bearing mice as shown in Table 12.6.9.1. Fig. 87: Therapeutic efficacy of inventive anti-CCR8 antibody after quantitative depletion of CD8a+ expression in diphtheria toxin treated DTR mice. Depleting Cd8+ T cells abrogates anti-tumor growth effect of TPP15825 (cf. group 02b vs group 01b). Fig. 88: Therapeutic efficacy of inventive anti-CCR8 antibody after quantitative depletion of CD19+ expression in diphtheria toxin treated DTR mice. Depleting Cd19+ B cells enhances the anti-tumor growth effect of TPP15825 (cf. group 02b vs group 01b). Fig. 89: Internalization curves for various inventive anti-CCR8 antibodies in HUVEC cells. An anti-CD71 antibody with known internalization profile was used as positive control. Corresponding data are shown in Table 10.5.2. None of the antibodies obtained with a method according to the current invention showed substantial internalization, making them particularly useful for ADCC / ADCP based approaches. BRIEF DESCRIPTION OF THE SEQUENCE IDS The sequence listing provided with the application via electronic filing is included herein in its entirety. SEQ ID NO:1 to SEQ ID NO:108 and SEQ ID NO:157 to SEQ ID NO:168 relate to isolated polypeptides which can be used as antigens or for off target panning. SEQ ID NO:109 to SEQ ID NO:156 relate to chemokine receptor proteins from different species. SEQ ID NO:201 to SEQ ID NO:965 relate to inventive antibodies. The column on sulfations is provided for convenience only and is not intended to restrict the respective sequence in any way. [Image disponible dans le document PDF, Image available in the PDF document] [Image disponible dans le document PDF, Image available in the PDF document] [Image disponible dans le document PDF, Image available in the PDF document] [Image disponible dans le document PDF, Image available in the PDF document] [Image disponible dans le document PDF, Image available in the PDF document] [Image disponible dans le document PDF, Image available in the PDF document] [Image disponible dans le document PDF, Image available in the PDF document] [Image disponible dans le document PDF, Image available in the PDF document] [Image disponible dans le document PDF, Image available in the PDF document] [Image disponible dans le document PDF, Image available in the PDF document] [Image disponible dans le document PDF, Image available in the PDF document] [Image disponible dans le document PDF, Image available in the PDF document] [Image disponible dans le document PDF, Image available in the PDF document] [Image disponible dans le document PDF, Image available in the PDF document] [Image disponible dans le document PDF, Image available in the PDF document] [Image disponible dans le document PDF, Image available in the PDF document] [Image disponible dans le document PDF, Image available in the PDF document] [Image disponible dans le document PDF, Image available in the PDF document] [Image disponible dans le document PDF, Image available in the PDF document] [Image disponible dans le document PDF, Image available in the PDF document] [Image disponible dans le document PDF, Image available in the PDF document] DEFINITIONS Unless otherwise defined, all scientific and technical terms used in the description, figures and claims have their ordinary meaning as commonly understood by one of ordinary skill in the art. In case of conflict, the present specification, including definitions, will prevail. If two or more documents referenced include conflicting and / or inconsistent disclosure with respect to each other, then the document having the later effective date shall control. Where reference to a database is made, the effective data shall be the version number applicable 26.05.2021, if not indicated otherwise. The materials, methods, and examples are illustrative only and are not intended to be limiting. Unless stated otherwise, the following terms used in this document, including the description and claims, have the definitions given below. The expression "about" or "~" as used herein refers to a value being within an acceptable error range for the particular value as determined by one of ordinary skill in the art, which will depend in part on how the value is measured or determined, i.e., on the limitations of the measurement system. For example, "about" can mean within 1 or more than 1 standard deviation, per the practice in the art. The term "about" is also used to indicate that the amount or value in question may be the value designated or some other value that is approximately the same. The phrase is intended to convey that similar values promote equivalent results or effects as described herein. In this context "about" may refer to a range above and / or below of up to 10 %. Wherever the term "about" is specified for a certain assay or embodiment, that definition prevails for the particular context. The terms "comprising", "including", "containing", "having" etc. shall be read expansively or open- ended and without limitation. The term comprising when used in the specification includes "consisting" of”. Singular forms such as "a", "an" or "the" include plural references unless the context clearly indicates otherwise. Thus, for example, reference to "a monoclonal antibody" includes a single monoclonal antibody as well as a plurality of monoclonal antibodies, either the same or different. Likewise reference to "cell" includes a single cell as well as a plurality of cells. Unless otherwise indicated, the term "at least" preceding a series of elements is to be understood to refer to every element in the series. The terms "at least one" and "at least one of" include for example, one, two, three, four, five or more elements. It is furthermore understood that slight variations above and below a stated range can be used to achieve substantially the same results as a value within the range. Also, unless indicated otherwise, the disclosure of ranges is intended as a continuous range including every value between the minimum and maximum values. The term "amino acid" or "amino acid residue" as used herein typically refers to a naturally-occuring amino acid. The one letter code is used herein to refer to the respective amino acid. As used herein, a "charged amino acid" is an amino acid which is negatively charged or positively charged. "Negatively charged amino acids" are aspartic acid (D) and glutamic acid (E). "Positively charged amino acids" are arginine (R) lysine (K) and histidine (H). "Polar amino acids" are all amino acids that form hydrogen bonds as donors or acceptors. These are all charged amino acids and asparagine (N), glutamine (Q), serine (S), threonine (T), tyrosine (Y) and cysteine (C). "Polar uncharged amino acids" are asparagine (N), glutamine (Q), serine (S), threonine (T), tyrosine (Y) and cysteine (C). "Amphiphatic amino acids" are tryptophan (W), tyrosine (Y) and methionine (M). "Aromatic amino acids" are phenylalanine (F), tyrosine (Y), and tryptophan (W). "Hydrophobic amino acids" are glycine (G), alanine (A), valine (V), leucine (L), isoleucine (I), proline (P), phenylalanine (F), methionine (M) and cysteine. "Small amino acids" are glycine (G), alanine (A), serine (S), proline (P), threonine (T), aspartic acid (D) and asparagine (N). As used herein, the terms "peptide", "polypeptide", and "protein" are used interchangeably, and refer to a compound comprised of amino acid residues covalently linked by peptide bonds. A protein or peptide must contain at least two amino acids, and no limitation is placed on the maximum number of amino acids. Polypeptides include any peptide or protein comprising two or more amino acids joined to each other by peptide bonds. As used herein, the term refers to both short chains, which also commonly are referred to in the art as peptides, oligopeptides and oligomers, for example, and to longer chains, which generally are referred to in the art as proteins, of which there are many types. "Polypeptides" include, for example, biologically active fragments, substantially homologous polypeptides, oligopeptides, homodimers, heterodimers, variants of polypeptides, modified polypeptides, derivatives, analogs, fusion proteins, among others. The polypeptides include natural peptides, recombinant peptides, synthetic peptides, or a combination thereof. Where generic reference is made to a gene or protein from a certain species such as mouse, the analogue from human shall likewise be meant, if not stated otherwise or obviously incompatible. This holds in particular in the context of biomarkers. The term "isolated" when applied to a nucleic acid, polypeptide, protein or antibody, denotes that the nucleic acid, polypeptide, protein or antibody is essentially free of other cellular components with which it is associated in the natural state. It is preferably in a homogeneous state. It can be in either a dry or aqueous solution. Purity and homogeneity are typically determined using analytical chemistry techniques such as polyacrylamide gel electrophoresis or high-performance liquid chromatography. A protein, polypeptide or antibody that is the predominant species present in a preparation is substantially purified. In particular, an isolated gene is separated from open reading frames that flank the gene and encode a protein other than the gene of interest. An isolated polypeptide may however be immobilized, e.g. on beads or particles, e.g. via a suitable linker. The term "purified" denotes that a nucleic acid or protein gives rise to essentially one band in an electrophoretic gel. Particularly, it means that the nucleic acid or protein is at least 85% pure, more preferably at least 95% pure, and most preferably at least 99% pure. As used herein, the term "synthetic", with reference to, for example, a synthetic nucleic acid molecule or a synthetic gene or a synthetic peptide refers to a nucleic acid molecule or polypeptide molecule that is produced by recombinant methods and / or by chemical synthesis methods. As used herein, production by recombinant means by using recombinant DNA methods means the use of the well-known methods of molecular biology for expressing proteins encoded by cloned DNA. "Post-translational modification(s)" (PTM) refer to the covalent modification(s) of peptides or proteins, which are introduced following protein biosynthesis under natural conditions. The term includes without limitation glycosylation, phosphorylation, acylation, adenylation, farnesylation, ubiquitination, and sulfation. Post-translational modifications may influence the activity of peptides or proteins. In 2004, Gutiérrez et al. have described the sulfation and glycosylation state of the murine CCR8 chemokine receptor, and the way in which these post-translational modifications affect CCR8 activity. They suggest that tyrosines at positions 14 and 15 in mouse CCR8 are sulfated amino acid residues, whereas asparagine 8 and threonines 10 and 12 are glycosylated. Furthermore, they show that the sulfations are important for the activity of CCR8 (Gutiérrez, Julio, et al. "Analysis of post-translational CCR8 modifications and their influence on receptor activity." Journal of Biological Chemistry 279.15 (2004): 14726-14733.). A "sulfation" is a posttranslational modification where a sulfate group is added to an amino acid such as a tyrosine residue of a polypeptide or protein. Tyrosine sulfation occurs in all multicellular organisms. Under physiological conditions it is catalyzed by tyrosylprotein sulfotransferases (TPSTs) 1 and 2, Golgi- resident enzymes which transfer sulfate from the cofactor PAPS (3'-phosphoadenosine 5'-phosphosulfate) to a context-dependent tyrosine in a protein substrate. Synthetic sulfation of tyrosine may be performed with a technique known in the art, e.g. as described in Bunschoten, Anton, et al. "A general sequence independent solid phase method for the site specific synthesis of multiple sulfated-tyrosine containing peptides." Chemical Communications 21 (2009): 2999-3001. A sulfated polypeptide is a polypeptide comprising at least one sulfation. A non-sulfated polypeptide is a polypeptide comprising no sulfation. A "tyrosine rich domain" (TRD) is a conserved domain which characterizes seven transmembrane proteins such as CXC and CC chemokine receptors. The TRD is typically located at the N terminus of the chemokine receptor and is typically linked to a LID domain via a cysteine, cf. Fig. 2 b. Thus, as used herein, the term TRD refers to the amino acid or protein sequence of a CXC or CC chemokine receptor which is located N terminal of the first cysteine counted from the N terminus. The TRD may or may not comprise a signal peptide. The TRD may or may not be modified. Besides tyrosine, a TRD often comprises negatively charged amino acid residues such as aspartic acid. TRDs have been proposed to be important structures for the interaction of chemokine receptors with their endogenous ligands. Under physiological conditions, the tyrosine residues in a TRD can be sulfated, non-sulfated or partially sulfated. The specific sequences for the TRDs of the respective chemokine receptors are provided in Table 4.1. However, it is obvious that mutations may be introduced in the TRD sequence without changing the overall charge and interaction pattern. Preferably, a TRD has at least a 90 %, 95 % or 99 % sequence identity or sequence similarity with at least one TRD sequence according to Table 4.1. The term "N terminus" or "N term" of a chemokine receptor as used herein refers to the N terminal amino acids of the chemokine receptor comprising at least the TRD. Where a polypeptide or protein comprises a signal peptide, the N terminus may also refer to the N terminal sequence behind the natural cleavage site of the polypeptide or protein. According to some preferred embodiments, the N terminus comprises the LID domain and the TRD domain of a chemokine receptor but does not comprise the natural cysteine between these two domains. Instead, the cysteine can be removed or can be replaced by a different amino acid. The "LID" domain of a chemokine receptor as used herein refers to an amino acid sequence located C terminal of the TRD of the chemokine receptor. TRD and LID domain are typically separated by a single cysteine. "Sequence identity" or "percent identity" is a number that describes how similar a query sequence is to a target sequence, more precisely how many characters in each sequence are identical after alignment. The most popular tool to calculate sequence identity is BLAST (basic local alignment search tool, https: / / blast.ncbi.nlm.nih.gov / ), which performs comparisons between pairs of sequences, searching for regions of local similarity. Suitable alignment methods are known in the art, e.g. Needleman-Wunsch algorithm for global-global alignment, using BLOSUM62 matrix, with gap opening penalty of 11 and a gap extension penalty of 1. Afterwards, the pairs of aligned identical residues can be counted and then divided by the total length of the alignment (including gaps, internal as well as external) to arrive at the percent identity value. For "percent similarity" or "sequence similarity" values, the same approach as for percent identity values can be used, except that what is counted, instead of pairs of identical residues, is the aligned residue pairs with BLOSUM62 values that are not negative (i.e., <com:Math><semantics>≥0<annotation encoding="application / x-tex">\geq 0< / annotation>< / semantics>< / com:Math>). "Seven transmembrane receptors" (7-TM receptors) are integral membrane proteins that contain seven membrane-spanning helices. As used herein, 7-TM receptors are G protein-coupled receptors. "Chemokine receptors" are seven transmembrane receptors. The chemokine receptor family contains 24 members in humans and can be subdivided, based on the class of chemokines they bind, into four subfamilies: CX3CR, CXCR, CCR, and XCR, all of them activating G proteins, and ACKR, containing 6 atypical receptors, unable to activate G proteins upon ligand binding. "CXC chemokine receptors" (CXCR) are integral membrane proteins that specifically bind and respond to cytokines of the CXC chemokine family. They represent one subfamily of chemokine receptors, a large family of G protein-linked receptors that are known as seven transmembrane (7-TM) proteins, since they span the cell membrane seven times. There are currently seven known CXC chemokine receptors in mammals, named CXCR1, CXCR2, CXCR3, CXCR4, CXCR5, and CXCR6. CXCR6 is more closely related in structure to CC chemokine receptors than to other CXC chemokine receptors. "CC chemokine receptors" (CCR, also beta chemokine receptors) are integral membrane proteins that specifically bind and respond to cytokines of the CC chemokine family. They represent one subfamily of chemokine receptors, a large family of G protein-linked receptors that are known as seven transmembrane (7-TM) proteins since they span the cell membrane seven times. The subfamily of the CC chemokine receptors comprises CCR1, CCR2, CCR3, CCR4, CCR5, CCR6, CCR7, CCR8, CCR9 and CCR10. The term "CCR8" refers to the C-C chemokine receptor type 8. The CCR8 protein is encoded by the gene CCR8 (NCBI gene ID 1237). Synonyms for CCR8 are inter alia CC-CKR-8, CCR-8, CDw198, CKRL1, CMKBR8, CMKBRL2, GPRCY6, CY6, TER1. The CCR8 protein comprises human, murine, rat, rhesus macaque and further mammalian and non-mammalian homologues. Sequence(s) for human CCR8 are accessible via UniProt Identifier P51685 (CCR8_HUMAN), for instance human isoform P51685-1 or P51685-2 (UniProt, November 29, 2019). Sequence(s) for murine CCR8 are accessible via UniProt Identifier P56484 (CCR8 MOUSE). Sequence(s) for Rhesus macaque CCR8 are accessible via UniProt Identifier O97665 (CCR8 MACMU). Different isoforms and variants may exist for the different species and are all comprised by the term CCR8. Also comprised are CCR8 molecules before and after maturation, i.e., independent of cleavage of one or more pro-domains. In addition, synthetic variants of the CCR8 protein may be generated and are comprised by the term CCR8. The protein CCR8 may furthermore be subject to various modifications, e.g., synthetic or naturally occurring modifications, such as post translational modifications. Recombinant human CCR8 is commercially available or can be manufactured as known in the art. CCR8 is a receptor for the chemokine CCL1 / SCYA1 / I-309. Barington et al. have reported the importance of conserved extracellular disulfide bridges and aromatic residues in extracellular loop 2 (ECL-2) for ligand binding and activation in the chemokine receptor CCR8 (Barington, Line, et al. "Role of conserved disulfide bridges and aromatic residues in extracellular loop 2 of chemokine receptor CCR8 for chemokine and small molecule binding." Journal of Biological Chemistry 291.31 (2016): 16208-16220.). Furthermore, they found that two distinct aromatic residues in ECL-2, Tyr184 (Cys + 1) and Tyr187 (Cys + 4), were crucial for binding of the CC chemokines CCL1 (agonist) and MC148 (antagonist), respectively, but not for small molecule binding. "Programmed Death-1 (PD-1)" refers to an immunoinhibitory receptor belonging to the CD28 family. PD-1 is expressed predominantly on previously activated T cells in vivo and binds to two ligands, PD-L1 and PD-L2. The term "PD-1" as used herein includes without limitation human PD-1 (hPD-1), variants, isoforms, and species homologs of hPD-1, and analogs having at least one common epitope with hPD-1. The complete hPD-1 sequence can be found under GenBank Accession No. U64863 (November 29, 2019). "Programmed Death Ligand-1 (PD-L1)" is one of two cell surface glycoprotein ligands for PD-1 (the other being PD-L2) that down regulate T cell activation and cytokine secretion upon binding to PD-1. The term "PD-L1" as used herein includes without limitation human PD-L1 (hPDL1), variants, isoforms, and species homologs of hPD-L1, and analogs having at least one common epitope with hPD-L1. The complete hPD-L1 sequence can be found under GenBank Accession No. Q9NZQ7 (November 29, 2019). "Tumor Proportion Score" (TPS) is the percentage of viable tumor cells showing partial or complete membrane staining at any intensity. For example, a specimen should be considered to have PD-L1 expression if TPS <com:Math><semantics>≥<annotation encoding="application / x-tex">\geq< / annotation>< / semantics>< / com:Math> 1% and high PDL1 expression if TPS <com:Math><semantics>≥<annotation encoding="application / x-tex">\geq< / annotation>< / semantics>< / com:Math> 50%. For example, PD-L1 protein expression in NSCLC is usually determined by using Tumor Proportion Score (TPS). "Combined Positive Score" (CPS) is the number of staining cells (tumor cells, lymphocytes, macrophages) divided by the total number of viable tumor cells, multiplied by 100. For example, a specimen should be considered to have PD-L1 expression if <com:Math><semantics>CPS≥1<annotation encoding="application / x-tex">CPS \ge 1< / annotation>< / semantics>< / com:Math> and to have high PD-L1 expression if CPS <com:Math><semantics>≥<annotation encoding="application / x-tex">\geq< / annotation>< / semantics>< / com:Math> 10. The FDA has approved the use of the PD-L1 IHC 22C3 pharmDx assay to determine a patient's eligibility for therapeutic antibody pembrolizumab. "FOXP3" is a 50-55 kD transcription factor, also known as Forkhead box protein P3, Scurfin, JM2, or IPEX. It is proposed to be a master regulatory gene and more specific marker of T regulatory cells than most cell surface markers. Transduced expression of FOXP3 in CD4+ / CD25- cells has been shown to induce GITR, CD103, and CTLA4 and impart a T regulatory cell phenotype. Biolegend antibody clones 206D and 259D recognize a human FOXP3 epitope in the region of amino acids 105-235. Poly6238 recognizes both human and mouse FOXP3 and was raised against the N-terminal portion of FOXP3. The term "modulation" refers to any alteration of an existing process or behavior, such as blocking (antagonism) and induction (agonism). For example, modulation of G protein independent signaling refers to any significant alteration of G-protein independent signaling. The term "internalization" of an antibody, fragment or conjugate refers to the uptake of the antibody, fragment or conjugate into a cell. Preferably, internalization is determined for a cell line with endogenous target expression, e.g. as described elsewhere herein for human or murine CCR8. Preferably, internalization is determined by measuring total internalized fluorescence intensity per cell and is quantified relative to an isotype control, e.g. as described in example 10.5. In brief, the antibody, fragment or conjugate and a matching isotype control are labeled with a dye and internalized fluorescence is determined and quantified for the antibody, fragment or conjugate relative to the isotype control. A "non- internalizing antibody" is defined as an antibody showing substantially the same internalization as a corresponding isotype control. A "low internalizing antibody" is defined as an antibody showing an internalization which is equal to or lower than the 10-fold of the internalization of the isotype control, preferably lower than the 9-, 8-, 7-, 6-, 5-, 4-, 3-, 2-, 1.5-, 1.4-, 1.3-, 1.2-, or 1.1-fold of the internalization of the isotype control. A "medium internalizing antibody" is defined as an antibody showing an internalization which is equal to or lower than the 21-fold of the internalization of the isotype control and higher than the 10-fold of the internalization of the isotype control. A "high internalizing antibody" is defined as an antibody showing an internalization which is higher than the 21-fold of the internalization of the isotype control. In the alternative, internalization can furthermore be quantified based on <com:Math><semantics>t(1 / 2)<annotation encoding="application / x-tex">t(1 / 2)< / annotation>< / semantics>< / com:Math>, i.e. as time until half of the amount of antibody, fragment or conjugate has been internalized. Preferably, antibodies according to the current invention are characterized by a time until half of the amount of antibody, fragment or conjugate has been internalized which is <com:Math><semantics>>2<annotation encoding="application / x-tex">> 2< / annotation>< / semantics>< / com:Math> hours, preferably <com:Math><semantics>>4<annotation encoding="application / x-tex">> 4< / annotation>< / semantics>< / com:Math>, <com:Math><semantics>>5<annotation encoding="application / x-tex">> 5< / annotation>< / semantics>< / com:Math>, <com:Math><semantics>>6<annotation encoding="application / x-tex">> 6< / annotation>< / semantics>< / com:Math>, <com:Math><semantics>>7<annotation encoding="application / x-tex">> 7< / annotation>< / semantics>< / com:Math>, <com:Math><semantics>>8<annotation encoding="application / x-tex">> 8< / annotation>< / semantics>< / com:Math>, <com:Math><semantics>>9<annotation encoding="application / x-tex">> 9< / annotation>< / semantics>< / com:Math>, <com:Math><semantics>>10<annotation encoding="application / x-tex">> 10< / annotation>< / semantics>< / com:Math>, <com:Math><semantics>>11<annotation encoding="application / x-tex">> 11< / annotation>< / semantics>< / com:Math>, <com:Math><semantics>><annotation encoding="application / x-tex">>< / annotation>< / semantics>< / com:Math> <com:Math><semantics>12,>13,>14,>15,>16,>17,>18,>19,>20,>21,>22,>23,>24,>26,>28,>30,or>48hours.<annotation encoding="application / x-tex">12, > 13, > 14, > 15, > 16, > 17, > 18, > 19, > 20, > 21, > 22, > 23, > 24, > 26, > 28, > 30, or > 48 hours.< / annotation>< / semantics>< / com:Math> Most preferably, antibodies according to the current invention are not internalized at all, i.e., no time can be defined until which half of the amount of antibody, fragment or conjugate has been internalized. An "isotype control" is an antibody or fragment that does not bind a target but has the same class and type as the reference antibody or fragment recognizing the target. An antibody or fragment is termed "cross-reactive" or "cross reactive" if the antibody or fragment binds an antigen from two or more different species, e.g. with a KD value of 10-7 M or less, more preferably of less than 10-8 M, even more preferably in the range from 10-9 M to 10-11 M. By the term "specifically binds" as used herein with respect to an antibody, is meant an antibody which recognizes a specific antigen, but does not substantially recognize or bind other molecules in a sample: An antibody characterized by substantial unspecific binding would lack therapeutic applicability, such that these embodiments are excluded. However, as known in the art, specific binding of an antibody or binder does not necessarily exclude an antibody or binder binding to further antigens / target molecules. An antibody that specifically binds to an antigen from one species may also bind to that antigen from one or more further species. Such cross-species reactivity does not itself alter the classification of an antibody as specific. In some instances, the terms "specific binding" or "specifically binding" can be used in reference to the interaction of an antibody, a protein, or a peptide with a second chemical species, to mean that the interaction is dependent upon the presence of a particular structure (e.g., an antigenic determinant or epitope) on the chemical species; for example, an antibody recognizes and binds to a specific protein structure rather than to protein generally. If an antibody is specific for epitope "A", the presence of a molecule containing epitope A (or free, unlabeled A), in a reaction containing labeled "A" and the antibody, will reduce the amount of labeled A bound to the antibody. In case of doubt, specific binding of an antibody or binder preferably describes binding of an antibody, antibody fragment or binder to its antigen / target with an affinity of at least 10-7 M (as KD value; i.e. preferably those with KD values smaller than 10-7 M), with the antibody or binder having an at least two times lower affinity for a non-specific antigen which is not the predetermined antigen / target molecule or a closely related antigen / target molecule. "Polyspecificity", also "polyreactivity" or "unspecific binding" refers to the binders' or antibodies' ability to bind a defined set of unrelated antigens. Unspecific binding is substantial, if the (therapeutic) applicability of the antibody is compromised. Polyspecificity for non-protein structures including without limitation target negative cell lines or tissues, baculo virus particle (BVP), insulin or DNA, may be evaluated as known in the art and as described herein. For example, unspecific binding to target negative human cell lines can be determined e.g. by FACS analysis using mock transfected CHO or HEK cells. In a second example, unspecific binding to different tissues can be analyzed by FACS analysis of a cell line or panel of cell lines derived from the respective tissue. In a third example, unspecific binding to immune cell populations can be analyzed by FACS after sorting the immune cell populations as known in the art. In a fourth example, unspecific binding to BVP, insulin or DNA can be analyzed using ELISA, e.g. as described in Hötzel, Isidro, et al. "A strategy for risk mitigation of antibodies with fast clearance." MAbs. Vol. 4. No. 6. Taylor & Francis, 2012.; Avery, Lindsay B., et al. "Establishing in vitro in vivo correlations" to screen monoclonal antibodies for physicochemical properties related to favorable human pharmacokinetics." MAbs. Vol. 10. No. 2. Taylor & Francis, 2018., and Jain, Tushar, et al. "Biophysical properties of the clinical-stage antibody landscape." Proceedings of the National Academy of Sciences 114.5 (2017): 944-949., referenced herein in their entirety and in particular with regards to the technical details necessary to analyze and quantify unspecific binding. An antibody without substantial unspecific binding is preferably characterized by an unspecific binding that is lower than unspecific binding of reference antibody Gantenerumab (Roche) and most preferably lower than unspecific binding of reference antibody Remicade (Janssen Biotech). The term "off target binding" refers to the ability of an antibody to bind individual proteins different from the intended target, for example proteins of the targets' protein family. Off target binding may be evaluated using commercial assays known in the art such as the Retrogenix off target profiling assay. In brief, antibodies are tested on microarrays containing HEK293 cells individually expressing several thousand human membrane proteins and secreted proteins. Binding of the antibody to a potential off target has to be confirmed by FACS using cells overexpressing the potential off target. The term "affinity" is a term of the art and describes the strength of binding between a binder, antibody or antibody fragment and a target. The "affinity" of antibodies and fragments thereof for a target can be determined using techniques well known in the art or described herein, for example by ELISA, isothermal titration calorimetry (ITC), surface plasmon resonance (SPR), flow cytometry or fluorescent polarization assays. Preferably the affinity is provided as dissociation constant KD. The "dissociation constant" (KD) has molar units (M) and corresponds to the concentration of the binder / antibody at which half of the target proteins are occupied at equilibrium. The smaller the dissociation constant is, the higher is the affinity between the binder or antibody and its target. According to the current invention, the antibodies preferably have a target affinity of at least 10-7 M (as KD value), more preferably of at least 10-8 M, even more preferably in the range from 10-9 M to 10-11 M. The KD values can be preferably determined by means of surface plasmon resonance spectroscopy, e.g. as described elsewhere herein. Where assay conditions were found to influence the determined KD, the assay setup with the least standard deviation shall be used. "Half maximal effective concentration" (EC50) refers to the concentration of a drug, antibody, fragment, conjugate or molecule which induces a response halfway between the baseline and maximum after a specified incubation time. In the context of antibody binding, the EC50 thus reflects the antibody concentration needed for half-maximal binding. An EC50 can be determined if an inflection point can be determined by mathematical modeling (e.g., non-linear regression) of the dose–response curve describing the relationship between applied drug, antibody, fragment, conjugate or molecule concentration and signal. For example, if the dose–response curve follows a sigmoidal curve, an EC50 can be determined. Where the response is an inhibition, the EC50 is termed half maximal inhibitory concentration (IC50). EC80 can be determined mutatis mutandis. The term "antibody" (Ab) refers to an immunoglobulin molecule (e.g. without limitation human IgG1, IgG2, IgG3, IgG4, IgM, IgD, IgE, IgA1, IgA2, mouse IgG1, IgG2a, IgG2b, IgG2c, IgG3, IgA, IgD, IgE or IgM, rat IgG1, IgG2a, IgG2b, IgG2c, IgA, IgD, IgE or IgM, rabbit IgA1, IgA2, IgA3, IgE, IgG, IgM, goat IgA, IgE, IgG1, IgG2, IgE, IgM or chicken IgY) that specifically binds to, or is immunologically reactive with, a particular antigen. Antibodies or antibody fragments comprise complementarity determining regions (CDRs), also known as hypervariable regions, in both the light chain and heavy chain variable domains. The more highly conserved portions of the variable domains are called the framework (FR). As is known in the art, the amino acid position / boundary delineating a hypervariable region of an antibody can vary, depending on the context and the various definitions known in the art. As used herein, numbering of immunoglobulin amino acid residues is done according to the immunoglobulin amino acid residue numbering system of Kabat et al.. The variable domains of native heavy and light chains each comprise four FR regions. The three CDRs in each chain are held together in close proximity by the FR regions and, with the CDRs from the other chain, contribute to the formation of the antigen binding site of antibodies, see Kabat, E. A., et al. "Sequences of Proteins of Immunological Interest (Natl. Inst. Health, Bethesda, MD), GPO Publ." No165-462 (1987). The term antibody as used herein also refers to antibody fragments, except where explicitly stated otherwise. Depending on the respective context, the term antibody may also refer to any proteinaceous binding molecule with immunoglobulin-like function. The term "CDR" refers to the complementary determining region of the antibody. As known in the art complementarity-determining regions (CDRs) are part of the variable chains in antibodies and T cell receptors. A set of CDRs constitutes a paratope. CDRs are crucial to the diversity of antigen specificities. There are three CDRs (CDR1, CDR2 and CDR3), arranged non-consecutively on the amino acid sequence of a variable domain of an antigen receptor. Since the antigen receptors are typically composed of two variable domains (on two different polypeptide chains, heavy and light chain), there are usually six CDRs for each antigen receptor that can collectively come into contact with the antigen. The CDRs of the light chain are LCDR1, LCDR2 and LCDR3. The CDRs of the heavy chain are termed HCDR1, HCDR2 and HCDR3. HCDR3 is the most variable complementary determining region (see, e.g., Chothia, Cyrus, and Arthur M. Lesk. "Canonical structures for the hypervariable regions of immunoglobulins." Journal of molecular biology 196.4 (1987): 901-917.; Kabat, E. A., et al. "Sequences of proteins of immunological interest. Bethesda, MD: US Department of Health and Human Services." Public Health Service, National Institutes of Health (1991): 103-511.). The "constant region" refers to the portion of the antibody molecule that confers effector functions. The heavy chain constant region can be selected from any of the five isotypes: alpha (<com:Math><semantics>α<annotation encoding="application / x-tex">\alpha< / annotation>< / semantics>< / com:Math>), delta (<com:Math><semantics>δ<annotation encoding="application / x-tex">\delta< / annotation>< / semantics>< / com:Math>), epsilon (<com:Math><semantics>ϵ<annotation encoding="application / x-tex">\epsilon< / annotation>< / semantics>< / com:Math>), gamma (g), or mu (<com:Math><semantics>μ<annotation encoding="application / x-tex">\mu< / annotation>< / semantics>< / com:Math>). The term "Fc domain", "Fc region" or "Fc part" as used herein refers to a C-terminal region of an antibody heavy chain that contains at least a portion of the constant region. The term includes native sequence Fc regions and variant Fc regions. For example, a human IgG heavy chain Fc region may extend from Cys226, or from Pro230, to the carboxyl-terminus of the heavy chain. Antibodies or binding fragments according to the current invention may have been modified to alter at least one constant region-mediated biological effector function. For example, in some embodiments, an antibody may be modified to reduce or enhance at least one constant region-mediated biological effector function relative to the unmodified antibody, e.g., reduced or improved binding to the Fc receptor (Fc<com:Math><semantics>γ<annotation encoding="application / x-tex">\gamma< / annotation>< / semantics>< / com:Math>R). FcγR binding may be reduced, e.g. by mutating the immunoglobulin constant region segment of the antibody at particular regions necessary for FcyR interactions (see, e.g., Canfield, Stephen M., and Sherie L. Morrison. "The binding affinity of human IgG for its high affinity Fc receptor is determined by multiple amino acids in the CH2 domain and is modulated by the hinge region." The Journal of experimental medicine 173.6 (1991): 1483-1491; and Lund, John, et al. "Human Fc gamma RI and Fc gamma RII interact with distinct but overlapping sites on human IgG." The Journal of Immunology 147.8 (1991): 2657-2662.). FcyR binding may be enhanced, e.g. by afucosylation. Reducing FcyR binding may also reduce other effector functions which rely on FcγR interactions, such as opsonization, phagocytosis and antigen-dependent cellular cytotoxicity ("ADCC"). Furthermore, addressing the interaction of Fc with FcRn allows to modulate the half-life of antibodies in vivo. Abrogating the interaction by e.g. introduction of mutation H435A leads to an extremely short half- life, since the antibody is no longer protected from lysosomal degradation by FcRn recycling. In some preferred embodiments according to all aspects, the antibody according to the current invention comprises mutation H435A or has otherwise been engineered for a reduced half-life. In contrast, antibodies comprising "YTE" mutations (M252Y / S254T / T256E) and / or equivalent mutations such as "LS" mutations (M428L / N434S) have been shown to significantly extend the half-life by more efficient recycling from endosomes in both pre-clincal species as well as humans (Dall'Acqua, William F., et al. "Increasing the affinity of a human IgG1 for the neonatal Fc receptor: biological consequences." The Journal of Immunology 169.9 (2002): 5171-5180.; Zalevsky, Jonathan, et al. "Enhanced antibody half-life improves in vivo activity." Nature biotechnology 28.2 (2010): 157-159.). In some preferred embodiments according to all aspects, the antibody according to the current invention comprises YTE mutations (M252Y / S254T / T256E) and / or equivalent mutations such as LS (M428L / N434S) or has otherwise been engineered for an improved half-life. Suitable Fc engineering approaches for extension of half-life can be found in Haraya, Kenta, Tatsuhiko Tachibana, and Tomoyuki Igawa. "Improvement of pharmacokinetic properties of therapeutic antibodies by antibody engineering." Drug metabolism and pharmacokinetics 34.1 (2019): 25-41., and / or Lee, Chang-Han, et al. "An engineered human Fc domain that behaves like a pH-toggle switch for ultra-long circulation persistence." Nature communications 10.1 (2019): 1-11. "Afucosylated" antibodies are antibodies engineered such that the oligosaccharides in the Fc region of the antibody do not have any fucose sugar units. Glycosylation of an antibody can alter its function. For example, if glycosylation at N297 in the CH2 domain of an IgG is completely eliminated, binding to FcyRs is lost. However, modulation of the specific carbohydrate composition at N297 can have the opposite effect and enhance the ADCC activity of the antibody. In brief, the affinity of an antibody for the activating FcyRs depends on the composition of the N297 N-linked oligosaccharide. There are 32 different possible combinations of oligosaccharides that can occur at this site. Naturally occurring human IgG and those produced by hybridomas or other common expression systems are usually composed of N- acetylglucosamine (GlcNAc) and three mannose residues that form a core carbohydrate. This core is attached to two additional GlcNAc groups to form biantennary branches. The addition of galactose at each branch can occur as well as the terminal addition of sialic acid to these galactose molecules. Fucose is often part of the core GlcNAc. This fucose, through steric hindrance, obstructs the interaction of the antibody with the FcyRIIIA. Thus, elimination of this fucose molecule while maintaining other forms of glycosylation at this site increases the binding of the antibody to the activating FcyRs, enhancing its ability to elicit ADCC and / or ADCP (Almagro, Juan C., et al. "Progress and challenges in the design and clinical development of antibodies for cancer therapy." Frontiers in immunology 8 (2018): 1751.). Methods of preparing fucose-less antibodies include growth in rat myeloma YB2 / 0 cells (ATCC CRL 1662). YB2 / 0 cells express low levels of FUT8 mRNA, which encodes <com:Math><semantics>α<annotation encoding="application / x-tex">\alpha< / annotation>< / semantics>< / com:Math>-1,6-fucosyltransferase, an enzyme necessary for fucosylation of polypeptides. Afucosylated antibodies are preferred for the current invention. "Antibody-dependent cellular cytotoxicity" ("ADCC"), also referred to as "antibody-dependent cell- mediated cytotoxicity", is a mechanism of cell-mediated immune defense whereby an immune cell actively lyses a target cell, whose membrane-surface antigens have been bound by specific antibodies. ADCC is mediated via interaction of the antibody or fragment with FcyRIIIa. In humans, FcyRIII exists in two different forms: FcyRIIIa (CD16a) and FcyRIIIb (CD16b). While FcyRIIIa is expressed on monocytes, neutrophils, mast cells, macrophages, and natural killer cells as a transmembrane receptor, FcyRIIIb is only expressed on neutrophils. These receptors bind to the Fc portion of IgG antibodies, which then activates antibody-dependent cell-mediated cytotoxicity (ADCC) mediated by the human effector cells. Different assay systems to determine ADCC induction in human subjects have been described in the literature and are suitable for characterization of the subject matter disclosed herein. For example, Yao- Te Hsieh et al. have studied different ADCC assay systems, namely assays based on (i) natural killer cells from human donors (FcyRIIIA + primary NK), (ii) FcyRIIIA engineered NK-92 cells and (iii) FcγRIIIA / NFAT-RE / luc2 engineered Jurkat T cells (Hsieh, Yao-Te, et al. "Characterization of FcγRIIIA effector cells used in in vitro ADCC bioassay: comparison of primary NK cells with engineered NK-92 and Jurkat T cells." Journal of Immunological Methods 441 (2017): 56-66, referenced herein in entirety; in particular, reference is made to the method description for these assays). In brief, all three effector cell systems differentially express FcyRIIIA and provide dose-dependent ADCC pathway activity, yet only primary NK and engineered NK-92 cells are capable of inducing ADCC-mediated cell lysis. For functional assessment of ADCC activity, primary NK or NK-92 (V-158) cells thus better reflect the physiologically relevant ADCC mechanism of action. As an engineered cell line, NK-92 cells may behave more reproducibly than primary NK and is therefore the preferred assay system to determine ADCC response in human subjects, e.g. in case of doubt. An antibody or antigen-binding fragment inducing ADCC is an antibody which may elicit a substantial amount of lysis of target cells in the presence of NK effector cells. Preferably, the ADCC induction results in the lysis of at least 2 %, 5 %, 10 %, 15 %, 20 %, 25 %, 30 %, 35 %, 40 %, 45 %, 50 %, 55 %, 60 %, 65 %, 70 %, 75 %, 80 %, 85 %, 90 %, 95 % or 99 % of the target cells. "Antibody-dependent cellular phagocytosis" ("ADCP") is the mechanism by which antibody- opsonized target cells activate the FcyRs on the surface of macrophages to induce phagocytosis, resulting in internalization and degradation of the target cell. For ADCP, binding to macrophages as effector cells typically occurs via the interaction of the antibodies FC part with FcyRIIa (CD32a) expressed by macrophages. An antibody or antigen-binding fragment inducing ADCP is an antibody which may elicit a substantial amount of phagocytosis of target cells in the presence of macrophages. Preferably, the ADCP induction results in the phagocytosis of at least 2 %, 5 %, 10 %, 15 %, 20 %, 25 %, 30 %, 35 %, 40 %, 45 %, 50 %, 55 %, 60 %, 65 %, 70 %, 75 %, 80 %, 85 %, 90 %, 95 % or 99 % of the target cells. "Complement-dependent cytotoxicity" ("CDC") is an effector function of IgG and IgM antibodies. When they are bound to a surface antigen on a target cell (e.g. bacterial or viral infected cell), the classical complement pathway is triggered by bonding protein C1q to these antibodies, resulting in formation of a membrane attack complex (MAC) and target cell lysis. Complement system is efficiently activated by human IgG1, IgG3 and IgM antibodies, weakly by IgG2 antibodies and is not activated by IgG4 antibodies. It is one mechanism of action by which therapeutic antibodies - also specific embodiments of the antibodies according to the current invention - can achieve an antitumor effect. Several laboratory methods exist for determining the efficacy of CDC and are known in the art. An antibody or antigen-binding fragment inducing CDC is an antibody which may elicit a substantial amount of formation of a membrane attack complex and lysis of target cells. Preferably, the CDC induction results in the lysis of at least 2 %, 5 %, 10 %, 15 %, 20 %, 25 %, 30 %, 35 %, 40 %, 45 %, 50 %, 55 %, 60 %, 65 %, 70 %, 75 %, 80 %, 85 %, 90 %, 95 % or 99 % of the target cells. Antibodies comprising an Fc region may or may not comprise a modification promoting the association of the first and the second subunit of the Fc domain. A "modification promoting the association of the first and the second subunit of the Fc domain" is a manipulation of the peptide backbone or the post-translational modifications of an Fc domain subunit that reduces or prevents the association of a polypeptide comprising the Fc domain subunit with an identical polypeptide to form a homodimer. Antibodies comprising an Fc region may or may not comprise a modification promoting the association of the first and the second subunit of the Fc domain. A modification promoting association as used herein particularly includes separate modifications made to each of the two Fc domain subunits desired to associate (i.e. the first and the second subunit of the Fc domain), wherein the modifications are complementary to each other so as to promote association of the two Fc domain subunits. For example, a modification promoting association may alter the structure or charge of one or both of the Fc domain subunits so as to make their association sterically or electrostatically favorable. Thus, (hetero)dimerization occurs between a polypeptide comprising the first Fc domain subunit and a polypeptide comprising the second Fc domain subunit, which might be non- identical, e.g. in the sense that further components fused to each of the subunits (e.g. antigen binding moieties) are not the same. In some embodiments the modification promoting association comprises an amino acid mutation in the Fc domain, specifically an amino acid substitution. In a particular embodiment, the modification promoting association comprises a separate amino acid mutation, specifically an amino acid substitution, in each of the two subunits of the Fc domain. A "fragment" of an antibody as used herein is required to substantially retain the desired affinity of the full-length antibody. As such, suitable fragments of an anti-human CCR8 antibody will retain the ability to bind to the target chemokine receptor, e.g. to bind to human CCR8 receptor. Fragments of an antibody comprise a portion of a full-length antibody, generally the antigen binding or variable region thereof. Examples of antibody fragments include, but are not limited to, Fab, Fab', F(ab')2, and Fv fragments, single-chain antibody molecules, diabodies and domain antibodies, see Holt, Lucy J., et al. "Domain antibodies: proteins for therapy." Trends in biotechnology 21.11 (2003): 484-490. A "Fab fragment" contains the constant domain of the light chain and the first constant domain (CH2) of the heavy chain. "Fab' fragments" differ from Fab fragments by the addition of a few residues at the carboxyl terminus of the heavy chain CH2 domain including one or more cysteines from the antibody hinge region. "F(ab') fragments" are produced by cleavage of the disulfide bond at the hinge cysteines of the F(ab')2 pepsin digestion product. Additional chemical couplings of antibody fragments are known to those of ordinary skill in the art. Fab and F(ab')2 fragments lack the Fc fragment of intact antibody, clear more rapidly from the circulation of animals, and may have less non-specific tissue binding than an intact antibody, see, e.g., Wahl, Richard L., Charles W. Parker, and Gordon W. Philpott. "Improved radioimaging and tumor localization with monoclonal F (ab') 2." Journal of nuclear medicine: official publication, Society of Nuclear Medicine 24.4 (1983): 316-325. An "Fv fragment" is the minimum fragment of an antibody that contains a complete target recognition and binding site. This region consists of a dimer of one heavy and one light chain variable domain in a tight, non-covalent association (VH-VL dimer). It is in this configuration that the three CDRs of each variable domain interact to define an antigen binding site on the surface of the VH-VL dimer. Often, the six CDRs confer antigen binding specificity upon the antibody. However, in some instances even a single variable domain (or half of an Fv comprising only three CDRs specific for a target) may have the ability to recognize and bind the antigen, although at a lower affinity than the entire binding site. "Single-chain Fv" or "scFv" antibody fragments comprise the VH and VL domains of an antibody in a single polypeptide chain. Generally, the Fv polypeptide further comprises a polypeptide linker between the VH and VL domains which enables the scFv to form the desired structure for antigen binding. "Single domain antibodies" are composed of single VH or VL domains which exhibit sufficient affinity to the target. In a specific embodiment, the single domain antibody is a camelized antibody, see, e.g., Riechmann, Lutz, and Serge Muyldermans. "Single domain antibodies: comparison of camel VH and camelised human VH domains." Journal of immunological methods 231.1-2 (1999): 25-38. "Bispecific antibodies" are monoclonal antibodies that have binding specificities for at least two different epitopes on the same or different antigens. In the present disclosure, one of the binding specificities can be directed towards the target chemokine receptor such as CCR8, the other can be for any other antigen, e.g., without limitation for a cell-surface protein, receptor, receptor subunit, tissue-specific antigen, virally derived protein, virally encoded envelope protein, bacterially derived protein, or bacterial surface protein. Bispecific antibody constructs according to the invention also encompass multispecific antibody constructs comprising multiple binding domains / binding sites, such as trispecific antibody constructs, where the construct comprises three binding domains. "Derivatized antibodies" are typically modified by glycosylation, acetylation, pegylation, phosphorylation, sulfation, amidation, derivatization by known protecting / blocking groups, proteolytic cleavage, linkage to a cellular ligand or other protein. Any of numerous chemical modifications may be carried out by known techniques, including, but not limited to, specific chemical cleavage, acetylation, formylation, metabolic synthesis of tunicamycin, etc. Additionally, the derivative may contain one or more non-natural amino acids, e.g., using ambrx technology, see, e.g., Wolfson, Wendy. "Amber codon flashing ambrx augments proteins with unnatural amino acids." Chemistry & biology 13.10 (2006): 1011-1012. Antibodies according to the current invention may be derivatized, e.g. glycosylated or sulfated. "Monoclonal antibodies" are substantially homogenous populations of antibodies binding a particular antigen. Monoclonal immunoglobulins may be obtained by methods well known to those skilled in the art (see for example, Köhler, Georges, and Cesar Milstein. "Continuous cultures of fused cells secreting antibody of predefined specificity." nature 256.5517 (1975): 495-497., and U.S. Patent No. 4,376,110). An immunoglobulin or immunoglobulin fragment with specific binding affinity can be isolated, enriched, or purified from a prokaryotic or eukaryotic organism. Routine methods known to those skilled in the art enable production of both immunoglobulins or immunoglobulin fragments and proteinaceous binding molecules with immunoglobulin-like functions, in both prokaryotic and eukaryotic organisms. The antibodies according to the current invention are preferably monoclonal. "Humanized antibodies" contain CDR regions derived from a non-human species, such as mouse, that have, for example, been engrafted, along with any necessary framework back-mutations, into human sequence-derived V regions. Thus, for the most part, humanized antibodies are human immunoglobulins (recipient antibody) in which residues from a hypervariable region of the recipient are replaced by residues from a hypervariable region of a non-human species (donor antibody) such as mouse, rat, rabbit or non- human primate having the desired specificity, affinity, and capacity. See, for example, U.S. Pat. Nos. 5,225,539; 5,585,089; 5,693,761; 5,693,762; 5,859,205. In some instances, framework residues of the human immunoglobulin are replaced by corresponding non-human residues. Furthermore, humanized antibodies may comprise residues that are not found in the recipient antibody or in the donor antibody. These modifications are made to further refine antibody performance (e.g., to obtain desired affinity). In general, the humanized antibody will comprise substantially all of at least one, and typically two, variable domains, in which all or substantially all of the hypervariable regions correspond to those of a non-human immunoglobulin and all or substantially all of the framework regions are those of a human immunoglobulin sequence. The humanized antibody optionally comprises at least a portion of an immunoglobulin constant region (Fc), typically that of a human immunoglobulin. For further details see Jones, Peter T., et al. "Replacing the complementarity-determining regions in a human antibody with those from a mouse." Nature 321.6069 (1986): 522-525.; Riechmann, Lutz, et al. "Reshaping human antibodies for therapy." Nature 332.6162 (1988): 323-327.; and Presta, Leonard G. "Antibody engineering." Current Opinion in Structural Biology 2.4 (1992): 593-596. Fully human antibodies (human antibodies) comprise human derived CDRs, i.e. CDRs of human origin. Preferably, a fully human antibody according to the current invention is an antibody having at least 90 %, 91 %, 92 %, 93 %, 94 %, 95 %, 96 %, 97 %, 98 %, 99 %, 99.5 % or 100 % sequence identity with the closest human VH germline gene (e.g. sequence extracted from recommended list and analyzed in IMGT / Domain-gap-align). As accepted by usual nomenclature systems such as the INN species subsystem in force until 2017, fully human antibodies may comprise a low number of germline deviations compared with the closest human germline reference determined based on the IMGT database (http: / / www.imgt.org, November 29, 2019). For example, a fully human antibody according to the current invention may comprise up to 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 12, 13, 14 or 15 germline deviations in the CDRs compared with the closest human germline reference. Fully human antibodies can be developed from human derived B cells by cloning techniques in combination with a cell enrichment or immortalization step. The majority of fully human antibodies in clinical use, however, were isolated either from immunized mice transgenic for the human IgG locus or from sophisticated combinatorial libraries by phage display (Brüggemann, Marianne, et al. "Human antibody production in transgenic animals." Archivum immunologiae et therapiae experimentalis 63.2 (2015): 101-108.; Carter, Paul J. "Potent antibody therapeutics by design." Nature reviews immunology 6.5 (2006): 343-357.; Frenzel, André, Thomas Schirrmann, and Michael Hust. "Phage display-derived human antibodies in clinical development and therapy." MAbs. Vol. 8. No. 7. Taylor & Francis, 2016.; Nelson, Aaron L., Eugen Dhimolea, and Janice M. Reichert. "Development trends for human monoclonal antibody therapeutics." Nature reviews drug discovery 9.10 (2010): 767-774.). Several techniques are available to generate fully human antibodies or to generate antibodies comprising human derived CDRs (cf. WO2008112640). Cambridge Antibody Technologies (CAT) and Dyax have obtained antibody cDNA sequences from peripheral B cells isolated from immunized humans and devised phage display libraries for the identification of human variable region sequences of a particular specificity. Briefly, the antibody variable region sequences are fused either with the Gene III or Gene VIII structure of the M13 bacteriophage. These antibody variable region sequences are expressed either as Fab or single chain Fv (scFv) structures at the tip of the phage carrying the respective sequences. Through rounds of a panning process using different levels of antigen binding conditions (stringencies), phages expressing Fab or scFv structures that are specific for the antigen of interest can be selected and isolated. The antibody variable region cDNA sequences of selected phages can then be elucidated using standard sequencing procedures. These sequences may then be used for the reconstruction of a full antibody having the desired isotype using established antibody engineering techniques. Antibodies constructed in accordance with this method are considered fully human antibodies (including the CDRs). In order to improve the immunoreactivity (antigen binding affinity and specificity) of the selected antibody, an in vitro maturation process can be introduced, including a combinatorial association of different heavy and light chains, deletion / addition / mutation at the CDR3 of the heavy and light chains (to mimic V-J, and V-D-J recombination), and random mutations (to mimic somatic hypermutation). An example of a "fully human" antibody generated by this method is the anti-tumor necrosis factor <com:Math><semantics>α<annotation encoding="application / x-tex">\alpha< / annotation>< / semantics>< / com:Math> antibody, Humira (adalimumab). The term "polynucleotide" refers to a recombinantly or synthetically produced polymeric desoxyribonucleotide or analog thereof, or a modified polynucleotide. The term comprises double and single stranded DNA or RNA. The polynucleotide can be integrated e.g. into minicircles, plasmids, cosmids, minichromosomes, or artificial chromosomes. The polynucleotide can be isolated or integrated in another nucleic acid molecule, e.g. in an expression vector or chromosome of a eukaryotic host cell. The term "vector", as used herein, refers to a nucleic acid molecule capable of propagating a nucleic acid molecule to which it is linked. The term further comprises plasmids (non-viral) and viral vectors. Certain vectors are capable of directing the expression of nucleic acids or polynucleotides to which they are operatively linked. Such vectors are referred to herein as "expression vectors". Expression vectors for eukaryotic use can be constructed by inserting a polynucleotide sequence encoding at least one protein of interest (POI) into a suitable vector backbone. The vector backbone can comprise the necessary elements to ensure maintenance of the vector and, if desirable, to provide amplification within the host. For viral vectors, e.g. lentiviral or retroviral vectors, further virus specific elements such as structural elements or other elements can be required and are well known in the art. These elements can be for instance provided in cis (on the same plasmid) or in trans (on a separate plasmid). Viral vectors may require helper viruses or packaging lines for large-scale transfection. Vectors may contain further elements such as e.g. enhancer elements (e.g. viral, eukaryotic), introns, and viral origins of plasmid replication for replication in mammalian cells. According to the current invention, expression vectors typically have a promoter sequence that drives expression of the POI. Expression of the POI and / or selective marker protein may be constitutive or regulated (e.g. inducible by addition or removal of small molecule inductors). Preferred regulatory sequences for mammalian host cell expression include viral elements that direct high levels of expression of a POI in mammalian cells, such as regulatory elements, promoters and / or enhancers derived from cytomegalovirus (CMV), Simian Virus 40 (SV40), adenovirus, (e.g., the adenovirus major late promoter Ad LP) or polyoma. For further description of viral regulatory elements, and sequences thereof, see e.g., U.S. 5,168,062, U.S. 4,510,245 and U.S. 4,968,615. The term "linker" or "spacer" as used herein refers to any molecule enabling a direct topological connection between two moieties. A moiety may be inter alia a polypeptide, a protein, an antibody, an antibody fragment, a cytotoxic moiety, a binding moiety, a moiety for detection such as a fluorophore, a moiety for immobilization or retrieval such as beads or magnetic beads, a reactive moiety, or any other molecule. The two moieties may be of the same type or different. Linkers may be part of conjugates and may even contribute to their function. For instance, for a conjugate comprising a polypeptide and a biotin, the presence of a spacer of approximately 4 Å (~5 atoms) between the carboxy group of the biotin and the 1st bulky amino acid of the peptide allows the biotin to reach the (strept)avidin binding pocket. Various linkers are known in the art and can be selected based on the moieties which shall be connected. The linker length typically ranges between 4 atoms and more than 200 atoms. Linkers exceeding 60 atoms in length generally comprise a population of compounds having an average length. "Linkers for polypeptides" may be attached through an amide linkage or any other functional residue. Linkers for polypeptides may be attached N-terminal or C-terminal of the polypeptide or may be attached via a reactive functional group or amino acid side chain. Polypeptides may be coupled for example to biotin, proteins such as human serum albumin (HSA), carrier proteins such as keyhole limpet hemocyanin (KLH), ovalbumin (OVA) or bovine serum albumin (BSA), fluorescent dyes, short amino acid sequences such as Flag tag, HA tag, Myc tag or His tag, reactive tags such as maleimides, iodoacetamides, alkyl halides, 3-mercaptopropyl or 4-azidobutyric acid, or to various further suitable moieties. Non-limiting examples for suitable linkers, e.g. for conjugation of polypeptides, include beta-alanine, 4-aminobutyric acid (GABA), (2-aminoethoxy) acetic acid (AEA), 5-aminovaleric acid (Ava), 6-aminohexanoic acid (Ahx), PEG2 spacer (8-amino-3,6-dioxaoctanoic acid), PEG3 spacer (12-amino-4,7,10-trioxadodecanoic acid), PEG4 spacer (15-amino-4,7,10,13-tetraoxapenta-decanoic acid), and Ttds (Trioxatridecan- succinamic acid). In some cases, the linker may be derived from a reactive moiety, e.g. maleimides, iodoacetamides, alkyl halides, 3-mercaptopropyl or 4-azidobutyric acid. In some cases, the linker may comprise polyethylene glycol (PEG), polypropylene glycol, polyoxyalkylenes, or copolymers of polyethylene glycol or polypropylene glycol. "Linkers for antibodies" are linkers establishing a covalent connection between different antibody portions and include peptide linker and non-proteinaceous polymers, including but not limited to polyethylene glycol (PEG), polypropylene glycol, polyoxyalkylenes, or copolymers of polyethylene glycol, polypropylene glycol. "Treating" a disease in a subject or "treating" a subject having a disease refers to subjecting the subject to a pharmaceutical treatment, e.g., the administration of a drug, such that at least one symptom of the disease is decreased or prevented from worsening. The terms "prevent", "preventing", "prevention" and the like refer to reducing the probability of developing a disease, disorder, or condition in a subject, who does not have, but is at risk of or susceptible to developing a disease, disorder, or condition. The term "effective amount" or "therapeutically effective amount" are used interchangeably herein and refer to an amount sufficient to achieve a particular biological result or to modulate or ameliorate a symptom in a subject, or the time of onset of a symptom, typically by at least about 10 %; usually by at least about 20 %, preferably at least about 30 %, or more preferably at least about 50 %. Efficacy of the use of an antibody in cancer therapy can be assessed based on the change in tumor burden. Both tumor shrinkage (objective response) and time to the development of disease progression are important endpoints in cancer clinical trials. Standardized response criteria, known as RECIST (Response Evaluation Criteria in Solid Tumors), were published in 2000. An update (RECIST 1.1) was released in 2009. RECIST criteria are typically used in clinical trials where objective response is the primary study endpoint, as well as in trials where assessment of stable disease, tumor progression or time to progression analyses are undertaken because these outcome measures are based on an assessment of anatomical tumor burden and its change over the course of the trial. An effective amount for a particular subject may vary depending on factors such as the condition being treated, the overall health of the subject, the method, route, and dose of administration and the severity of side effects. When in combination, an effective amount is in ratio to a combination of components and the effect is not limited to individual components alone. If not defined otherwise, "Complete Response" (CR) is defined as disappearance of all target lesions. Any pathological lymph nodes (whether target or non-target) must have reduction in short axis to <10 mm. For "Partial Response" (PR) at least a 30 % decrease in the sum of diameters of target lesions has to be reached, taking as reference the baseline sum diameters. For "Progressive Disease" (PD) at least a 20 % increase in the sum of diameters of target lesions, taking as reference the smallest sum on study (this includes the baseline sum if that is the smallest on study). In addition to the relative increase of 20%, the sum must also demonstrate an absolute increase of at least 5 mm. In "Stable Disease" (SD) neither sufficient shrinkage to qualify for PR nor sufficient increase to qualify for PD is observed, taking as reference the smallest sum diameters while on study. Secondary outcome measures that can be used to determine the therapeutic benefit of the inventive antibodies described herein include the following: "Objective Response Rate" (ORR) is defined as the proportion of subjects who achieve a complete response (CR) or partial response (PR). "Progression Free Survival" (PFS) is defined as the time from the first dose date of an antibody to either disease progression or death, whichever occurs first. "Overall Survival" (OS) is defined as the length of time from either the date of diagnosis or the start of treatment for a disease, that patients diagnosed with the disease are still alive. "Duration of Overall Response" (DOR) is defined as the time from the participant's initial CR or PR to the time of disease progression. "Depth of Response" (DpR) is defined as the percentage of tumor shrinkage observed at the maximal response point compared to baseline tumor load. Clinical endpoints for both ORR and PFS can be determined based on RECIST 1.1 criteria described above. Where non-human subjects are analyzed, the aforementioned parameters to determine therapeutic efficacy and benefit have to be adapted as discussed elsewhere herein, cf. example 12 ff. Typical "subjects" according to the current invention include human and non-human subjects. Subjects can be mammals such as mice, rats, cats, dogs, primates and / or humans. "Pharmaceutical compositions" (also "therapeutic formulations") of the antibody, fragment or conjugate can be prepared by mixing the antibody having the desired degree of purity with optional physiologically acceptable carriers, excipients or stabilizers, e.g. according to Remington's Pharmaceutical Sciences (18th ed.; Mack Pub. Co.: Eaton, Pa., 1990), e.g. in the form of lyophilized formulations or aqueous solutions. Acceptable carriers, excipients, or stabilizers are nontoxic to recipients at the dosages and concentrations employed, and include buffers such as phosphate, citrate, and other organic acids; antioxidants including ascorbic acid and methionine; preservatives (such as octadecyldimethylbenzyl ammonium chloride; hexamethonium chloride; benzalkonium chloride, benzethonium chloride; phenol, butyl or benzyl alcohol; alkyl parabens such as methyl or propyl paraben; catechol; resorcinol; cyclohexanol; 3-pentanol; and m-cresol); low molecular weight (less than about 10 residues) polypeptide; proteins, such as serum albumin, gelatin, or immunoglobulins; hydrophilic polymers such as polyvinylpyrrolidone; amino acids such as glycine, glutamine, asparagine, histidine, arginine, or lysine; monosaccharides, disaccharides, and other carbohydrates including glucose, mannose, or dextrins; chelating agents such as EDTA; sugars such as sucrose, mannitol, trehalose or sorbitol; salt- forming counter-ions such as sodium; metal complexes (e.g., Zn-protein complexes); and / or non-ionic surfactants such as Tween®, Pluronic® or polyethylene glycol (PEG). A "host cell" is a cell that is used to receive, maintain, reproduce and amplify a vector. A host cell also can be used to express the polypeptide, e.g. an antibody or fragment thereof encoded by the vector. The nucleic acid contained in the vector is replicated when the host cell divides, thereby amplifying the nucleic acids. Preferred host cells are mammalian cells, such as CHO cells or HEK cells. Further preferred host cells are rat myeloma YB2 / 0 cell. A "cell with endogenous target expression" is a cell which expresses a target protein at a level which is comparable to the physiological or diseased situation. Typically, cells which have been engineered for overexpression express a target protein at much higher levels. The term "intra-tumoral", "intratumoral", "tumor infiltrating" or "tumoral" in the context of cells, structures, proteins, antibodies, or markers refers to their localization within the tumor tissue. Cells which are "positive" or "+" for a certain marker or protein are cells characterized by substantial expression of that marker or protein. Marker or protein expression can be determined and quantified as known in the art, e.g. to define different cell populations. For the characterization of (immune) cell populations, the marker expression can be determined by FACS or using any other technique described herein. "Leukocytes" are immune cells expressing CD45. "CD45+ cells", as used herein, refer to all leukocytes. CD45 can be used as a marker to distinguish immune cells and non-immune cells. The term "lymphocyte" refers to all immature, mature, undifferentiated, and differentiated white lymphocyte populations, including tissue specific and specialized varieties. It encompasses, by way of non-limiting example, B cells, T cells, NKT cells, and NK cells. In some embodiments, lymphocytes include all B cell lineages including pre-B cells, progenitor B cells, early pro-B cells, late pro-B cells, large pre-B cells, small pre-B cells, immature B cells, mature B cells, plasma B cells, memory B cells, B- 1 cells, B-2 cells, and anergic AN1 / T3 cell populations. "T cells" are immune cells expressing TCRαβ, CD3, and CD8 or CD4. As used herein, the term includes naive T cells, CD4+ T cells, CD8+ T cells, regulatory T cells, memory T cells, activated T cells, anergic T cells, tolerant T cells, chimeric B cells, and antigen-specific T cells and further T cell populations known in the art. In some embodiments, the presence of a T cell receptor (TCR) on the cell surface distinguishes T cells from other lymphocytes. "CD8+ T cells" (also "cytotoxic T cell", "TC", "cytotoxic T lymphocyte", "CTL", "T-killer cell", "cytolytic T cell", "CD8+ T-cell" or "killer T cell") are T cells expressing CD3, CD45 and CD8. CD8+ T cells can kill cancer cells, cells that are infected (particularly with viruses), or otherwise damaged cells. "CD4+ T cells" (also "T helper cells", "Th cells") are immune cells expressing CD3, CD4 and CD45. There are several subsets of T helper cells, such as, without limitation, Th1, Th2, and Th17. CD4+ T cells help suppress or regulate immune responses. They are essential in B cell antibody class switching, in the activation and growth of cytotoxic T cells, and in maximizing bactericidal activity of phagocytes such as macrophages. As used herein, the term "Treg cells" (also "Tregs", "regulatory T cells", "T regulatory cells", "suppressor T cells") refers to immune cells expressing CD3, CD4, CD45, and FoxP3, and furthermore expressing high levels of CD25 and low levels of CD127. Identification of Treg cells may be performed as described elsewhere herein. Treg cells typically also express high levels of CTLA-4, GITR, and LAG- 3. In the literature, Tregs have furthermore been classified based on memory marker CD45RO. Under physiological conditions, Treg cells maintain immunological tolerance. During an immune response, Treg cells stop T cell-mediated immunity and suppress auto-reactive T cells that have escaped negative selection within the thymus. Treg cells can also suppress other types of immune cells such as NK cells and B cells. Adaptive Treg cells (called Th3 or Tr1 cells) are thought to be generated during an immune response. Treg cells furthermore play an important role in immune escape by suppressing antitumor immunity, thereby providing an environment of immune tolerance. T cells that recognize cancer cells are often present in large numbers in tumors, but their cytotoxic function is suppressed by nearby immune- suppressor cells. Tregs are abundant in many different cancers, are highly enriched in the tumor microenvironment, and are well known for their role in tumor progression. "Activated Treg cells" express CD4, CD45, FoxP3, CD69 and CCR8, and furthermore have a high expression of CD25, and have a low expression of CD127. CD69 is a T cell activation marker. "CCR8 positive regulatory T cells" or "CCR8+ regulatory T cells" are Tregs expressing CCR8. "CD4conv cells" are conventional CD4+, CD25- T cells. "Gamma delta T cells" are T cells that express a distinctive T-cell receptor, TCRγδ, on their surface. Gamma delta T cells also express CD3. "B cells" are immune cells expressing CD19, and mature B cells express CD20 and CD22. B cells upon activation via CD40 undergo differentiation where somatic hypermutation and enhanced immunoglobulin class switch occur resulting in mature B cells or plasma cells (capable of secreting Abs). B cells are involved in humoral immunity of the adaptive immune system, and are antigen presenting cells. "Macrophages" are immune cells expressing low CD14, high CD16, CD11b, CD68, CD163, and CD206. Macrophages engulf and digest cellular debris, foreign substances, microbes or cancer cells by phagocytosis. Besides phagocytosis, macrophages play a critical role in innate immunity and also help initiate adaptive immunity by recruiting other immune cells. For example, macrophages are important as antigen presenters to T cells. Macrophages that encourage inflammation are called M1 macrophages, whereas those that decrease inflammation and encourage tissue repair are called M2 macrophages. As used herein, "M1 macrophages" are a subset of macrophages expressing ACOD1. M1 macrophages have pro-inflammatory, bactericidal, and phagocytic functions. As used herein, "M2 macrophages" are a subset of macrophages expressing MRC1 (CD206). M2 macrophages secrete anti-inflammatory interleukins, play a role in wound healing and are needed for revascularization and reepithelialization. Tumor-associated macrophages are mainly of the M2 phenotype and seem to actively promote tumor growth. "Dendritic Cells" (DCs) are bone marrow derived leukocytes and are the most potent type of antigen- presenting cells. DCs are specialized to capture and process antigens, converting proteins to peptides that are presented on major histocompatibility complex (MHC) molecules recognized by T cells. As defined herein, DCs are characterized by expression of CD1c, CD14, CD16, CD141, CD11c and CD123. Different subpopulations of Dendritic cells exist. In human, DC1 are immunogenic while DC2 cells are tolerogenic. Mature DC express CD83, while plasmacytoid DC express CD123. "NK cells" (also natural killer cells) are immune cells which express CD45, CD16, CD56, NKG2D, but are CD3 negative. NK cells do not require activation to kill cells that are missing "self" markers of MHC class 1. NCR1 (also referred to as CD335 or NKp46) is expressed on NK cells and on a subset of NKT cells. "Natural killer T (NKT) cells" are a heterogeneous group of T cells that share properties of both T cells and natural killer cells. "iNKT cells" (also "invariant natural killer T cells") express invariant αβ TCR (Vα24-Jα18, CD24lo), CD44hi, NK1.1 (mouse), and NKG2D. The invariant TCR recognizes glycoplipid antigen presented by non-polymorphic MHC class I-like molecule, CD1d. These cells can influence an immune response by rapidly producing large amounts of cytokines, i.e. IFNg. As known in the art, "effector cells" are immune cells that actively support immune response after stimulation. As used herein, effector cells refer to immune cells expressing Fcy receptors and are therefore able to mediate ADCC or ADCP. Non-limiting examples of effector cells are monocytes, neutrophils, mast cells, and, preferably, macrophages, and natural killer cells. "Tertiary lymphoid structures" are intra-tumoral structures characterized by increased expression of LTta, LTtb, Cxcr5 and Cxcl13. The term "chimeric antigen receptor" or "CAR" as used herein, refers to an artificial T cell surface receptor that is engineered to be expressed on an immune effector cell and specifically bind an antigen. CARs may be used as a therapy with adoptive cell transfer. Monocytes are removed from a patient (blood, tumor or ascites fluid) and modified so that they express the receptors specific to a particular form of antigen. In some embodiments, the CARs have been expressed with specificity to a tumor associated antigen. CARs may also comprise an intracellular activation domain, a transmembrane domain and an extracellular domain comprising a tumor associated antigen binding region. In some aspects, CARs comprise fusions of single-chain variable fragments (scFv) derived monoclonal antibodies, fused to CD3- zeta transmembrane and intracellular domain. The specificity of CAR designs may be derived from ligands of receptors (e.g., peptides). In some embodiments, a CAR can target cancers by redirecting a monocyte / macrophage expressing the CAR specific for tumor associated antigens. Dosing schemes are abbreviated as known in the art, e.g. every day (QD), every 2 days (Q2D), or every 3 days (Q3D). EMBODIMENTS ANTIGENS AND ANTIBODIES BINDING CHEMOKINE RECEPTORS ASPECT 1 – ANTIGEN According to a first aspect there is provided an isolated sulfated polypeptide comprising the tyrosine rich domain (TRD) of a seven transmembrane receptor. A tyrosine rich domain is a conserved, N terminal domain, which characterizes seven transmembrane receptors such as CXC and CC chemokine receptors, cf. example 1. As used herein, the term TRD refers to the amino acid or protein sequence of a CXC or CC chemokine receptor which is located N terminal of the first cysteine counted from the N terminus. Besides tyrosine, a TRD typically comprises negatively charged amino acid residues such as aspartic acid. The TRDs for all CC and CXC chemokine receptors are listed in example 4, Table 4.1 for mouse, monkey and human. Tyrosine sulfation is a ubiquitous posttranslational protein modification which occurs in all multicellular organisms. It is catalyzed by tyrosylprotein sulfotransferases (TPSTs) 1 and 2, Golgi-resident enzymes which transfer sulfate from the cofactor PAPS (3'-phosphoadenosine 5'-phosphosulfate) to a context- dependent tyrosine in a protein substrate. Currently, only a small fraction of sulfated proteins is known and the understanding of the biological sulfation mechanisms and specific modification positions is still in progress, cf. example 4. While post-translational modifications, such as glycosylation, phosphorylation, acylation, adenylation, farnesylation, ubiquitination, and sulfation are frequent in proteins of living systems, antibody generation is typically performed based on the unmodified target sequence. The inventors developed an unusual approach for antibody generation, and surprisingly found that the synthetically sulfated polypeptides according to the first aspect could be used to increase both, the success rates for antibody generation for chemokine receptors per se, and also the success rates for chemokine receptor antibodies with superior functional properties for therapeutic uses, as discussed elsewhere herein. The increased success rate for highly specific chemokine receptor antibodies was particularly surprising, because research antibodies which are designed for the sequence independent detection of sulfated tyrosine as a post-translational modification are rare. The seven transmembrane receptor may be from any species expressing chemokine receptors characterized by a TRD, e.g. human, monkey, macaca fascicularis (cynomolgus monkey), macaca mulatta (rhesus macaque), rodent, mouse, rat, horse, bovine, pig, dog, cat and camel. According to some first embodiments of the first aspect, there is provided an isolated polypeptide, wherein the isolated polypeptide comprises the tyrosine rich domain (TRD) of a seven transmembrane receptor, further characterized in that at least 25 %, at least 50 %, or at least 75 % of the tyrosine residues of the TRD are sulfated. For example, in a highly successful antibody campaign, the TRD of human or cynomolgus CCR8 was sulfated at positions Y3, Y15 and Y17, while Y16 was omitted, i.e. 75 % of tyrosines in the TRD were sulfated (Table 6.1). In another example, the TRD of human CCR4 was sulfated at positions 19 and 22 and was used for off-target binding, i.e. 50 % of the tyrosines were sulfated (Table 8.1). In yet another approach, the TRD of murine CCR4 was sulfated at position 22 and used for off target binding, i.e. 25 % of tyrosines in the TRD were sulfated (Table 6.1). Table 4.1 shows a list of sulfated peptides including the preferred positions for tyrosine sulfations. Without being bound by theory, the inventors believe that the introduction of additional charges in the form of tyrosine sulfations tailors the antibody to recognize a specific pattern of negative charges. This recognition seems to require an increased percentage of tyrosines and positively charged amino acids, at least in the HCDR3 of the antibody, i.e., the use of the isolated sulfated polypeptides according to the current invention also influenced the structural composition of the antibodies and in particular the amino acid composition of the HCDR3, cf. example 9. According to some second embodiments of the first aspect, which may be or may not be the same as the first embodiments according to the first aspect, there is provided an isolated polypeptide, wherein the seven transmembrane receptor is human, cynomolgus or mouse. In some of these second embodiments the seven transmembrane receptor is murine. In some preferred of these second embodiments the seven transmembrane receptor is human and / or cynomolgus. In some preferred of these second embodiments the seven transmembrane receptor is human. In some of these second embodiments the seven transmembrane receptor is cynomolgus. According to some third embodiments of the first aspect, which may be or may not be the same as the first and / or second embodiments according to the first aspect, there is provided an isolated polypeptide, wherein the seven transmembrane receptor is a chemokine receptor, preferably a) a CC chemokine receptor such as CCR1, CCR2, CCR3, CCR4, CCR5, CCR6, CCR7, CCR8, CCR9 or CCR10, b) a CXC chemokine receptor such as CXCR1, CXCR2, CXCR3, CXCR4, CXCR5, or CXCR6, or c) CX3CR1 or CXCR1. In some of these third embodiments, the seven transmembrane receptor is a CC chemokine receptor or a CXC chemokine receptor. In some of these third embodiments, the seven transmembrane receptor is a CC chemokine receptor, such as CCR1, CCR2, CCR3, CCR4, CCR5, CCR6, CCR7, CCR8, CCR9 or CCR10. In some preferred of these third embodiments, the seven transmembrane receptor is CCR8 or CCR4. In some highly preferred of these third embodiments, the seven transmembrane receptor is CCR8. In some of these third embodiments, the seven transmembrane receptor is a CXC chemokine receptor, such as CXCR1, CXCR2, CXCR3, CXCR4, CXCR5, or CXCR6. In some of these third embodiments, the seven transmembrane receptor is CX3CR1 or CXCR1. In some preferred embodiments of the first aspect, there is provided an isolated polypeptide which comprises the TRD of a human or cynomolgus seven transmembrane receptor, further characterized in that at least 25 %, at least 50 %, or at least 75 % of the tyrosine residues of the TRD are sulfated, wherein the seven transmembrane receptor is a CC chemokine receptor or a CXC chemokine receptor, and preferably, wherein the seven transmembrane receptor is CCR8 or CCR4. According to some embodiments A of the third embodiments of the first aspect, the isolated sulfated polypeptide comprises a sequence according to or having at least 90 %, 95 % or 98 % sequence identity with a) SEQ ID NO:1 (CCR1_HUMAN_TRD), preferably wherein at least Y10 and / or Y18 have been sulfated, or b) SEQ ID NO:7 (CCR2 HUMAN TRD), preferably wherein at least Y26 has been sulfated, or c) SEQ ID NO:13 (CCR3 HUMAN TRD), preferably wherein Y16 and / or Y17 have been sulfated, or d) SEQ ID NO:19 (CCR4 HUMAN TRD), preferably wherein at least Y22 has been sulfated and preferably furthermore Y16, Y19 and / or Y20 have been sulfated, or e) SEQ ID NO:25 (CCR5 HUMAN TRD), preferably wherein two, three or all of Y3, Y10, Y14 and Y15 have been sulfated, or f) SEQ ID NO:31 (CCR6 HUMAN TRD), preferably wherein at least two or three of Y18, Y26 and Y27 have been sulfated, or g) SEQ ID NO:37 (CCR7 HUMAN TRD), preferably wherein one or both of Y8 and Y17 have been sulfated, or h) SEQ ID NO:43 (CCR8 HUMAN TRD), preferably wherein at least two or all of Y3, Y15 and Y17 have been sulfated, or SEQ ID NO:61 (CCR9_HUMAN_TRD), wherein at least Y28 and preferably also Y17 and / or Y37 have been sulfated, or j) SEQ ID NO:67 (CCR10 HUMAN TRD), preferably wherein at least one or both of Y14 and Y22 have been sulfated, or k) SEQ ID NO:73 (CXCR1 HUMAN TRD), preferably wherein Y27 has been sulfated, or 1) SEQ ID NO:79 (CXCR2 HUMAN TRD), preferably wherein Y23 and / or Y25 have been sulfated, or m) SEQ ID NO:85 (CXCR3 HUMAN TRD), preferably wherein at least one or both of Y27 and Y29 have been sulfated, or n) SEQ ID NO:91 (CXCR4 HUMAN TRD), preferably wherein at least Y12 and / or Y21 have been sulfated, or o) SEQ ID NO:97 (CXCR5 HUMAN TRD), preferably wherein at least one of Y3 and Y27 have been sulfated, or p) SEQ ID NO:103 (CXCR6 HUMAN TRD), preferably wherein at least one or both of Y6 and Y10 has been sulfated, or q) SEQ ID NO:157 (CX3CR1 HUMAN TRD), preferably wherein at least Y14 has been sulfated, or r) SEQ ID NO:163 (CXCR1 HUMAN TRD), preferably wherein at least Y27 has been sulfated. According to some embodiments B of the third embodiments of the first aspect, the isolated sulfated polypeptide comprises a sequence according to or having at least 90 %, 95 % or 98 % sequence identity with a) SEQ ID NO:3 (CCR1_MOUSE_TRD), preferably wherein at least Y10 and / or Y18 have been sulfated, or b) SEQ ID NO:9 (CCR2 MOUSE TRD), preferably wherein at least Y37 and / or Y39 has been sulfated, or c) SEQ ID NO:15 (CCR3 MOUSE TRD), preferably wherein Y20 and / or Y22 has been sulfated, or d) SEQ ID NO:21 (CCR4 MOUSE TRD), preferably wherein at least Y22 has been sulfated and preferably furthermore Y16, Y19 and / or Y20 have been sulfated, or e) SEQ ID NO:27 (CCR5 MOUSE TRD), preferably wherein two or three of Y10, Y12 and Y16 have been sulfated, or f) SEQ ID NO:33 (CCR6 MOUSE TRD), preferably wherein at least two or three of Y13, Y18 and Y19 have been sulfated, g) SEQ ID NO:39 (CCR7 MOUSE TRD), preferably wherein one or both of Y8 and Y17 and optionally Y20 have been sulfated have been sulfated, or h) SEQ ID NO:45 (CCR8 MOUSE TRD), preferably wherein at least two or all of Y3, Y14 and Y15 have been sulfated, or i) SEQ ID NO:63 (CCR9 MOUSE TRD), preferably wherein at least Y28 has been sulfated, and preferably also Y19 has been sulfated, or j) SEQ ID NO:69 (CCR10 MOUSE TRD), preferably wherein at least one, two or all of Y14, Y17 and Y22 has been sulfated, or k) SEQ ID NO:75 (CXCR1 MOUSE TRD), preferably wherein at least Y6 has been sulfated, or 1) SEQ ID NO:81 (CXCR2 MOUSE TRD), preferably wherein Y24 has been sulfated, or m) SEQ ID NO:87 (CXCR3 MOUSE TRD), preferably wherein at least one or both of Y27 and Y29 have been sulfated, or n) SEQ ID NO:93 (CXCR4 MOUSE TRD), preferably wherein at least Y23, Y13 and / or Y14 have been sulfated, or o) SEQ ID NO:99 (CXCR5 MOUSE TRD), preferably wherein at least Y3 and / or Y14 and / or Y20 and / or Y26 have been sulfated, or p) SEQ ID NO:105 (CXCR6 MOUSE TRD), preferably wherein at least one or both of Y11 and Y15 have been sulfated, or q) SEQ ID NO:159 (CX3CR1 MOUSE TRD), preferably wherein at least Y15 has been sulfated, or r) SEQ ID NO:165 (CXCR1 MOUSE TRD), preferably wherein at least Y6 has been sulfated. According to some embodiments C of the third embodiments of the first aspect, the isolated sulfated polypeptide comprises a sequence according to or having at least 90 %, 95 % or 98 % sequence identity with a) SEQ ID NO:2 (CCR1 MACFA TRD), preferably wherein at least Y10 and / or Y18 have been sulfated, or b) SEQ ID NO:8 (CCR2 MACMU TRD), preferably wherein at least Y26 has been sulfated, or c) SEQ ID NO:14 (CCR3 MACFA TRD), preferably wherein Y16 has been sulfated, or d) SEQ ID NO:20 (CCR4_MACFA_TRD), preferably wherein at least Y22 has been sulfated and preferably furthermore Y16, Y19 and / or Y20 have been sulfated, or e) SEQ ID NO:26 (CCR5 MACMU TRD), preferably wherein two, three or all of Y3, Y10, Y14 and Y15 have been sulfated, or f) SEQ ID NO:32 (CCR6 MACFA TRD), preferably wherein at least two or three of Y23, Y31 and Y32 have been sulfated, or g) SEQ ID NO:38 (CCR7 MACFA TRD), preferably wherein one or both of Y8 and Y17 have been sulfated, or h) SEQ ID NO:44 (CCR8 MACFA TRD), preferably wherein at least two or all of Y3, Y15 and Y17 have been sulfated, or 1) SEQ ID NO:62 (CCR9 MACFA TRD), preferably wherein at least Y28, and preferably also Y17 and / or Y37 has been sulfated, or 1) SEQ ID NO:68 (CCR10 MACFA TRD), preferably wherein at least one or both of Y14 and Y22 has been sulfated, or k) SEQ ID NO:74 (CXCR1_MACFA_TRD), preferably wherein at least one of Y14 and Y28 has been sulfated, or 1) SEQ ID NO:80 (CXCR2_MACFA_TRD), preferably wherein Y20 and / or Y22 have been sulfated, or m) SEQ ID NO:86 (CXCR3 MACFA TRD), preferably wherein at least one or both of Y27 and Y29 have been sulfated, or n) SEQ ID NO:92 (CXCR4 MACFA TRD), preferably wherein at least Y12 and / or Y21 have been sulfated, or 0) SEQ ID NO:98 (CXCR5_MACFA_TRD), preferably wherein at least one of Y3 and Y27 have been sulfated, or p) SEQ ID NO:104 (CXCR6 MACFA TRD), preferably wherein at least two or all of Y4, Y7 and Y39 have been sulfated, or q) SEQ ID NO:158 (CX3CR1 MACFA TRD), preferably wherein at least Y20 has been sulfated, or r) SEQ ID NO:164 (CXCR1 MACMU TRD), preferably wherein at least Y14 has been sulfated. In some fourth embodiments of the first aspect, which may be or may not be the same as the first, second and / or third embodiments according to the first aspect, the isolated polypeptide comprises the N terminus of the seven transmembrane receptor including TRD and LID domain, preferably wherein at least the cysteine between the TRD and the LID domain has been removed or has been altered into a different amino acid. The extracellular domains of chemokine receptors can be structured into four regions: (i) an N-terminal domain which can be subdivided into (a) the membrane-distal tyrosine-rich domain (TRD), (b) a cysteine, and (c) a LID domain, (iii) an extracellular domain 1 (ECL1), (iii) an extracellular domain 2 (ECL2), and (iv) an extracellular domain 3 (ECL3). Some of the polypeptides according to the current invention are difficult to handle, e.g. due to a high tendency for aggregation. Without being bound by theory, the inventors believe, that the high "stickiness" results from the increased numbers of charged amino acids and charged sulfate residues. For the polypeptides comprising the N terminus of a chemokine receptor, the aggregation properties could be ameliorated by removal or amino acid exchange of the cysteine between TRD and LID domain. Optimal results were obtained by altering the cysteine into a serine (example 5, Table 4.1). In some of the fourth embodiments according to the first aspect, the cysteine may be omitted and TRD and LID are directly connected. In some different of the fourth embodiments according to the first aspect, the cysteine may be replaced by a different polar uncharged amino acid. In some preferred of the fourth embodiments according to the first aspect, the cysteine is replaced by a serine (cf. Table 4.1). In some of the fourth embodiments according to the first aspect, the cysteine may be replaced by at least one different amino acid. According to some embodiments A of the fourth embodiments of the first aspect, the isolated sulfated polypeptide comprises a sequence according to or having at least 90 %, 95 % or 98 % sequence identity with a) SEQ ID NO:4 (CCR1 HUMAN N term), wherein at least Y10 and / or Y18 have been sulfated, b) SEQ ID NO:10 (CCR2_HUMAN_N term), wherein at least Y26 has been sulfated, c) SEQ ID NO:16 (CCR3_HUMAN_N term), wherein Y16 and / or Y17 have been sulfated, d) SEQ ID NO:22 (CCR4 HUMAN_N term), wherein at least Y22 has been sulfated and preferably furthermore Y16, Y19 and / or Y20 have been sulfated, e) SEQ ID NO:28 (CCR5 HUMAN N term), wherein two, three or all of Y3, Y10, Y14 and Y15 have been sulfated, f) SEQ ID NO:34 (CCR6 HUMAN N term), wherein at least two or three of Y18, Y26 and Y27 have been sulfated, g) SEQ ID NO:40 (CCR7 HUMAN N term), wherein one or both of Y8 and Y17 have been sulfated, h) SEQ ID NO:46 (CCR8 HUMAN N term), wherein at least two or all of Y3, Y15 and Y17 have been sulfated, 1) SEQ ID NO:64 (CCR9 HUMAN N term), wherein at least Y28, and preferably also Y17 and / or Y37 have been sulfated, j) SEQ ID NO:70 (CCR10 HUMAN N term), wherein at least one or both of Y14 and Y22 have been sulfated, k) SEQ ID NO:76 (CXCR1_HUMAN_N term), wherein Y27 has been sulfated, 1) SEQ ID NO:82 (CXCR2 HUMAN N term), wherein Y23 and / or Y25 have been sulfated, m) SEQ ID NO:88 (CXCR3 HUMAN N term), wherein at least one or both of Y27 and Y29 have been sulfated, n) SEQ ID NO:94 (CXCR4 HUMAN N term), wherein at least Y12 and / or Y21 have been sulfated, 0) SEQ ID NO:100 (CXCR5 HUMAN N term), wherein at least one of Y3 and Y27 have been sulfated, or p) SEQ ID NO:106 (CXCR6 HUMAN N term), wherein at least one or both of Y6 and Y10 have been sulfated, or q) SEQ ID NO:160 (CX3CR1 HUMAN N term), preferably wherein at least Y14 has been sulfated, or r) SEQ ID NO:166 (CXCR1_HUMAN_N term), preferably wherein at least Y27 has been sulfated. According to some embodiments B of the fourth embodiments of the first aspect, the isolated sulfated polypeptide comprises a sequence according to or having at least 90 %, 95 % or 98 % sequence identity with a) SEQ ID NO:6 (CCR1 MOUSE N term), preferably wherein at least Y10 and / or Y18 have been sulfated, or b) SEQ ID NO:12 (CCR2 MOUSE N term), preferably wherein at least Y37 and / or Y39 has been sulfated, or c) SEQ ID NO:18 (CCR3 MOUSE N term), preferably wherein Y20 and / or Y22 has been sulfated, or d) SEQ ID NO:24 (CCR4 MOUSE N term), preferably wherein at least Y22 has been sulfated and preferably furthermore Y16, Y19 and / or Y20 have been sulfated, or e) SEQ ID NO:30 (CCR5 MOUSE N term), preferably wherein two or three of Y10, Y12 and Y16 have been sulfated, or f) SEQ ID NO:36 (CCR6 MOUSE N term), preferably wherein at least two or three of Y13, Y18 and Y19 have been sulfated, g) SEQ ID NO:42 (CCR7 MOUSE N term), preferably wherein one or both of Y8 and Y17 and optionally Y20 have been sulfated, or h) SEQ ID NO:48 (CCR8 MOUSE N term with <com:Math><semantics>C=X<annotation encoding="application / x-tex">C = X< / annotation>< / semantics>< / com:Math> or S), preferably wherein at least two or all of Y3, Y14 and Y15 have been sulfated, or i) SEQ ID NO:66 (CCR9 MOUSE N term), preferably wherein at least Y28 has been sulfated, and preferably also Y19 has been sulfated, or j) SEQ ID NO:72 (CCR10 MOUSE N term), preferably wherein at least one, two or all of Y14, Y17 and Y22 has been sulfated, or k) SEQ ID NO:78 (CXCR1_MOUSE_N term), preferably wherein at least Y6 has been sulfated, or 1) SEQ ID NO:84 (CXCR2 MOUSE N term), preferably wherein Y24 has been sulfated, or m) SEQ ID NO:90 (CXCR3 MOUSE N term), preferably wherein at least one or both of Y27 and Y29 have been sulfated, or n) SEQ ID NO:96 (CXCR4_MOUSE_N term), preferably wherein at least Y23 and / or Y14 have been sulfated, or o) SEQ ID NO:102 (CXCR5 MOUSE N term), preferably wherein at least Y3 and / or Y14 and / or Y20 and / or Y26 have been sulfated, or p) SEQ ID NO:108 (CXCR6_MOUSE_N term), preferably wherein at least one or both of Y11 and Y15 have been sulfated, or q) SEQ ID NO:162 (CX3CR1_MOUSE_N term), preferably wherein at least Y15 has been sulfated, or r) SEQ ID NO:168 (CXCR1 MOUSE N term), preferably wherein at least Y6 has been sulfated. According to some embodiments C of the fourth embodiments of the first aspect, the isolated sulfated polypeptide comprises a sequence according to or having at least 90 %, 95 % or 98 % sequence identity with a) SEQ ID NO:5 (CCR1 MACFA N term), preferably wherein at least Y10 and / or Y18 have been sulfated, or b) SEQ ID NO:11 (CCR2 MACMU N term), preferably wherein at least Y26 has been sulfated, or c) SEQ ID NO:17 (CCR3 MACFA N term), preferably wherein Y16 has been sulfated, or d) SEQ ID NO:23 (CCR4 MACFA N term), preferably wherein at least Y22 has been sulfated and preferably furthermore Y16, Y19 and / or Y20 have been sulfated, or e) SEQ ID NO:29 (CCR5 MACMU N term), preferably wherein two, three or all of Y3, Y10, Y14 and Y15 have been sulfated, or f) SEQ ID NO:35 (CCR6 MACFA N term), preferably wherein at least two or three of Y23, Y31 and Y32 have been sulfated, or g) SEQ ID NO:41 (CCR7 MACFA N term), preferably wherein one or both of Y8 and Y17 have been sulfated, or h) SEQ ID NO:47 (CCR8 MACFA N term), preferably wherein at least two or all of Y3, Y15 and Y17 have been sulfated, or i) SEQ ID NO:65 (CCR9 MACFA N term), preferably wherein at least Y28, and preferably also Y17 and / or Y37 have been sulfated, or j) SEQ ID NO:71 (CCR10 MACFA N term), preferably wherein at least one or both of Y14 and Y22 has been sulfated, or k) SEQ ID NO:77 (CXCR1 MACFA N term), preferably wherein at least one of Y14 and Y28 has been sulfated, or 1) SEQ ID NO:83 (CXCR2 MACFA N term), preferably wherein Y20 and / or Y22 have been sulfated, or m) SEQ ID NO:89 (CXCR3_MACFA_N term), preferably wherein at least one or both of Y27 and Y29 have been sulfated, or n) SEQ ID NO:95 (CXCR4 MACFA N term), preferably wherein at least Y12 and / or Y21 have been sulfated, or o) SEQ ID NO:101 (CXCR5_MACFA_N term), preferably wherein at least one of Y3 and Y27 have been sulfated, or p) SEQ ID NO:107 (CXCR6_MACFA_N term), preferably wherein at least two or all of Y4, Y7 and Y39 have been sulfated, or q) SEQ ID NO:161 (CX3CR1 MACFA N term), preferably wherein at least Y20 or Y22 has been sulfated, or r) SEQ ID NO:167 (CXCR1 MACMU N term), preferably wherein at least Y14 or Y28 has been sulfated. In some of the fourth embodiments of the first aspect, the isolated sulfated polypeptide comprises a sequence according to a) SEQ ID NO:4 (CCR1 HUMAN N term), SEQ ID NO:5 (CCR1 MACFA N term), or SEQ ID NO:6 (CCR1 MOUSE N term), preferably wherein at least Y10 and / or Y18 have been sulfated, or b) SEQ ID NO:10 (CCR2_HUMAN_N term), or SEQ ID NO:11 (CCR2_ MACMU_N term), preferably wherein at least Y26 has been sulfated, or c) SEQ ID NO:12 (CCR2 MOUSE N term), preferably wherein at least Y37 and / or Y39 has been sulfated, or d) SEQ ID NO:16 (CCR3 HUMAN N term), preferably wherein Y16 and / or Y17 have been sulfated, or e) SEQ ID NO:17 (CCR3 MACFA N term), preferably wherein Y16 has been sulfated, or f) SEQ ID NO:18 (CCR3 MOUSE N term), preferably wherein Y20 and / or Y22 has been sulfated, or g) SEQ ID NO:22 (CCR4 HUMAN N term), SEQ ID NO:23 (CCR4 MACFA N term), or SEQ ID NO:24 (CCR4 MOUSE N term), preferably wherein at least Y22 has been sulfated and preferably furthermore Y16, Y19 and / or Y20 have been sulfated, or h) SEQ ID NO:28 (CCR5 HUMAN N term), or SEQ ID NO:29 (CCR5 MACMU N term), preferably wherein two, three or all of Y3, Y10, Y14 and Y15 have been sulfated, or i) SEQ ID NO:30 (CCR5 MOUSE N term), preferably wherein two or three of Y10, Y12 and Y16 have been sulfated, or 1) SEQ ID NO:34 (CCR6 HUMAN N term), preferably wherein at least two or three of Y18, Y26 and Y27 have been sulfated, or k) SEQ ID NO:35 (CCR6 MACFA N term), preferably wherein at least two or three of Y23, Y31 and Y32 have been sulfated, or 1) SEQ ID NO:36 (CCR6 MOUSE N term), preferably wherein at least two or three of Y13, Y18 and Y19 have been sulfated, or m) SEQ ID NO:40 (CCR7_HUMAN_N term), or SEQ ID NO:41 (CCR7_MACFA_N term), preferably wherein one or both of Y8 and Y17 have been sulfated, or n) SEQ ID NO:42 (CCR7_MOUSE_N term), preferably wherein one or both of Y8 and Y17 and optionally Y20 have been sulfated have been sulfated, or o) SEQ ID NO:46 (CCR8 HUMAN N term with C = X or S), or SEQ ID NO:47 (CCR8 MACFA N term with <com:Math><semantics>C=X<annotation encoding="application / x-tex">C = X< / annotation>< / semantics>< / com:Math> or S), preferably wherein at least two or all of Y3, Y15 and Y17 have been sulfated, or p) SEQ ID NO:48 (CCR8_MOUSE_N term with C = X or S), preferably wherein at least two or all of Y3, Y14 and Y15 have been sulfated, or q) SEQ ID NO:64 (CCR9 HUMAN N term), or SEQ ID NO:65 (CCR9 MACFA N term), preferably wherein at least Y28, and preferably also Y17 and / or Y37 has been sulfated, or r) SEQ ID NO:66 (CCR9 MOUSE N term), preferably wherein at least Y28 has been sulfated, and preferably also Y19 has been sulfated, or s) SEQ ID NO:70 (CCR10 HUMAN N term), or SEQ ID NO:71 (CCR10 MACFA N term), preferably wherein at least one or both of Y14 and Y22 has been sulfated, or t) SEQ ID NO:72 (CCR10 MOUSE N term), preferably wherein at least one, two or all of Y14, Y17 and Y22 has been sulfated, or u) SEQ ID NO:76 (CXCR1 HUMAN N term), preferably wherein Y27 has been sulfated, or V) SEQ ID NO:77 (CXCR1 MACFA N term), preferably wherein at least one of Y14 and Y28 has been sulfated, or w) SEQ ID NO:78 (CXCR1 MOUSE N term), preferably wherein at least Y6 has been sulfated, or x) SEQ ID NO:82 (CXCR2 HUMAN N term), preferably wherein Y23 and / or Y25 have been sulfated, or y) SEQ ID NO:83 (CXCR2_MACFA_N term), preferably wherein Y20 and / or Y22 have been sulfated, or z) SEQ ID NO:84 (CXCR2 MOUSE N term), preferably wherein Y24 has been sulfated, or aa) SEQ ID NO:88 (CXCR3 HUMAN N term), SEQ ID NO:89 (CXCR3 MACFA N term), or SEQ ID NO:90 (CXCR3 MOUSE N term), preferably wherein at least one or both of Y27 and Y29 have been sulfated, or bb) SEQ ID NO:94 (CXCR4 HUMAN N term), or SEQ ID NO:95 (CXCR4 MACFA N term), preferably wherein at least Y12 and / or Y21 have been sulfated, or cc) SEQ ID NO:96 (CXCR4 MOUSE N term), preferably wherein at least Y23 and / or Y14 have been sulfated, or dd) SEQ ID NO:100 (CXCR5_HUMAN_N term), or SEQ ID NO:101 (CXCR5_MACFA_N term), preferably wherein at least one of Y3 and Y27 have been sulfated, or ee) SEQ ID NO:102 (CXCR5 MOUSE N term), preferably wherein at least Y3 and / or Y14 and / or Y20 and / or Y26 have been sulfated, or ff) SEQ ID NO:106 (CXCR6_HUMAN_N term), preferably wherein at least one or both of Y6 and Y10 has been sulfated, or gg) SEQ ID NO:107 (CXCR6 MACFA N term), preferably wherein at least two or all of Y4, Y7 and Y39 have been sulfated, or hh) SEQ ID NO:108 (CXCR6 MOUSE N term), preferably wherein at least one or both of Y11 and Y15 have been sulfated, or ii) SEQ ID NO:160 (CX3CR1 HUMAN N term), preferably wherein at least Y14 has been sulfated, or JJ) SEQ ID NO:161 (CX3CR1 MACFA N term), preferably wherein at least Y20 or Y22 has been sulfated, or kk) SEQ ID NO:162 (CX3CR1_MOUSE_N term), preferably wherein at least Y15 has been sulfated, or 11) SEQ ID NO:166 (CXCR1 HUMAN N term), preferably wherein at least Y27 has been sulfated, or mm) SEQ ID NO:167 (CXCR1 MACMU N term), preferably wherein at least Y14 or Y28 has been sulfated, or nn) SEQ ID NO:168 (CXCR1 MOUSE N term), preferably wherein at least Y6 has been sulfated. In some of the first, second, third or fourth embodiments of the first aspect, the isolated sulfated polypeptide comprises a sequence according to or having at least 90 % sequence identity with a) SEQ ID NO:1 (CCR1 HUMAN TRD), SEQ ID NO:4 (CCR1 HUMAN N term), SEQ ID NO:2 (CCR1 MACFA_TRD), SEQ ID NO:5 (CCR1_MACFA_N term), SEQ ID NO:3 (CCR1 MOUSE TRD) or SEQ ID NO:6 (CCR1 MOUSE N term), preferably wherein at least Y10 and / or Y18 have been sulfated, or b) SEQ ID NO:7 (CCR2 HUMAN TRD), SEQ ID NO:10 (CCR2 HUMAN N term), SEQ ID NO:8 (CCR2 MACMU TRD) or SEQ ID NO:11 (CCR2 MACMU N term), preferably wherein at least Y26 has been sulfated, or c) SEQ ID NO:9 (CCR2 MOUSE TRD) or SEQ ID NO:12 (CCR2 MOUSE N term), preferably wherein at least Y37 and / or Y39 has been sulfated, or d) SEQ ID NO:13 (CCR3 HUMAN TRD) or SEQ ID NO:16 (CCR3 HUMAN N term), preferably wherein Y16 and / or Y17 have been sulfated, or e) SEQ ID NO:14 (CCR3 MACFA TRD) or SEQ ID NO:17 (CCR3 MACFA N term), preferably wherein Y16 has been sulfated, or f) SEQ ID NO:15 (CCR3_MOUSE_TRD) or SEQ ID NO:18 (CCR3_MOUSE_N term), preferably wherein Y20 and / or Y22 have been sulfated, or g) SEQ ID NO:19 (CCR4 HUMAN TRD), SEQ ID NO:22 (CCR4 HUMAN N term), SEQ ID NO:20 (CCR4 MACFA TRD), SEQ ID NO:23 (CCR4 MACFA N term), SEQ ID NO:21 (CCR4 MOUSE TRD) or SEQ ID NO:24 (CCR4_MOUSE_N term), preferably wherein at least Y22 has been sulfated and preferably furthermore Y16, Y19 and / or Y20 have been sulfated, or h) SEQ ID NO:25 (CCR5 HUMAN TRD), SEQ ID NO:28 (CCR5 HUMAN N term), SEQ ID NO:26 (CCR5 MACMU TRD) or SEQ ID NO:29 (CCR5 MACMU N term), preferably wherein two, three or all of Y3, Y10, Y14 and Y15 have been sulfated, or i) SEQ ID NO:27 (CCR5 MOUSE TRD) or SEQ ID NO:30 (CCR5 MOUSE N term), preferably wherein two or three of Y10, Y12 and Y16 have been sulfated, or j) SEQ ID NO:31 (CCR6 HUMAN TRD) or SEQ ID NO:34 (CCR6 HUMAN N term), preferably wherein at least two or three of Y18, Y26 and Y27 have been sulfated, or k) SEQ ID NO:32 (CCR6 MACFA TRD) or SEQ ID NO:35 (CCR6 MACFA N term), preferably wherein at least two or three of Y23, Y31 and Y32 have been sulfated, or 1) SEQ ID NO:33 (CCR6 MOUSE TRD) or SEQ ID NO:36 (CCR6 MOUSE N term), preferably wherein at least two or three of Y13, Y18 and Y19 have been sulfated, or m) SEQ ID NO:37 (CCR7 HUMAN TRD), SEQ ID NO:40 (CCR7 HUMAN N term), SEQ ID NO:38 (CCR7_MACFA_TRD) or SEQ ID NO:41 (CCR7_MACFA_N term), preferably wherein one or both of Y8 and Y17 have been sulfated, or n) SEQ ID NO:39 (CCR7 MOUSE TRD) or SEQ ID NO:42 (CCR7 MOUSE N term), preferably wherein one or both of Y8 and Y17 and optionally Y20 have been sulfated have been sulfated, or o) SEQ ID NO:43 (CCR8 HUMAN TRD), SEQ ID NO:44 (CCR8 MACFA TRD), SEQ ID NO:46 (CCR8 HUMAN N term with <com:Math><semantics>C=X<annotation encoding="application / x-tex">C = X< / annotation>< / semantics>< / com:Math> or S), or SEQ ID NO:47 (CCR8 MACFA N term with <com:Math><semantics>C=X<annotation encoding="application / x-tex">C = X< / annotation>< / semantics>< / com:Math> or S), preferably wherein at least two or all of Y3, Y15 and Y17 have been sulfated, or p) SEQ ID NO:45 (CCR8 MOUSE TRD) or SEQ ID NO:48 (CCR8 MOUSE N term with C = X or S), preferably wherein at least two or all of Y3, Y14 and Y15 have been sulfated, or q) SEQ ID NO:61 (CCR9 HUMAN TRD), SEQ ID NO:64 (CCR9 HUMAN N term), SEQ ID NO:62 (CCR9 MACFA TRD) or SEQ ID NO:65 (CCR9 MACFA N term), preferably wherein at least Y28, and preferably also Y17 and / or Y37 has been sulfated, or r) SEQ ID NO:63 (CCR9 MOUSE TRD) or SEQ ID NO:66 (CCR9 MOUSE N term), preferably wherein at least Y28 has been sulfated, and preferably also Y19 has been sulfated, or s) SEQ ID NO:67 (CCR10 HUMAN TRD), SEQ ID NO:70 (CCR10 HUMAN N term), SEQ ID NO:68 (CCR10 MACFA TRD) or SEQ ID NO:71 (CCR10_MACFA_N term), preferably wherein at least one or both of Y14 and Y22 has been sulfated, or t) SEQ ID NO:69 (CCR10_MOUSE_TRD) or SEQ ID NO:72 (CCR10_MOUSE_N term), preferably wherein at least one, two or all of Y14, Y17 and Y22 has been sulfated, or u) SEQ ID NO:73 (CXCR1_HUMAN_TRD) or SEQ ID NO:76 (CXCR1_HUMAN N term), preferably wherein Y27 has been sulfated, or v) SEQ ID NO:74 (CXCR1 MACFA TRD) or SEQ ID NO:77 (CXCR1 MACFA N term), preferably wherein at least one of Y14 and Y28 has been sulfated, or w) SEQ ID NO:75 (CXCR1_MOUSE_TRD) or SEQ ID NO:78 (CXCR1_MOUSE_N term), preferably wherein at least Y6 has been sulfated, or x) SEQ ID NO:79 (CXCR2_HUMAN_TRD) or SEQ ID NO:82 (CXCR2 HUMAN N term), preferably wherein Y23 and / or Y25 have been sulfated, or y) SEQ ID NO:80 (CXCR2_MACFA _TRD) or SEQ ID NO:83 (CXCR2_MACFA_N term), preferably wherein Y20 and / or Y22 have been sulfated, or z) SEQ ID NO:81 (CXCR2 MOUSE TRD) or SEQ ID NO:84 (CXCR2 MOUSE N term), preferably wherein Y24 has been sulfated, or aa) SEQ ID NO:85 (CXCR3 HUMAN TRD), SEQ ID NO:88 (CXCR3 HUMAN N term), SEQ ID NO:86 (CXCR3 MACFA TRD), SEQ ID NO:89 (CXCR3 MACFA N term), SEQ ID NO:87 (CXCR3 MOUSE TRD) or SEQ ID NO:90 (CXCR3_MOUSE_N term), preferably wherein at least one or both of Y27 and Y29 have been sulfated, or bb) SEQ ID NO:91 (CXCR4 HUMAN TRD), SEQ ID NO:94 (CXCR4 HUMAN N term), SEQ ID NO:92 (CXCR4_MACFA_TRD) or SEQ ID NO:95 (CXCR4_MACFA_N term), preferably wherein at least Y12 and / or Y21 have been sulfated, or cc) SEQ ID NO:93 (CXCR4 MOUSE TRD) or SEQ ID NO:96 (CXCR4 MOUSE N term), preferably wherein at least Y23 and / or Y14 have been sulfated, or dd) SEQ ID NO:97 (CXCR5_HUMAN_TRD), SEQ ID NO:100 (CXCR5_HUMAN_N term), SEQ ID NO:98 (CXCR5_MACFA_TRD) or SEQ ID NO:101 (CXCR5_MACFA_N term), preferably wherein at least one of Y3 and Y27 have been sulfated, or ee) SEQ ID NO:99 (CXCR5 MOUSE TRD) or SEQ ID NO:102 (CXCR5 MOUSE N term), preferably wherein at least Y3 and / or Y14 and / or Y20 and / or Y26 have been sulfated, or ff) SEQ ID NO:103 (CXCR6 HUMAN TRD) or SEQ ID NO:106 (CXCR6 HUMAN N term), preferably wherein at least one or both of Y6 and Y10 has been sulfated, or gg) SEQ ID NO:104 (CXCR6 MACFA TRD) or SEQ ID NO:107 (CXCR6 MACFA N term), preferably wherein at least two or all of Y4, Y7 and Y39 have been sulfated, or hh) SEQ ID NO:105 (CXCR6 MOUSE TRD) or SEQ ID NO:108 (CXCR6 MOUSE N term), preferably wherein at least one or both of Y11 and Y15 have been sulfated, or ii) SEQ ID NO:157 (CX3CR1 HUMAN TRD) or SEQ ID NO:160 (CX3CR1 HUMAN N term), preferably wherein at least Y14 has been sulfated, or jj) SEQ ID NO:158 (CX3CR1 MACFA TRD), preferably wherein at least Y20 has been sulfated, or kk) SEQ ID NO:161 (CX3CR1_MACFA_N term), preferably wherein at least Y20 or Y22 has been sulfated, or II) SEQ ID NO:159 (CX3CR1 MOUSE TRD) or SEQ ID NO:162 (CX3CR1 MOUSE N term), preferably wherein at least Y15 has been sulfated, or mm) SEQ ID NO:163 (CXCR1 HUMAN TRD) or SEQ ID NO:166 (CXCR1 HUMAN N term), preferably wherein at least Y27 has been sulfated, or nn) SEQ ID NO:164 (CXCR1_MACMU_TRD), preferably wherein at least Y14 has been sulfated or oo) SEQ ID NO:167 (CXCR1 MACMU N term), preferably wherein at least Y14 or Y28 has been sulfated, or pp) SEQ ID NO:165 (CXCR1_MOUSE_TRD) or SEQ ID NO:168 (CXCR1_MOUSE_N term), preferably wherein at least Y6 has been sulfated. Preferably, the isolated polypeptide according to the current aspect is immobilized, e.g. via a linker. Immobilization may occur without limitation on suitable beads, particles, proteins, or solid supports. ASPECT 2 – CONJUGATE COMPRISING ISOLATED POLYPEPTIDE According to a second aspect of the current invention, there is provided a conjugate comprising an isolated sulfated polypeptide according to the first aspect. For example, the conjugate may comprise a polypeptide according to the first embodiments of the first aspect. For example, the conjugate may comprise a polypeptide according to the second embodiments of the first aspect. For example, the conjugate may comprise a polypeptide according to the third embodiments of the first aspect. For example, the conjugate may comprise a polypeptide according to some embodiments A, B, C of the third embodiments of the first aspect. For example, the conjugate may comprise a polypeptide according to the fourth embodiments of the first aspect. For example, the conjugate may comprise a polypeptide according to some embodiments A, B, C of the fourth embodiments of the first aspect. For example, the isolated sulfated polypeptide may be attached to a tag or linker for immobilization or retrieval. Suitable tags are selected from the tags known in the art, for example small organic molecules like biotin (which binds strongly and non-covalently to streptavidin), derivatives thereof, or short peptide sequence such as Flag tag, HA tag, Myc tag or His tag (cf. Table 4.1 or example 10.1.2). For some applications, the tag can be a protein, such as human serum albumin (cf. Table 4.1 or example 10.1.2), or a carrier protein, such as KLH, OVA or BSA, or a larger structure such as a bead or magnetic particle. Preferably, the tag can be attached via the C term or at the N term of the TRD or the N terminus of the chemokine receptor but may also be attached via a reactive residue or amino acid side chain, such as a lysine within the TRD. In some embodiments, the tag is attached via a linker, which can be any linker known in the art. Suitable linker include trioxatridecan-succinamic acid (Ttds) linker (cf. Table 4.1), beta- alanine, GABA, AEA, Ava, Ahx, PEG2 spacer, PEG3 spacer, PEG4 spacer, O1Pen, O2Oc or O1Pen-O1. ASPECT 3 – ANTIGEN PRODUCTION METHOD Sulfated peptides may be difficult to synthesize e.g. because the sulfate is unstable under acidic conditions (Houben-Weyl, Methods of Organic Chemistry Vol. E 22b, Synthesis of Peptides and Peptidomimetics, 4th Edition, section 6.6.1.2 Synthesis of Sulfated Tyrosine Peptides with Tyrosine O-Sulfate Synthons, p.440 ff. in: Felix, Arthur et al.:2004). According to a 3rd aspect there is provided a method for production of the isolated sulfated polypeptide according to the first aspect or conjugate according to the second aspect, wherein the method comprises synthesis of the isolated polypeptide and sulfation of the respective tyrosine residues. Synthesis of the isolated polypeptide according to the first aspect and sulfation of the respective tyrosine residues may occur as described in example 5, or may occur according to any other method known in the art. In chapter 6.6.1 "Methods of Organic Chemistry Vol. E 22b, Synthesis of Peptides and Peptidomimetics", Houben-Weyl describe various chemical approaches for the synthesis of sulfated tyrosine peptides. The chapter, and in particular these methods, are referenced in their entirety. For example, synthesis may be performed using the sequence independent solid phase method previously described by Bunschoten et al. (Bunschoten, Anton, et al. "A general sequence independent solid phase method for the site specific synthesis of multiple sulfated-tyrosine containing peptides." Chemical communications 21 (2009): 2999-3001.). In brief, a peptide is synthesized according to the Fmoc-tBu-strategy, followed by selective deprotection of the tyrosine residues to be sulfated and introduction of a protected sulfate group. Upon completion of the synthesis of the sulfated peptide, it is cleaved from the resin by acidolysis and protection groups are removed with the exception of the sulfate protection group, thereby preventing undesired acid induced removal of the sulfate group(s) during this step. Finally, the sulfate protecting groups can be removed in a slightly acidic reductive step, leaving the sulfate groups untouched. Chen et al. have reported a short and efficient one-step route to sY-containing peptides, wherein Fmoc- protected fluorosulfated tyrosine (Y(OSO2F)) is incorporated into the peptide of interest through an Fmoc- based solid-phase synthetic strategy (cf. Chen, Wentao, et al. "Synthesis of Sulfotyrosine-Containing Peptides by Incorporating Fluorosulfated Tyrosine Using an Fmoc-Based Solid-Phase Strategy." Angewandte Chemie 128.5 (2016): 1867-1870.). Standard simultaneous peptide-resin cleavage and removal of the acid-labile side-chain protecting groups yield the crude peptides containing fluorosulfated tyrosine. Basic ethylene glycol, serving as solvent and reactant, transforms the fluorosulfated tyrosine peptides into sulfotyrosine peptides in high yield. Global sulfation of polypeptides is likewise possible, for example using sulfur trioxide-pyridine. According to the current invention, this route can be used, if all tyrosines have to be sulfated or if "crude" mixtures of partially sulfated polypeptides shall be used for further steps. Furthermore, sulfation may occur enzymatically, e.g. in a biotransformation reaction using the natural sulfation enzymes or engineered versions thereof. Preferably, the sulfation of the respective tyrosine may occur chemically or enzymatically. Preferably, the synthesis of the isolated polypeptide occurs using Fmoc-tBu-strategy. According to some embodiments of the 3rd aspect, the method comprises purifying the obtained polypeptides. Purification may occur for example by HPLC, e.g. using a C18 column. According to some embodiments of the 3rd aspect, the method comprises analytical characterization of the polypeptide. Without limitation, analytical characterization may be performed using spectroscopic methods or mass spectrometry. ASPECT 4 – USES OF THE ANTIGEN / METHODS COMPR. USE OF THE ANTIGEN According to a 4<com:Sup>th< / com:Sup> aspect there is provided the use of the isolated sulfated polypeptide according to the first aspect or conjugate according to the second aspect for antibody generation, as antigen or for off-target panning, and / or for characterization of an antibody. For example, the isolated sulfated polypeptide according to the first aspect or conjugate according to the second aspect can be used for the generation of a fully human antibody or a fragment thereof. For example, the isolated sulfated polypeptide according to the first aspect or conjugate according to the second aspect can be used for the generation of a cross reactive antibody. According to some first embodiments according to the 4<com:Sup>th< / com:Sup> aspect, there is provided the use of the isolated sulfated polypeptide according to the first aspect or conjugate according to the second aspect for antibody generation. In particular, the isolated sulfated polypeptide according to the first aspect may be used to facilitate the generation of antibodies specifically recognizing chemokine receptors, as described elsewhere herein. According to some second embodiments according to the 4<com:Sup>th< / com:Sup> aspect, which may be the same as or different from the first embodiments according to the 4<com:Sup>th< / com:Sup> aspect, the isolated sulfated polypeptide according to the first aspect or conjugate according to the second aspect is used as antigen, e.g. to select antibodies, antibody fragments or molecules specifically binding to chemokine receptors, cf examples 6 and 8. According to some third embodiments according to the 4th aspect, which may be the same as or different from the first and / or second embodiments according to the 4<com:Sup>th< / com:Sup> aspect, the isolated sulfated polypeptide according to the first aspect or conjugate according to the second aspect is used for off-target panning to select antibodies which do not bind a certain seven transmembrane receptor, e.g. a chemokine receptor (off-target receptor), cf examples 6 and 8. According to some fourth embodiments, the method according to the 4<com:Sup>th< / com:Sup> aspect comprises the use of the isolated sulfated polypeptide according to the first aspect or conjugate according to the second aspect for characterization of an antibody. Preferably, the antibody is an antibody according to the current invention. For example, the characterization of the antibody may comprise the use of ELISA, surface plasmon resonance, mass spectrometry, competition assays, staining, IHC, FACS, or various further assays known in the art. ASPECT 5 – ANTIBODY PRODUCTION METHOD According to a 5<com:Sup>th< / com:Sup> aspect, there is provided a method for obtaining an antibody or binder, the method comprising the use of the isolated sulfated polypeptide according to the first aspect or conjugate according to the second aspect. According to some first embodiments, the method according to the 5th aspect comprises the use of the isolated sulfated polypeptide according to the first aspect or conjugate according to the second aspect as antigen. According to some preferred of the first embodiments of the 5<com:Sup>th< / com:Sup> aspect, the method comprises the use of at least one further isolated polypeptide or conjugate thereof, wherein the at least one further isolated polypeptide comprises a TRD a) of a seven transmembrane receptor different from the first seven transmembrane receptor, or b) of the first seven transmembrane receptor derived from a different species, preferably wherein the at least one further isolated polypeptide is an isolated polypeptide according to the first aspect. According to some embodiments A of the first embodiments of the 5<com:Sup>th< / com:Sup> aspect, the method comprises the use of at least one further isolated polypeptide or conjugate, preferably according to the first or second aspect, preferably either as antigen or for off-target selection. For these embodiments, the first isolated sulfated polypeptide comprises a TRD of a first seven transmembrane receptor (e.g. a chemokine receptor) and the further isolated polypeptide or conjugate comprises a TRD of a seven transmembrane receptor different from the first seven transmembrane receptor. Where the further isolated polypeptide or conjugate is used as antigen, the method is a method for the production of antibodies or binders recognizing at least two different seven transmembrane receptors, e.g. two different chemokine receptor family members. Where the further isolated polypeptide or conjugate is used for off target panning, the method is a method for the production of antibodies or binders recognizing only a specific seven transmembrane receptor, e.g. to avoid off target binding to the further chemokine receptor family members. According to some embodiments B of the first embodiments of the 5<com:Sup>th< / com:Sup> aspect, the method comprises the use of at least one further isolated polypeptide or conjugate, preferably according to the first or second aspect, either as antigen or for off-target selection. For these embodiments, the first isolated polypeptide comprises a TRD of a first seven transmembrane receptor of a first species (e.g. a human chemokine receptor) and the further isolated polypeptide comprises a TRD of the same seven transmembrane receptor derived from a different species (e.g. a cynomolgus chemokine receptor). For example, the first polypeptide may comprise the TRD of a human chemokine receptor, and the second polypeptide may comprise the TRD of a cynomolgus chemokine receptor. These embodiments B are of particular advantage, because the generation of chemokine receptor antibodies or binders which are cross reactive for both human and a suitable model species is difficult for chemokine receptors, in particular for CCR8. While the overall consensus between the transmembrane domains is comparably high, the extracellular domains of chemokine receptors have a low consensus between the different chemokine receptor family members, and also between the species for a given chemokine receptor (Fig. 1, Fig. 2 a). However, according to the current invention it was now found, that small sulfated tyrosine comprising motifs within the TRD are sufficiently conserved for a given chemokine receptor to be used to obtain high numbers of cross-reactive antibodies. Example 6 describes the generation of cross-reactive antibodies for human and cynomolgus, and example 10.1.1 shows excellent affinities in both species for various antibodies according to the current invention. Compared with rodents and mice, cynomolgus is a preferred model system, because mouse models have failed to predict immunological side effects. The method according to the 5<com:Sup>th< / com:Sup> aspect may be any method for antibody generation known in the art. For example, the method may be a conventional immunization method, e.g. wherein the polypeptide according to the first aspect is conjugated to KLH and is administered to a suitable animal for immunization. For example, after immunization, the splenocytes of the immunized animals can be used for the generation of hybridoma cells, which produce the antibodies of the animals, and in a second step can be screened for antibodies specifically binding to the antigen by methods known in the art like e.g. ELISA as well as binding to an off-target, if applicable. Alternatively, the splenocytes can be directly screened for the production of antibodies binding to the antigen in droplet based microfluidic systems or in cell culture assays. Afterwards only selected splenocytes are directly applied to sequencing to obtain the sequence of the antibody or hybridoma generation. Another method can comprise using the antigen for panning with an antibody library which for example can be a phage display library, e.g. without limitation as described elsewhere herein, or alternatively a mammalian library. After panning of the library on the antigen the enriched antibodies can be screened for specific binding to the antigen by methods known in the art like e.g. ELISA or SPR, as described in more detail herein. According to some second embodiments of the 5<com:Sup>th< / com:Sup> aspect, which may be the same as or different from the first embodiments of the 5<com:Sup>th< / com:Sup> aspect, the method for obtaining an antibody according to the 5<com:Sup>th< / com:Sup> aspect, is a method comprising the use of a phage display library, a transgenic animal, or any other technique available in the art for the generation of antibodies comprising human CDRs. In some embodiments A of the second embodiments of the 5<com:Sup>th< / com:Sup> aspect, the method comprises the use of a human phage display library, cf. example 6 and example 8. For example, the phage display library can be a fully human antibody phage display library, such as the BioInvent n-CoDeR Fab lambda library. In some preferred embodiments, the Phage display library is enriched for tyrosine and / or histidine content. In a first step, the phage display library comprising bacteriophages displaying antibodies or antibody fragments on their outside may be combined with the immobilized isolated polypeptide according to the first aspect or conjugate according to the second aspect to allow binding to the isolated polypeptide or conjugate. In an optional second depletion step, which may occur before or after the first step, the phage display library comprising bacteriophages displaying antibodies or antibody fragments on their outside may be combined with an immobilized isolated polypeptide or conjugate according to the first aspect, being different from the isolated polypeptide of the first step, to deplete off-target binders. In an optional third step, which may occur before or after the first step, or may occur before or after the second step, the phage display library comprising bacteriophages displaying antibodies or antibody fragments on their outside may be combined with an immobilized isolated polypeptide according to the first aspect or conjugate according to the second aspect being different from the isolated polypeptide of the first step and from the isolated polypeptide of the optional second step, to obtain cross reactive binders. Each of the steps may be repeated multiple times, e.g. one, two, three, four, five, six, seven eight, nine, ten or more times. Binding antibodies or fragments can be retrieved for expansion by infection of suitable bacterial hosts and the DNA can be sequenced as known in the art to obtain the sequence of the seven transmembrane receptor antibody or fragment. In some embodiments B of the second embodiments of the 5<com:Sup>th< / com:Sup> aspect, the method for obtaining an antibody according to the 5th aspect, is a method comprising the use of transgenic animals as described by Lonberg (Lonberg, Nils. "Human antibodies from transgenic animals." Nature biotechnology 23.9 (2005): 1117-1125.). For example, the transgenic animal may be a XenoMouse (Abgenix Inc., Fremont, CA, e.g. U.S. Patent No. 5,939,598), the HuMAb Mouse (GenPharm-Medarex, San Jose, CA), the RenMab Mouse (Biocytogen), or any other animal known in the art for the generation of fully human antibodies. In some embodiments C of the second embodiments of the 5<com:Sup>th< / com:Sup> aspect, the method for obtaining an antibody according to the 5th aspect, is a method comprising the use of in vitro activated B cells (see, U.S. Pat. Nos. 5,567,610 and 5,229,275). According to some third embodiments of the 5<com:Sup>th< / com:Sup> aspect there is provided a method for obtaining an antibody or antibody fragment or a binder, which specifically binds to a human and / or cynomolgus and / or murine CC or CXC chemokine receptor, the method comprising a) (synthetically) sulfating a polypeptide comprising a tyrosine rich domain (TRD) and b) selection of an antibody, antibody fragment or binder recognizing the sulfated polypeptide, and c) optionally producing the antibody, antibody fragment or binder. In some embodiments, the use according to the 4<com:Sup>th< / com:Sup> aspect, or the method according to the 5<com:Sup>th< / com:Sup> aspect is a use / method to obtain an antibody with favorable properties as described elsewhere herein, preferably wherein the antibody a) comprises human derived CDRs, and / or b) is a human, rat or murine IgG antibody, preferably a human IgG1 antibody or a murine IgG2a antibody, and / or c) is cross reactive for two different seven transmembrane receptors, and / or d) is cross reactive for a human and a cynomolgus seven transmembrane receptor, and / or e) is characterized by a HCDR3 region comprising between 10 and 34 % of tyrosine and / or between 2 and 20 % of histidine, preferably between 7 and 20 % of histidine and / or f) does not modulate G protein independent signaling of the chemokine receptor, and / or g) is a non-internalizing antibody or is characterized by an internalization into a cell with endogenous target expression which is lower than the 1.5, 2, 3, 4, 5, 6, 7, or 10-fold of the internalization of the isotype control. The method according to the current aspect can be used to obtain high numbers of antibodies binding chemokine receptors. Interestingly, a comparably high number of these antibodies were characterized by properties differentiating them from the known antibodies obtained with conventional methods as described elsewhere herein. ASPECT 6 – ANTIBODY DEFINED BY ANTIGEN According to the current invention, there is provided an isolated antibody or antigen-binding fragment thereof or a binder obtained with a method or use according to a previous aspect. As will be appreciated by skilled artisans, antibodies and / or binding fragments are "modular" in nature. Throughout the disclosure, various specific aspects and embodiments of the various "modules" composing the antibodies and / or binding fragments are described. As specific non-limiting examples, various specific embodiments of VH CDRs, VH chains, VL CDRs and VL chains or functional features are described. It is intended that all of the specific embodiments may be combined with each other as though each specific combination were explicitly described individually. As specific non-limiting examples, various specific functional embodiments are described. It is intended that all of the specific embodiments may be combined with each other as though each specific combination were explicitly described individually. According to a 6<com:Sup>th< / com:Sup> aspect, there is provided an isolated antibody or antigen-binding fragment thereof, (specifically) binding to a first isolated sulfated polypeptide which comprises the tyrosine rich domain (TRD) of a seven transmembrane receptor, wherein at least 25 %, at least 50 % or at least 75 % of the tyrosine residues of the TRD are sulfated. Preferably, the first isolated sulfated polypeptide furthermore comprises the LID domain of the seven transmembrane receptor. Preferably, the cysteine between the TRD and the LID domain has been removed or has been exchanged into a different amino acid. Preferably, the first isolated sulfated polypeptide comprises the N terminus of a seven transmembrane receptor including its tyrosine rich domain (TRD) and optionally including its LID domain, and even more preferably, at least 25 %, at least 50 % or at least 75 % of the tyrosine residues of the TRD are sulfated. In preferred embodiments, the isolated antibody or antigen-binding fragment thereof binds its target(s) with a KD value of < 5E-8 M, < 4E-8 M, < 3E-8 M, < 2E-8 M, < 1E-8 M, < 9E-9 M, < 8E-9 M, < 7E-9 <com:Math><semantics>Ms<6E−9Ms<5E−9Ms<4E−9Ms<3E−9Ms<2.5E−9Ms<2E−9Ms<1.5E−9Ms<1E−9Ms<9E−10<annotation encoding="application / x-tex">M_{s} < 6E-9 M_{s} < 5E-9 M_{s} < 4E-9 M_{s} < 3E-9 M_{s} < 2.5E-9 M_{s} < 2E-9 M_{s} < 1.5E-9 M_{s} < 1E-9 M_{s} < 9E-10< / annotation>< / semantics>< / com:Math> M, < 8E-10 M, < 7E-10 M, < 6E-10 M, < 5E-10 M, < 4E-10 M, < 3E-10 M, < 2.5E-10 M, < 2E-10 M, < 1.5E-10 M, < 1E-10 M, or < 9E-11 M. For example, the inventive antibody may bind its target(s) with a KD value between < 8E-9 M and > 4E-10 M. Where the isolated antibody or antigen-binding fragment thereof binds more than one target, most preferably it binds its' targets with an affinity in the same order of magnitude. According to some preferred embodiments, the isolated antibody or antigen-binding fragment thereof a) comprises human derived CDRs, and / or b) is cross reactive for human and cynomolgus, and / or c) is characterized by a HCDR3 region comprising between 10 and 34 % of tyrosine and / or between 7 and 20 % of histidine, and / or d) does not modulate G protein independent signaling of the seven transmembrane receptor, and / or e) is a non-internalizing antibody or is characterized by an internalization into a cell with endogenous target expression which is lower than the 1.5, 2, 3, 4, 5, 6, 7, or 10-fold of the internalization of the isotype control, and / or f) induces ADCC and / or ADCP and / or g) is a human, rat or murine IgG antibody, preferably a human IgG1 antibody or a murine IgG2a antibody, and / or h) is an scFv, Fab, Fab' or a F(ab')2 fragment. According to some first embodiments of the 6<com:Sup>th< / com:Sup> aspect, the seven transmembrane receptor is a chemokine receptor. In some of these first embodiments, the seven transmembrane receptor is a CC chemokine receptor or a CXC chemokine receptor. In some of these first embodiments, the seven transmembrane receptor is a CC chemokine receptor, such as CCR1, CCR2, CCR3, CCR4, CCR5, CCR6, CCR7, CCR8, CCR9 or CCR10. In some preferred of these first embodiments, the seven transmembrane receptor is CCR8 or CCR4. In some most preferred of these first embodiments, the seven transmembrane receptor is CCR8. In some of the first embodiments, the seven transmembrane receptor is a CXC chemokine receptor, such as CXCR1, CXCR2, CXCR3, CXCR4, CXCR5, or CXCR6. In some of the first embodiments, the seven transmembrane receptor is CX3CR1 or CXCR1. According to some second embodiments of the <com:Math><semantics>6th<annotation encoding="application / x-tex">6^{th}< / annotation>< / semantics>< / com:Math> aspect, which may or may not be the same as the first embodiments of the 6<com:Sup>th< / com:Sup> aspect, the seven transmembrane receptor may be from any species expressing chemokine receptors characterized by a TRD, e.g. human, monkey, macaca fascicularis (cynomolgus monkey), macaca mulatta (rhesus macaque), rodent, mouse, rat, horse, bovine, pig, dog, cat and camel. In some of these second embodiments of the 6<com:Sup>th< / com:Sup> aspect, the seven transmembrane receptor is murine. In some most preferred of these second embodiments of the sixth aspect, the seven transmembrane receptor is human. In some of these second embodiments of the sixth aspect, the seven transmembrane receptor is cynomolgus. In some preferred of these embodiments, the seven transmembrane receptor is human, cynomolgus or mouse. In some of these preferred second embodiments of the sixth aspect, the seven transmembrane receptor is human or cynomolgus. In some preferred embodiments, the seven transmembrane receptor is a human, cynomolgus or mouse seven transmembrane receptor and the seven transmembrane receptor is a) a CC chemokine receptor, preferably CCR1, CCR2, CCR3, CCR4, CCR5, CCR6, CCR7, CCR8, CCR9 or CCR10, b) a CXC chemokine receptor, preferably CXCR1, CXCR2, CXCR3, CXCR4, CXCR5, or CXCR6, or c) CX3CR1 or CXCR1. According to some third embodiments of the 6<com:Sup>th< / com:Sup> aspect, which may be or may not be the same as the first and / or second embodiments according to the 6<com:Sup>th< / com:Sup> aspect, the (first) isolated sulfated polypeptide comprises or consists of a sequence according to a) SEQ ID NO:1 (CCR1_HUMAN_TRD), SEQ ID NO:4 (CCR1_HUMAN_N term), SEQ ID NO:2 (CCR1 MACFA_TRD), SEQ ID NO:5 (CCR1_MACFA_N term), SEQ ID NO:3 (CCR1 MOUSE TRD) or SEQ ID NO:6 (CCR1_MOUSE_N term), preferably wherein at least Y10 and / or Y18 have been sulfated, or b) SEQ ID NO:7 (CCR2 HUMAN TRD), SEQ ID NO:10 (CCR2 HUMAN N term), SEQ ID NO:8 (CCR2_MACMU_TRD) or SEQ ID NO:11 (CCR2_MACMU_N term), preferably wherein at least Y26 has been sulfated, or c) SEQ ID NO:9 (CCR2 MOUSE TRD) or SEQ ID NO:12 (CCR2 MOUSE N term), preferably wherein at least Y37 and / or Y39 has been sulfated, or d) SEQ ID NO:13 (CCR3 HUMAN TRD) or SEQ ID NO:16 (CCR3 HUMAN N term), preferably wherein Y16 and / or Y17 have been sulfated, or e) SEQ ID NO:14 (CCR3 MACFA TRD) or SEQ ID NO:17 (CCR3 MACFA N term), preferably wherein Y16 has been sulfated, or f) SEQ ID NO:15 (CCR3 MOUSE TRD) or SEQ ID NO:18 (CCR3 MOUSE N term), preferably wherein Y20 and / or Y22 has been sulfated, or g) SEQ ID NO:19 (CCR4 HUMAN TRD), SEQ ID NO:22 (CCR4 HUMAN N term), SEQ ID NO:20 (CCR4 MACFA TRD), SEQ ID NO:23 (CCR4_MACFA_N term), SEQ ID NO:21 (CCR4 MOUSE TRD) or SEQ ID NO:24 (CCR4 MOUSE N term), preferably wherein at least Y22 has been sulfated and preferably furthermore Y16, Y19 and / or Y20 have been sulfated, or h) SEQ ID NO:25 (CCR5_HUMAN_TRD), SEQ ID NO:28 (CCR5_HUMAN_N term), SEQ ID NO:26 (CCR5 MACMU TRD) or SEQ ID NO:29 (CCR5 MACMU N term), preferably wherein two, three or all of Y3, Y10, Y14 and Y15 have been sulfated, or i) SEQ ID NO:27 (CCR5_MOUSE_TRD) or SEQ ID NO:30 (CCR5_MOUSE_N term), preferably wherein two or three of Y10, Y12 and Y16 have been sulfated, or j) SEQ ID NO:31 (CCR6_HUMAN_TRD) or SEQ ID NO:34 (CCR6_HUMAN_N term), preferably wherein at least two or three of Y18, Y26 and Y27 have been sulfated, or k) SEQ ID NO:32 (CCR6 MACFA TRD) or SEQ ID NO:35 (CCR6 MACFA N term), preferably wherein at least two or three of Y23, Y31 and Y32 have been sulfated, or l) SEQ ID NO:33 (CCR6_MOUSE_TRD) or SEQ ID NO:36 (CCR6_MOUSE_N term), preferably wherein at least two or three of Y13, Y18 and Y19 have been sulfated, or m) SEQ ID NO:37 (CCR7 HUMAN TRD), SEQ ID NO:40 (CCR7 HUMAN N term), SEQ ID NO:38 (CCR7 MACFA TRD) or SEQ ID NO:41 (CCR7 MACFA N term), preferably wherein one or both of Y8 and Y17 have been sulfated, or n) SEQ ID NO:39 (CCR7 MOUSE TRD) or SEQ ID NO:42 (CCR7 MOUSE N term), preferably wherein one or both of Y8 and Y17 and optionally Y20 have been sulfated have been sulfated, or 0) SEQ ID NO:43 (CCR8 HUMAN TRD), SEQ ID NO:44 (CCR8 MACFA TRD), SEQ ID NO:46 (CCR8_HUMAN_N term with C = X or S), or SEQ ID NO:47 (CCR8_MACFA_N term with C = X or S), preferably wherein at least two or all of Y3, Y15 and Y17 have been sulfated, or p) SEQ ID NO:45 (CCR8 MOUSE TRD) or SEQ ID NO:48 (CCR8 MOUSE N term with C = X or S), preferably wherein at least two or all of Y3, Y14 and Y15 have been sulfated, or q) SEQ ID NO:61 (CCR9_HUMAN_TRD), SEQ ID NO:64 (CCR9_HUMAN_N term), SEQ ID NO:62 (CCR9 MACFA TRD) or SEQ ID NO:65 (CCR9 MACFA N term), preferably wherein at least Y28, and preferably also Y17 and / or Y37 has been sulfated, or r) SEQ ID NO:63 (CCR9 MOUSE TRD) or SEQ ID NO:66 (CCR9 MOUSE N term), preferably wherein at least Y28 has been sulfated, and preferably also Y19 has been sulfated, or s) SEQ ID NO:67 (CCR10 HUMAN TRD), SEQ ID NO:70 (CCR10 HUMAN N term), SEQ ID NO:68 (CCR10 MACFA TRD) or SEQ ID NO:71 (CCR10 MACFA N term), preferably wherein at least one or both of Y14 and Y22 has been sulfated, or t) SEQ ID NO:69 (CCR10_MOUSE_TRD) or SEQ ID NO:72 (CCR10_MOUSE_N term), preferably wherein at least one, two or all of Y14, Y17 and Y22 has been sulfated, or u) SEQ ID NO:73 (CXCR1 HUMAN TRD) or SEQ ID NO:76 (CXCR1 HUMAN N term), preferably wherein Y27 has been sulfated, or v) SEQ ID NO:74 (CXCR1 MACFA TRD) or SEQ ID NO:77 (CXCR1 MACFA N term), preferably wherein at least one of Y14 and Y28 has been sulfated, or w) SEQ ID NO:75 (CXCR1 MOUSE TRD) or SEQ ID NO:78 (CXCR1 MOUSE N term), preferably wherein at least Y6 has been sulfated, or x) SEQ ID NO:79 (CXCR2_HUMAN_TRD) or SEQ ID NO:82 (CXCR2_HUMAN_N term), preferably wherein Y23 and / or Y25 have been sulfated, or y) SEQ ID NO:80 (CXCR2_MACFA _TRD) or SEQ ID NO:83 (CXCR2_MACFA_N term), preferably wherein Y20 and / or Y22 have been sulfated, or z) SEQ ID NO:81 (CXCR2_MOUSE_TRD) or SEQ ID NO:84 (CXCR2_MOUSE_N term), preferably wherein Y24 has been sulfated, or aa) SEQ ID NO:85 (CXCR3_HUMAN_TRD), SEQ ID NO:88 (CXCR3_HUMAN_N term), SEQ ID NO:86 (CXCR3 MACFA TRD), SEQ ID NO:89 (CXCR3 MACFA N term), SEQ ID NO:87 (CXCR3 MOUSE_TRD) or SEQ ID NO:90 (CXCR3_MOUSE_N term), preferably wherein at least one or both of Y27 and Y29 have been sulfated, or bb) SEQ ID NO:91 (CXCR4 HUMAN TRD), SEQ ID NO:94 (CXCR4 HUMAN N term), SEQ ID NO:92 (CXCR4 MACFA TRD) or SEQ ID NO:95 (CXCR4 MACFA N term), preferably wherein at least Y12 and / or Y21 have been sulfated, or cc) SEQ ID NO:93 (CXCR4 MOUSE TRD) or SEQ ID NO:96 (CXCR4 MOUSE N term), preferably wherein at least Y23 and / or Y14 have been sulfated, or dd) SEQ ID NO:97 (CXCR5 HUMAN TRD), SEQ ID NO:100 (CXCR5 HUMAN N term), SEQ ID NO:98 (CXCR5_MACFA_TRD) or SEQ ID NO:101 (CXCR5_MACFA_N term), preferably wherein at least one of Y3 and Y27 have been sulfated, or ee) SEQ ID NO:99 (CXCR5 MOUSE TRD) or SEQ ID NO:102 (CXCR5 MOUSE N term), preferably wherein at least Y3 and / or Y14 and / or Y20 and / or Y26 have been sulfated, or ff) SEQ ID NO:103 (CXCR6 HUMAN TRD) or SEQ ID NO:106 (CXCR6 HUMAN N term), preferably wherein at least one or both of Y6 and Y10 has been sulfated, or gg) SEQ ID NO:104 (CXCR6_MACFA _TRD) or SEQ ID NO:107 (CXCR6_MACFA N term), preferably wherein at least two or all of Y4, Y7 and Y39 have been sulfated, or hh) SEQ ID NO:105 (CXCR6 MOUSE TRD) or SEQ ID NO:108 (CXCR6 MOUSE N term), preferably wherein at least one or both of Y11 and Y15 have been sulfated, or ii) SEQ ID NO:157 (CX3CR1 HUMAN TRD) or SEQ ID NO:160 (CX3CR1 HUMAN N term), preferably wherein at least Y14 has been sulfated, or 11) SEQ ID NO:158 (CX3CR1 MACFA TRD), preferably wherein at least Y20 has been sulfated, or kk) SEQ ID NO:161 (CX3CR1 MACFA N term), preferably wherein at least Y20 or Y22 has been sulfated, or 11) SEQ ID NO:159 (CX3CR1 MOUSE TRD) or SEQ ID NO:162 (CX3CR1 MOUSE N term), preferably wherein at least Y15 has been sulfated, or mm) SEQ ID NO:163 (CXCR1 HUMAN TRD) or SEQ ID NO:166 (CXCR1 HUMAN N term), preferably wherein at least Y27 has been sulfated, or nn) SEQ ID NO:164 (CXCR1_MACMU_TRD), preferably wherein at least Y14 has been sulfated or oo) SEQ ID NO:167 (CXCR1 MACMU N term), preferably wherein at least Y14 or Y28 has been sulfated, or pp) SEQ ID NO:165 (CXCR1_MOUSE_TRD) or SEQ ID NO:168 (CXCR1_MOUSE_N term), preferably wherein at least Y6 has been sulfated. According to some embodiments A of the third embodiments of the 6<com:Sup>th< / com:Sup> aspect, the (first) isolated sulfated polypeptide comprises or consists of a sequence according to a. SEQ ID NO:1 (CCR1 HUMAN TRD), preferably wherein at least Y10 and / or Y18 have been sulfated, or b. SEQ ID NO:7 (CCR2 HUMAN TRD), preferably wherein at least Y26 has been sulfated, or C. SEQ ID NO:13 (CCR3 HUMAN TRD), preferably wherein Y16 and / or Y17 have been sulfated, or d. SEQ ID NO:19 (CCR4 HUMAN TRD), preferably wherein at least Y22 has been sulfated and preferably furthermore Y16, Y19 and / or Y20 have been sulfated, or e. SEQ ID NO:25 (CCR5 HUMAN_TRD), preferably wherein two, three or all of Y3, Y10, Y14 and Y15 have been sulfated, or f. SEQ ID NO:31 (CCR6 HUMAN TRD), preferably wherein at least two or three of Y18, Y26 and Y27 have been sulfated, or g. SEQ ID NO:37 (CCR7 HUMAN TRD), preferably wherein one or both of Y8 and Y17 have been sulfated, or h. SEQ ID NO:43 (CCR8 HUMAN TRD), preferably wherein at least two or all of Y3, Y15 and Y17 have been sulfated, or 1. SEQ ID NO:61 (CCR9 HUMAN TRD), preferably also Y17 and / or Y37 has been sulfated, or 1. SEQ ID NO:67 (CCR10 HUMAN TRD), preferably wherein at least one or both of Y14 and Y22 has been sulfated, or k. SEQ ID NO:73 (CXCR1 HUMAN TRD), preferably wherein Y27 has been sulfated, or SEQ ID NO:79 (CXCR2 HUMAN TRD), preferably wherein Y23 and / or Y25 have been sulfated, or m. SEQ ID NO:85 (CXCR3 HUMAN TRD), preferably wherein at least one or both of Y27 and Y29 have been sulfated, or n. SEQ ID NO:91 (CXCR4 HUMAN TRD), preferably wherein at least Y12 and / or Y21 have been sulfated, or 0. SEQ ID NO:97 (CXCR5 HUMAN TRD), preferably wherein at least one of Y3 and Y27 have been sulfated, or p. SEQ ID NO:103 (CXCR6_HUMAN_TRD), preferably wherein at least one or both of Y6 and Y10 has been sulfated, or q. SEQ ID NO:157 (CX3CR1 HUMAN TRD), preferably wherein at least Y14 has been sulfated, or r. SEQ ID NO:163 (CXCR1 HUMAN TRD), preferably wherein at least Y27 has been sulfated. According to some embodiments B of the third embodiments of the 6<com:Sup>th< / com:Sup> aspect, the (first) isolated sulfated polypeptide comprises or consists of a sequence according to a) SEQ ID NO:3 (CCR1 MOUSE TRD), preferably wherein at least Y10 and / or Y18 have been sulfated, or b) SEQ ID NO:9 (CCR2 MOUSE TRD), preferably wherein at least Y37 and / or Y39 has been sulfated, or c) SEQ ID NO:15 (CCR3 MOUSE TRD), preferably wherein Y20 and / or Y22 has been sulfated, or d) SEQ ID NO:21 (CCR4 MOUSE TRD), preferably wherein at least Y22 has been sulfated and preferably furthermore Y16, Y19 and / or Y20 have been sulfated, or e) SEQ ID NO:27 (CCR5 MOUSE TRD), preferably wherein two or three of Y10, Y12 and Y16 have been sulfated, or f) SEQ ID NO:33 (CCR6 MOUSE TRD), preferably wherein at least two or three of Y13, Y18 and Y19 have been sulfated, g) SEQ ID NO:39 (CCR7_MOUSE_TRD), preferably wherein one or both of Y8 and Y17 and optionally Y20 have been sulfated have been sulfated, or h) SEQ ID NO:45 (CCR8 MOUSE TRD), preferably wherein at least two or all of Y3, Y14 and Y15 have been sulfated, or 1) SEQ ID NO:63 (CCR9 MOUSE TRD), preferably wherein at least Y28 has been sulfated, and preferably also Y19 has been sulfated, or 1) SEQ ID NO:69 (CCR10_MOUSE_TRD), preferably wherein at least one, two or all of Y14, Y17 and Y22 has been sulfated, or k) SEQ ID NO:75 (CXCR1 MOUSE TRD), preferably wherein at least Y6 has been sulfated, or 1) SEQ ID NO:81 (CXCR2 MOUSE TRD), preferably wherein Y24 has been sulfated, or m) SEQ ID NO:87 (CXCR3 MOUSE TRD), preferably wherein at least one or both of Y27 and Y29 have been sulfated, or n) SEQ ID NO:93 (CXCR4 MOUSE TRD), preferably wherein at least Y23 and / or Y14 have been sulfated, or o) SEQ ID NO:99 (CXCR5 MOUSE TRD), preferably wherein at least Y3 and / or Y14 and / or Y20 and / or Y26 have been sulfated, or p) SEQ ID NO:105 (CXCR6 MOUSE TRD), preferably wherein at least one or both of Y11 and Y15 have been sulfated, or q) SEQ ID NO:159 (CX3CR1 MOUSE TRD), preferably wherein at least Y15 has been sulfated, or r) SEQ ID NO:165 (CXCR1 MOUSE TRD), preferably wherein at least Y6 has been sulfated. According to some embodiments C of the third embodiments of the 6<com:Sup>th< / com:Sup> aspect, the (first) isolated sulfated polypeptide comprises or consists of a sequence according to a) SEQ ID NO:2 (CCR1 MACFA TRD), preferably wherein at least Y10 and / or Y18 have been sulfated, or b) SEQ ID NO:8 (CCR2 MACMU TRD), preferably wherein at least Y26 has been sulfated, or c) SEQ ID NO:14 (CCR3 MACFA TRD), preferably wherein Y16 has been sulfated, or d) SEQ ID NO:20 (CCR4 MACFA TRD), preferably wherein at least Y22 has been sulfated and preferably furthermore Y16, Y19 and / or Y20 have been sulfated, or e) SEQ ID NO:26 (CCR5 MACMU TRD), preferably wherein two, three or all of Y3, Y10, Y14 and Y15 have been sulfated, or f) SEQ ID NO:32 (CCR6 MACFA_TRD), preferably wherein at least two or three of Y23, Y31 and Y32 have been sulfated, or g) SEQ ID NO:38 (CCR7 MACFA TRD), preferably wherein one or both of Y8 and Y17 have been sulfated, or h) SEQ ID NO:44 (CCR8 MACFA TRD), preferably wherein at least two or all of Y3, Y15 and Y17 have been sulfated, or i) SEQ ID NO:62 (CCR9 MACFA TRD), preferably wherein at least Y28, and preferably also Y17 and / or Y37 has been sulfated, or 1) SEQ ID NO:68 (CCR10 MACFA TRD), preferably wherein at least one or both of Y14 and Y22 has been sulfated, or k) SEQ ID NO:74 (CXCR1 MACFA TRD), preferably wherein at least one of Y14 and Y28 has been sulfated, or 1) SEQ ID NO:80 (CXCR2 MACFA TRD), preferably wherein Y20 and / or Y22 have been sulfated, or m) SEQ ID NO:86 (CXCR3 MACFA TRD), preferably wherein at least one or both of Y27 and Y29 have been sulfated, or n) SEQ ID NO:92 (CXCR4 MACFA TRD), preferably wherein at least Y12 and / or Y21 have been sulfated, or o) SEQ ID NO:98 (CXCR5 MACFA TRD), preferably wherein at least one of Y3 and Y27 have been sulfated, or p) SEQ ID NO:104 (CXCR6 MACFA TRD), preferably wherein at least two or all of Y4, Y7 and Y39 have been sulfated, or q) SEQ ID NO:158 (CX3CR1 MACFA TRD), preferably wherein at least Y20 has been sulfated, or r) SEQ ID NO:164 (CXCR1 MACMU TRD), preferably wherein at least Y14 has been sulfated. According to some fourth embodiments of the 6<com:Sup>th< / com:Sup> aspect, which may or may not be the same as the first, second and / or third embodiments of the 6<com:Sup>th< / com:Sup> aspect, the first isolated sulfated polypeptide comprises the N terminus of a seven transmembrane receptor including tyrosine rich domain (TRD) and preferably LID domain, and at least 25 %, at least 50 % or at least 75 % of the tyrosine residues of the TRD are sulfated, preferably wherein at least one / the cysteine between the TRD and the LID domain has been removed or has been exchanged into a different amino acid. According to some embodiments A of the fourth embodiments of the 6th aspect, the (first) isolated sulfated polypeptide comprises or consists of a sequence according to a) SEQ ID NO:4 (CCR1 HUMAN N term), preferably wherein at least Y10 and / or Y18 have been sulfated, b) SEQ ID NO:10 (CCR2 HUMAN N term), preferably wherein at least Y26 has been sulfated, c) SEQ ID NO:16 (CCR3_HUMAN_N term), preferably wherein Y16 and / or Y17 have been sulfated, d) SEQ ID NO:22 (CCR4 HUMAN N term), preferably wherein at least Y22 has been sulfated and preferably furthermore Y16, Y19 and / or Y20 have been sulfated, e) SEQ ID NO:28 (CCR5 HUMAN N term), preferably wherein two, three or all of Y3, Y10, Y14 and Y15 have been sulfated, f) SEQ ID NO:34 (CCR6 HUMAN N term), preferably wherein at least two or three of Y18, Y26 and Y27 have been sulfated, g) SEQ ID NO:40 (CCR7 HUMAN N term), preferably wherein one or both of Y8 and Y17 have been sulfated, h) SEQ ID NO:46 (CCR8_HUMAN_N term with <com:Math><semantics>C=X<annotation encoding="application / x-tex">C = X< / annotation>< / semantics>< / com:Math> or S), preferably wherein at least two or all of Y3, Y15 and Y17 have been sulfated, 1) SEQ ID NO:64 (CCR9_HUMAN_N term), preferably wherein at least Y28, and preferably also Y17 and / or Y37 have been sulfated, 1) SEQ ID NO:70 (CCR10_HUMAN_N term), preferably wherein at least one or both of Y14 and Y22 have been sulfated, k) SEQ ID NO:76 (CXCR1_HUMAN_N term), preferably wherein Y27 has been sulfated, 1) SEQ ID NO:82 (CXCR2 HUMAN N term), preferably wherein Y23 and / or Y25 have been sulfated, m) SEQ ID NO:88 (CXCR3 HUMAN N term), preferably wherein at least one or both of Y27 and Y29 have been sulfated, n) SEQ ID NO:94 (CXCR4 HUMAN N term), preferably wherein at least Y12 and / or Y21 have been sulfated, 0) SEQ ID NO:100 (CXCR5 HUMAN N term), preferably wherein at least one of Y3 and Y27 have been sulfated, or p) SEQ ID NO:106 (CXCR6 HUMAN N term), preferably wherein at least one or both of Y6 and Y10 have been sulfated, q) SEQ ID NO:160 (CX3CR1 HUMAN N term), preferably wherein at least Y14 has been sulfated, or r) SEQ ID NO:166 (CXCR1_HUMAN_N term), preferably wherein at least Y27 has been sulfated. According to some embodiments B of the fourth embodiments of the 6th aspect, the (first) isolated sulfated polypeptide comprises or consists of a sequence according to a) SEQ ID NO:6 (CCR1_MOUSE_N term), preferably wherein at least Y10 and / or Y18 have been sulfated, or b) SEQ ID NO:12 (CCR2 MOUSE N term), preferably wherein at least Y37 and / or Y39 has been sulfated, or c) SEQ ID NO:18 (CCR3 MOUSE N term), preferably wherein Y20 and / or Y22 has been sulfated, or d) SEQ ID NO:24 (CCR4 MOUSE N term), preferably wherein at least Y22 has been sulfated and preferably furthermore Y16, Y19 and / or Y20 have been sulfated, or e) SEQ ID NO:30 (CCR5 MOUSE N term), preferably wherein two or three of Y10, Y12 and Y16 have been sulfated, or f) SEQ ID NO:36 (CCR6 MOUSE N term), preferably wherein at least two or three of Y13, Y18 and Y19 have been sulfated, g) SEQ ID NO:42 (CCR7_MOUSE_N term), preferably wherein one or both of Y8 and Y17 and optionally Y20 have been sulfated have been sulfated, or h) SEQ ID NO:48 (CCR8 MOUSE N term with <com:Math><semantics>C=X<annotation encoding="application / x-tex">C = X< / annotation>< / semantics>< / com:Math> or S), preferably wherein at least two or all of Y3, Y14 and Y15 have been sulfated, or 1) SEQ ID NO:66 (CCR9 MOUSE N term), preferably wherein at least Y28 has been sulfated, and preferably also Y19 has been sulfated, or 1) SEQ ID NO:72 (CCR10 MOUSE N term), preferably wherein at least one, two or all of Y14, Y17 and Y22 has been sulfated, or k) SEQ ID NO:78 (CXCR1 MOUSE N term), preferably wherein at least Y6 has been sulfated, or 1) SEQ ID NO:84 (CXCR2 MOUSE N term), preferably wherein Y24 has been sulfated, or m) SEQ ID NO:90 (CXCR3 MOUSE N term), preferably wherein at least one or both of Y27 and Y29 have been sulfated, or n) SEQ ID NO:96 (CXCR4 MOUSE N term), preferably wherein at least Y13 and / or Y14 have been sulfated, or 0) SEQ ID NO:102 (CXCR5 MOUSE N term), preferably wherein at least Y3 and / or Y14 and / or Y20 and / or Y26 have been sulfated, or p) SEQ ID NO:108 (CXCR6_MOUSE_N term), preferably wherein at least one or both of Y11 and Y15 have been sulfated, or q) SEQ ID NO:162 (CX3CR1 MOUSE N term), preferably wherein at least Y15 has been sulfated, or r) SEQ ID NO:168 (CXCR1_MOUSE_N term), preferably wherein at least Y6 has been sulfated. According to some embodiments C of the fourth embodiments of the 6th aspect, the (first) isolated sulfated polypeptide comprises or consists of a sequence according to a) SEQ ID NO:5 (CCR1 MACFA N term), preferably wherein at least Y10 and / or Y18 have been sulfated, or b) SEQ ID NO:11 (CCR2_MACMU_N term), preferably wherein at least Y26 has been sulfated, or c) SEQ ID NO:17 (CCR3 MACFA N term), preferably wherein Y16 has been sulfated, or d) SEQ ID NO:23 (CCR4 MACFA N term), preferably wherein at least Y22 has been sulfated and preferably furthermore Y16, Y19 and / or Y20 have been sulfated, or e) SEQ ID NO:29 (CCR5 MACMU N term), preferably wherein two, three or all of Y3, Y10, Y14 and Y15 have been sulfated, or f) SEQ ID NO:35 (CCR6 MACFA N term), preferably wherein at least two or three of Y23, Y31 and Y32 have been sulfated, or g) SEQ ID NO:41 (CCR7 MACFA N term), preferably wherein one or both of Y8 and Y17 have been sulfated, or h) SEQ ID NO:47 (CCR8 MACFA N term with <com:Math><semantics>C=X<annotation encoding="application / x-tex">C = X< / annotation>< / semantics>< / com:Math> or S), preferably wherein at least two or all of Y3, Y15 and Y17 have been sulfated, or 1) SEQ ID NO:65 (CCR9_MACFA_N term), preferably wherein at least Y28, and preferably also Y17 and / or Y37 has been sulfated, or 1) SEQ ID NO:71 (CCR10 MACFA N term), preferably wherein at least one or both of Y14 and Y22 has been sulfated, or k) SEQ ID NO:77 (CXCR1 MACFA N term), preferably wherein at least one of Y14 and Y28 has been sulfated, or 1) SEQ ID NO:83 (CXCR2_MACFA_N term), preferably wherein Y20 and / or Y22 have been sulfated, or m) SEQ ID NO:89 (CXCR3 MACFA N term), preferably wherein at least one or both of Y27 and Y29 have been sulfated, or n) SEQ ID NO:95 (CXCR4 MACFA N term), preferably wherein at least Y12 and / or Y21 have been sulfated, or 0) SEQ ID NO:101 (CXCR5 MACFA N term), preferably wherein at least one of Y3 and Y27 have been sulfated, or p) SEQ ID NO:107 (CXCR6 MACFA N term), preferably wherein at least two or all of Y4, Y7 and Y39 have been sulfated, or q) SEQ ID NO:161 (CX3CR1 MACFA N term), preferably wherein at least Y20 or Y22 has been sulfated, or r) SEQ ID NO:167 (CXCR1_MACMU_N term), preferably wherein at least Y14 or Y28 has been sulfated. According to some fifth embodiments of the <com:Math><semantics>6th<annotation encoding="application / x-tex">6^{th}< / annotation>< / semantics>< / com:Math> aspect, which may be or may not be the same as the first, second, third and / or fourth embodiments according to the 6<com:Sup>th< / com:Sup> aspect, the isolated antibody or antigen- binding fragment thereof, (specifically) binds to a second isolated sulfated polypeptide which comprises the tyrosine rich domain (TRD) of a seven transmembrane receptor. Preferably the seven transmembrane receptor of the TRD comprised by the second isolated sulfated polypeptide a) is different from the seven transmembrane receptor of the TRD comprised by the first isolated sulfated polypeptide, or is b) the corresponding seven transmembrane receptor of the TRD comprised by the first isolated sulfated polypeptide but from a different species. According to some preferred embodiments, the second isolated sulfated polypeptide which comprises the tyrosine rich domain (TRD) of a seven transmembrane receptor is different from the first isolated sulfated polypeptide which comprises the tyrosine rich domain (TRD) of a seven transmembrane receptor and is an isolated polypeptide with a sequence according to any of embodiments A, B, or C according to the third and / or fourth embodiments of the 6<com:Sup>th< / com:Sup> aspect. For example, the first isolated sulfated polypeptide may comprise the TRD of a seven transmembrane receptor of a first species and the second isolated sulfated polypeptide may comprise the TRD of a seven transmembrane receptor of a second species, preferably wherein the species are human and cynomolgus, or human and mouse, or human and rat. According to some embodiments A of the fifth embodiments of the 6<com:Sup>th< / com:Sup> aspect, the antibody or fragment specifically binds to a) a first isolated sulfated polypeptide comprising SEQ ID NO:1 (CCR1 HUMAN TRD), preferably wherein at least Y10 and / or Y18 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:2 (CCR1 MACFA TRD), preferably wherein at least Y10 and / or Y18 have been sulfated, or b) a first isolated sulfated polypeptide comprising SEQ ID NO:7 (CCR2 HUMAN TRD), preferably wherein at least Y26 has been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:8 (CCR2 MACMU TRD), preferably wherein at least Y26 has been sulfated, or c) a first isolated sulfated polypeptide comprising SEQ ID NO:13 (CCR3 HUMAN TRD), preferably wherein Y16 and / or Y17 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:14 (CCR3 MACFA TRD), preferably wherein Y16 has been sulfated, or d) a first isolated sulfated polypeptide comprising SEQ ID NO:19 (CCR4 HUMAN TRD), preferably wherein at least Y22 has been sulfated and preferably furthermore Y16, Y19 and / or Y20 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:20 (CCR4 MACFA TRD), preferably wherein at least Y22 has been sulfated and preferably furthermore Y16, Y19 and / or Y20 have been sulfated, or e) a first isolated sulfated polypeptide comprising SEQ ID NO:25 (CCR5_HUMAN_TRD), preferably wherein two, three or all of Y3, Y10, Y14 and Y15 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:26 (CCR5_MACMU_TRD), preferably wherein two, three or all of Y3, Y10, Y14 and Y15 have been sulfated, or f) a first isolated sulfated polypeptide comprising SEQ ID NO:31 (CCR6 HUMAN TRD), preferably wherein at least two or three of Y18, Y26 and Y27 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:32 (CCR6 MACFA TRD), preferably wherein at least two or three of Y23, Y31 and Y32 have been sulfated, or g) a first isolated sulfated polypeptide comprising SEQ ID NO:37 (CCR7 HUMAN TRD), preferably wherein one or both of Y8 and Y17 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:38 (CCR7_MACFA_TRD), preferably wherein one or both of Y8 and Y17 have been sulfated, or h) a first isolated sulfated polypeptide comprising SEQ ID NO:43 (CCR8 HUMAN TRD), preferably wherein at least two or all of Y3, Y15 and Y17 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:44 (CCR8 MACFA TRD), preferably wherein at least two or all of Y3, Y15 and Y17 have been sulfated, or i) a first isolated sulfated polypeptide comprising SEQ ID NO:61 (CCR9_HUMAN_TRD), preferably also Y17 and / or Y37 has been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:62 (CCR9 MACFA TRD), preferably wherein at least Y28, and preferably also Y17 and / or Y37 has been sulfated, or j) a first isolated sulfated polypeptide comprising SEQ ID NO:67 (CCR10 HUMAN TRD), preferably wherein at least one or both of Y14 and Y22 has been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:68 (CCR10_MACFA_TRD), preferably wherein at least one or both of Y14 and Y22 has been sulfated, or k) a first isolated sulfated polypeptide comprising SEQ ID NO:73 (CXCR1 HUMAN TRD), preferably wherein Y27 has been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:74 (CXCR1 MACFA TRD), preferably wherein at least one of Y14 and Y28 has been sulfated, or 1) a first isolated sulfated polypeptide comprising SEQ ID NO:79 (CXCR2 HUMAN TRD), preferably wherein Y23 and / or Y25 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:80 (CXCR2 MACFA TRD), preferably wherein Y20 and / or Y22 have been sulfated, or m) a first isolated sulfated polypeptide comprising SEQ ID NO:85 (CXCR3 HUMAN TRD), preferably wherein at least one or both of Y27 and Y29 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:86 (CXCR3 MACFA TRD), preferably wherein at least one or both of Y27 and Y29 have been sulfated, or n) a first isolated sulfated polypeptide comprising SEQ ID NO:91 (CXCR4 HUMAN TRD), preferably wherein at least Y12 and / or Y21 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:92 (CXCR4 MACFA TRD), preferably wherein at least Y12 and / or Y21 have been sulfated, or o) a first isolated sulfated polypeptide comprising SEQ ID NO:97 (CXCR5 HUMAN TRD), preferably wherein at least one of Y3 and Y27 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:98 (CXCR5 MACFA TRD), preferably wherein at least one of Y3 and Y27 have been sulfated, or p) a first isolated sulfated polypeptide comprising SEQ ID NO:103 (CXCR6 HUMAN TRD), preferably wherein at least one or both of Y6 and Y10 has been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:104 (CXCR6 MACFA TRD), preferably wherein at least two or all of Y4, Y7 and Y39 have been sulfated q) a first isolated sulfated polypeptide comprising SEQ ID NO:157 (CX3CR1 HUMAN TRD), preferably wherein at least Y14 has been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:158 (CX3CR1 MACFA TRD), preferably wherein at least Y20 has been sulfated, or r) a first isolated sulfated polypeptide comprising SEQ ID NO:163 (CXCR1 HUMAN TRD), preferably wherein at least Y27 has been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:164 (CXCR1 MACMU TRD), preferably wherein at least Y14 has been sulfated. According to some embodiments B of the fifth embodiments of the 6<com:Sup>th< / com:Sup> aspect, the antibody or fragment specifically binds to a) a first isolated sulfated polypeptide comprising SEQ ID NO:4 (CCR1 HUMAN N term), preferably wherein at least Y10 and / or Y18 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:5 (CCR1 MACFA N term), preferably wherein at least Y10 and / or Y18 have been sulfated, b) a first isolated sulfated polypeptide comprising SEQ ID NO:10 (CCR2 HUMAN N term), preferably wherein at least Y26 has been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:11 (CCR2 MACMU N term), preferably wherein at least Y26 has been sulfated, c) a first isolated sulfated polypeptide comprising SEQ ID NO:16 (CCR3 HUMAN N term), preferably wherein Y16 and / or Y17 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:17 (CCR3 MACFA N term), preferably wherein Y16 has been sulfated, d) a first isolated sulfated polypeptide comprising SEQ ID NO:22 (CCR4 HUMAN N term), preferably wherein at least Y22 has been sulfated and preferably furthermore Y16, Y19 and / or Y20 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:23 (CCR4 MACFA N term), preferably wherein at least Y22 has been sulfated and preferably furthermore Y16, Y19 and / or Y20 have been sulfated, e) a first isolated sulfated polypeptide comprising SEQ ID NO:28 (CCR5 HUMAN N term), preferably wherein two, three or all of Y3, Y10, Y14 and Y15 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:29 (CCR5 MACMU N term), preferably wherein two, three or all of Y3, Y10, Y14 and Y15 have been sulfated, f) a first isolated sulfated polypeptide comprising SEQ ID NO:34 (CCR6 HUMAN N term), preferably wherein at least two or three of Y18, Y26 and Y27 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:35 (CCR6_MACFA_N term), preferably wherein at least two or three of Y23, Y31 and Y32 have been sulfated, g) a first isolated sulfated polypeptide comprising SEQ ID NO:40 (CCR7 HUMAN N term), preferably wherein one or both of Y8 and Y17 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:41 (CCR7 MACFA N term), preferably wherein one or both of Y8 and Y17 have been sulfated, h) a first isolated sulfated polypeptide comprising SEQ ID NO:46 (CCR8 HUMAN N term with C = X or S), preferably wherein at least two or all of Y3, Y15 and Y17 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:47 (CCR8 MACFA N term with <com:Math><semantics>C=X<annotation encoding="application / x-tex">C = X< / annotation>< / semantics>< / com:Math> or S), preferably wherein at least two or all of Y3, Y15 and Y17 have been sulfated, 1) a first isolated sulfated polypeptide comprising SEQ ID NO:64 (CCR9_ HUMAN_N term), preferably wherein at least Y28, and preferably also Y17 and / or Y37 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:65 (CCR9 MACFA N term), preferably wherein at least Y28, and preferably also Y17 and / or Y37 has been sulfated, 1) a first isolated sulfated polypeptide comprising SEQ ID NO:70 (CCR10 HUMAN N term), preferably wherein at least one or both of Y14 and Y22 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:71 (CCR10 MACFA N term), preferably wherein at least one or both of Y14 and Y22 has been sulfated, k) a first isolated sulfated polypeptide comprising SEQ ID NO:76 (CXCR1 HUMAN N term), preferably wherein Y27 has been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:77 (CXCR1 MACFA N term), preferably wherein at least one of Y14 and Y28 has been sulfated, 1) a first isolated sulfated polypeptide comprising SEQ ID NO:82 (CXCR2 HUMAN N term), preferably wherein Y23 and / or Y25 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:83 (CXCR2 MACFA N term), preferably wherein Y20 and / or Y22 have been sulfated, m) a first isolated sulfated polypeptide comprising SEQ ID NO:88 (CXCR3 HUMAN N term), preferably wherein at least one or both of Y27 and Y29 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:89 (CXCR3 MACFA N term), preferably wherein at least one or both of Y27 and Y29 have been sulfated, n) a first isolated sulfated polypeptide comprising SEQ ID NO:94 (CXCR4 HUMAN N term), preferably wherein at least Y12 and / or Y21 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:95 (CXCR4 MACFA N term), preferably wherein at least Y12 and / or Y21 have been sulfated, o) a first isolated sulfated polypeptide comprising SEQ ID NO:100 (CXCR5 HUMAN N term), preferably wherein at least one of Y3 and Y27 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:101 (CXCR5 MACFA N term), preferably wherein at least one of Y3 and Y27 have been sulfated, or p) a first isolated sulfated polypeptide comprising SEQ ID NO:106 (CXCR6 HUMAN N term), preferably wherein at least one or both of Y6 and Y10 have been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:107 (CXCR6 MACFA N term), preferably wherein at least two or all of Y4, Y7 and Y39 have been sulfated, or q) a first isolated sulfated polypeptide comprising SEQ ID NO:160 (CX3CR1 HUMAN N term), preferably wherein at least Y14 has been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:161 (CX3CR1_MACFA_N term), preferably wherein at least Y20 or Y22 has been sulfated, or r) a first isolated sulfated polypeptide comprising SEQ ID NO:166 (CXCR1 HUMAN N term), preferably wherein at least Y27 has been sulfated, and a second isolated sulfated polypeptide comprising SEQ ID NO:167 (CXCR1 MACMU N term), preferably wherein at least Y14 or Y28 has been sulfated. According to some embodiments C1 of the fifth embodiments of the 6<com:Sup>th< / com:Sup> aspect, the antibody or fragment specifically binds to a first isolated sulfated polypeptide comprising a sequence according to some embodiments A of the third embodiments of the 6<com:Sup>th< / com:Sup> aspect and binds to a second isolated sulfated polypeptide comprising a sequence according to some embodiments B or C of the third embodiments of the 6<com:Sup>th< / com:Sup> aspect, wherein preferably the first and the second polypeptide comprise the TRD of the same receptor but from different species. According to some embodiments C2 of the fifth embodiments of the 6<com:Sup>th< / com:Sup> aspect, the antibody or fragment specifically binds to a first isolated sulfated polypeptide comprising a sequence according to some embodiments A of the fourth embodiments of the 6<com:Sup>th< / com:Sup> aspect and binds to a second isolated sulfated polypeptide comprising a sequence according to some embodiments B or C of the fourth embodiments of the 6<com:Sup>th< / com:Sup> aspect, wherein preferably the first and the second polypeptide comprise the TRD of the same receptor but from different species. According to some sixth embodiments of the <com:Math><semantics>6th<annotation encoding="application / x-tex">6^{th}< / annotation>< / semantics>< / com:Math> aspect, which may be or may not be the same as the first, second, third, fourth and / or fifth embodiments according to the 6<com:Sup>th< / com:Sup> aspect, the dissociation constant or the EC50 of the antibody or antigen-binding fragment for binding the first isolated sulfated polypeptide and / or for binding said seven transmembrane receptor is below 200 nM, 150 nM, 100 nM, 10 nM, 5 nM, 2.5 nM, 1 nM, 0.5 nM or 0.25 nM. According to some embodiments A of the sixth embodiments of the 6<com:Sup>th< / com:Sup> aspect, the dissociation constant or the EC50 of the antibody or antigen-binding fragment for binding the first isolated sulfated polypeptide and / or for binding said seven transmembrane receptor is below 200 nM, 199 nM, 198 nM, 197 nM, 196 nM, 195 nM, 194 nM, 193 nM, 192 nM, 191 nM, 190 nM, 189 nM, 188 nM, 187 nM, 186 nM, 185 nM, 184 nM, 183 nM, 182 nM, 181 nM, 180 nM, 179 nM, 178 nM, 177 nM, 176 nM, 175 nM, 174 nM, 173 nM, 172 nM, 171 nM, 170 nM, 169 nM, 168 nM, 167 nM, 166 nM, 165 nM, 164 nM, 163 nM, 162 nM, 161 nM, 160 nM, 159 nM, 158 nM, 157 nM, 156 nM, 155 nM, 154 nM, 153 nM, 152 nM, 151 nM, 150 nM, 149 nM, 148 nM, 147 nM, 146 nM, 145 nM, 144 nM, 143 nM, 142 nM, 141 nM, 140 nM, 139 nM, 138 nM, 137 nM, 136 nM, 135 nM, 134 nM, 133 nM, 132 nM, 131 nM, 130 nM, 129 nM, 128 nM, 127 nM, 126 nM, 125 nM, 124 nM, 123 nM, 122 nM, 121 nM, 120 nM, 119 nM, 118 nM, 117 nM, 116 nM, 115 nM, 114 nM, 113 nM, 112 nM, 111 nM, 110 nM, 109 nM, 108 nM, 107 nM, 106 nM, 105 nM, 104 nM, 103 nM, 102 nM, 101 nM, 100 nM, 99 nM, 98 nM, 97 nM, 96 nM, 95 nM, 94 nM, 93 nM, 92 nM, 91 nM, 90 nM, 89 nM, 88 nM,87 nM, 86 nM, 85 nM, 84 nM, 83 nM, 82 nM, 81 nM, 80 nM, 79 nM, 78 nM, 77 nM, 76 nM, 75 nM, 74 nM, 73 nM, 72 nM, 71 nM, 70 nM, 69 nM, 68 nM, 67 nM, 66 nM, 65 nM, 64 nM, 63 nM, 62 nM, 61 nM, 60 nM, 59 nM, 58 nM, 57 nM, 56 nM, 55 nM, 54 nM, 53 nM, 52 nM, 51 nM, 50 nM, 49 nM, 48 nM, 47 nM, 46 nM, 45 nM, 44 nM, 43 nM, 42 nM, 41 nM, 40 nM, 39 nM, 38 nM, 37 nM, 36 nM, 35 nM, 34 nM, 33 nM, 32 nM, 31 nM, 30 nM, 29 nM, 28 nM, 27 nM, 26 nM, 25 nM, 24 nM, 23 nM, 22 nM, 21 nM, 20 nM, 19 nM, 18 nM, 17 nM, 16 nM, 15 nM, 14 nM, 13 nM, 12 nM, 11 nM, 10 nM, 9 nM, 8 nM, 7 nM, 6 nM, 5 nM, 4 nM, 3 nM, 2 nM, 1 nM, 0.9 nM, 0.8 nM, 0.7 nM, 0.6 nM, 0.5 nM, 0.4 nM, 0.3 nM, 0.25 nM, 0.2 nM, 0.15 nM, or 0.1 nM. Preferably, the dissociation constant or the EC50 of the antibody or antigen-binding fragment for binding the first isolated sulfated polypeptide and / or for said seven transmembrane receptor is below 10 nM, 5 nM, 2.5 nM, 1 nM, 0.5 nM, 0.25 nM, 0.2 nM, 0.15 nM, or 0.1 nM. Preferably, EC50 can be determined in CHO cells overexpressing the target. As disclosed for instance in example 10.1.1, the antibodies obtained with a method disclosed herein have excellent affinities for their respective target. For example, TPP-21181, TPP-17578, TPP-19546, TPP-18206, TPP-21360 and TPP- 23411 bound human CCR8 with an EC50 of 4.8 nM, 1.7 nM, 0.8 nM, 0.6 nM, ~0.9 nM or 1.7 nM in CHO cells engineered to overexpress CCR8. Also, TPP-21181, TPP-17578, TPP-19546, TPP-18206, TPP- 21360 and TPP-23411 bound cynomolgus CCR8 with an EC50 of 1.8 nM, 1 nM, 0.5 nM, 0.7 nM, ~0.55 nM or 0.9 nM. In addition, TPP-17578, TPP-19546, TPP-18206, and TPP-21360 bound to human regulatory T cells with an EC50 of 25 nM, 15 nM, 23 nM or 10 nM. In addition, anti-murine CCR8 antibody TPP-14099 binds CHO cells expressing murine CCR8 with an EC50 of 3 nM and murine iTregs with an EC50 of 13.2 nM, cf. Table 10.1.1.5. According to some embodiments B of the sixth embodiments of the 6<com:Sup>th< / com:Sup> aspect, which may or may not be the same as the embodiments A of the sixth embodiments of the 6<com:Sup>th< / com:Sup> aspect, the dissociation constant or the EC50 of the antibody or antigen-binding fragment for binding the second isolated sulfated polypeptide and / or for binding the second seven transmembrane receptor is below 200 nM, 199 nM, 198 nM, 197 nM, 196 nM, 195 nM, 194 nM, 193 nM, 192 nM, 191 nM, 190 nM, 189 nM, 188 nM, 187 nM, 186 nM, 185 nM, 184 nM, 183 nM, 182 nM, 181 nM, 180 nM, 179 nM, 178 nM, 177 nM, 176 nM, 175 nM, 174 nM, 173 nM, 172 nM, 171 nM, 170 nM, 169 nM, 168 nM, 167 nM, 166 nM, 165 nM, 164 nM, 163 nM, 162 nM, 161 nM, 160 nM, 159 nM, 158 nM, 157 nM, 156 nM, 155 nM, 154 nM, 153 nM, 152 nM, 151 nM, 150 nM, 149 nM, 148 nM, 147 nM, 146 nM, 145 nM, 144 nM, 143 nM, 142 nM, 141 nM, 140 nM, 139 nM, 138 nM, 137 nM, 136 nM, 135 nM, 134 nM, 133 nM, 132 nM, 131 nM, 130 nM, 129 nM, 128 nM, 127 nM, 126 nM, 125 nM, 124 nM, 123 nM, 122 nM, 121 nM, 120 nM, 119 nM, 118 nM, 117 nM, 116 nM, 115 nM, 114 nM, 113 nM, 112 nM, 111 nM, 110 nM, 109 nM, 108 nM, 107 nM, 106 nM, 105 nM, 104 nM, 103 nM, 102 nM, 101 nM, 100 nM, 99 nM, 98 nM, 97 nM, 96 nM, 95 nM, 94 nM, 93 nM, 92 nM, 91 nM, 90 nM, 89 nM, 88 nM,87 nM, 86 nM, 85 nM, 84 nM, 83 nM, 82 nM, 81 nM, 80 nM, 79 nM, 78 nM, 77 nM, 76 nM, 75 nM, 74 nM, 73 nM, 72 nM, 71 nM, 70 nM, 69 nM, 68 nM, 67 nM, 66 nM, 65 nM, 64 nM, 63 nM, 62 nM, 61 nM, 60 nM, 59 nM, 58 nM, 57 nM, 56 nM, 55 nM, 54 nM, 53 nM, 52 nM, 51 nM, 50 nM, 49 nM, 48 nM, 47 nM, 46 nM, 45 nM, 44 nM, 43 nM, 42 nM, 41 nM, 40 nM, 39 nM, 38 nM, 37 nM, 36 nM, 35 nM, 34 nM, 33 nM, 32 nM, 31 nM, 30 nM, 29 nM, 28 nM, 27 nM, 26 nM, 25 nM, 24 nM, 23 nM, 22 nM, 21 nM, 20 nM, 19 nM, 18 nM, 17 nM, 16 nM, 15 nM, 14 nM, 13 nM, 12 nM, 11 nM, 10 nM, 9 nM, 8 nM, 7 nM, 6 nM, 5 nM, 4 nM, 3 nM, 2 nM, 1 nM, 0.9 nM, 0.8 nM, 0.7 nM, 0.6 nM, 0.5 nM, 0.4 nM, 0.3 nM, 0.25 nM, 0.2 nM, 0.15 nM, or 0.1 nM. Preferably, the dissociation constant (KD) or the EC50 of the antibody or antigen-binding fragment for binding the second isolated sulfated polypeptide and / or for binding the second seven transmembrane receptor is below 10 nM, 5 nM, 2.5 nM, 1 nM, 0.5 or 0.25 nM. According to some embodiments AB of the sixth embodiments of the 6<com:Sup>th< / com:Sup> aspect, the dissociation constant (KD) or the EC50 of the antibody or antigen-binding fragment for binding the first isolated sulfated polypeptide and / or the first seven transmembrane receptor is below 10 nM, 5 nM, 2.5 nM, 1 nM, 0.5 nM or 0.25 nM and the dissociation constant (KD) or the EC50 of the antibody or antigen-binding fragment for binding the second isolated sulfated polypeptide and / or the second seven transmembrane receptor is below 10 nM, 5 nM, 2.5 nM, 1 nM, 0.5 nM or 0.25 nM. According to some seventh embodiments of the 6<com:Sup>th< / com:Sup> aspect, which may be or may not be the same as the first, second, third, fourth, fifth and / or sixth embodiments according to the 6<com:Sup>th< / com:Sup> aspect, the dissociation constant (KD) of the antibody for binding the first isolated sulfated polypeptide is lower than the dissociation constant (KD) of the antibody for binding a first isolated non-sulfated polypeptide having the same sequence as the first isolated sulfated polypeptide. Preferably, the antibody does not substantially bind a first isolated non-sulfated polypeptide having the same sequence as the first isolated sulfated polypeptide. According to some embodiments A of the seventh embodiments of the 6<com:Sup>th< / com:Sup> aspect, the dissociation constant or the EC50 of the antibody for binding the first isolated non-sulfated polypeptide is higher than 100 nM, 150 nM, 200 nM, 250 nM, 300 nM, 350 nM, 400 nM, 450 nM, 500 nM, 600 nM, 700 nM, 800 nM, 900 nM, 1 <com:Math><semantics>μ<annotation encoding="application / x-tex">\mu< / annotation>< / semantics>< / com:Math>M, 1.25 <com:Math><semantics>μ<annotation encoding="application / x-tex">\mu< / annotation>< / semantics>< / com:Math>M, 1.5 <com:Math><semantics>μ<annotation encoding="application / x-tex">\mu< / annotation>< / semantics>< / com:Math>M, 1.75 <com:Math><semantics>μ<annotation encoding="application / x-tex">\mu< / annotation>< / semantics>< / com:Math>M, 2 <com:Math><semantics>μ<annotation encoding="application / x-tex">\mu< / annotation>< / semantics>< / com:Math>M, 2.25 <com:Math><semantics>μ<annotation encoding="application / x-tex">\mu< / annotation>< / semantics>< / com:Math>M, 2.5 <com:Math><semantics>μ<annotation encoding="application / x-tex">\mu< / annotation>< / semantics>< / com:Math>M, 2.75 <com:Math><semantics>μ<annotation encoding="application / x-tex">\mu< / annotation>< / semantics>< / com:Math>M, or 3 <com:Math><semantics>μ<annotation encoding="application / x-tex">\mu< / annotation>< / semantics>< / com:Math>M, or is not detectable. Preferably, the dissociation constant or the EC50 of the antibody for binding the first isolated non-sulfated polypeptide is higher than 100 nM, 250 nM, 500 nM, 1 µM, 2 µM or 3 µM, or is not detectable. According to some embodiments B of the seventh embodiments of the 6<com:Sup>th< / com:Sup> aspect, which may be the same as the embodiments A of the seventh embodiments of the 6<com:Sup>th< / com:Sup> aspect, the dissociation constant or the EC50 of the antibody or fragment for binding the first isolated sulfated polypeptide is below 10 nM, 5 nM, 2.5 nM, 1 nM, 0.5 nM or 0.25 nM, and the dissociation constant or the EC50 of the antibody or fragment for binding the first isolated non-sulfated polypeptide is higher than 10 nM, 25 nM, 50 nM, 100 nM, 250 nM or 500 nM, or is not detectable. The antibody according to the 6th aspect may comprise CDRs derived from human, monkey, macaca fascicularis (cynomolgus monkey), macaca mulatta (rhesus macaque), rodent, mouse, rat, horse, bovine, pig, dog, cat and camel. Preferably, the antibody according to the 6<com:Sup>th< / com:Sup> aspect comprises human, rat or mouse derived CDRs. According to some 8<com:Sup>th< / com:Sup> embodiments of the 6<com:Sup>th< / com:Sup> aspect, which may be and are suggested to be combined with the first, second, third, fourth, fifth, sixth and / or seventh embodiments of the sixth aspect, the isolated antibody or antigen-binding fragment comprises human derived CDRs. According to some highly preferred embodiments, the human derived CDRs comprise no deviations or less than 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14 or 15 deviations from the closest human germline. The closest human germline may be determined as known in the art, e.g. in silico using IgBLAST (Ye, Jian, et al. "IgBLAST: an immunoglobulin variable domain sequence analysis tool." Nucleic acids research 41.W1 (2013): W34- W40.) with data retrieved from the IMGT human germline database. The antibodies according to these 8<com:Sup>th< / com:Sup> embodiments can be obtained as described e.g. in example 6 or 8, or as described elsewhere herein. According to some 9<com:Sup>th< / com:Sup> embodiments of the 6<com:Sup>th< / com:Sup> aspect, which may be and are suggested to be combined with the first, second, third, fourth, fifth, sixth, seventh, or 8<com:Sup>th< / com:Sup> embodiments of the 6<com:Sup>th< / com:Sup> aspect, the isolated antibody or antigen-binding fragment is cross reactive for human and cynomolgus, cf. example 10.1.1. Preferably, the dissociation constant (KD) or the EC50 of the antibody or antigen-binding fragment for binding a human chemokine receptor is below 200 nM, 150 nM, 100 nM, 10 nM, 5 nM, 2.5 nM, 1 nM, 0.5 or 0.25 nM, such as below 10 nM, 5 nM, 2.5 nM, 1 nM, 0.5 or 0.25 nM. Preferably, the dissociation constant (KD) or the EC50 of the antibody or antigen-binding fragment for binding a cynomolgus chemokine receptor is below 10 nM, 5 nM, 2.5 nM, 1 nM, 0.5 or 0.25 nM. According to some 10<com:Sup>th< / com:Sup> embodiments of the 6<com:Sup>th< / com:Sup> aspect, which may be and are suggested to be combined with the first, second, third, fourth, fifth, sixth, seventh, 8th, and / or 9th embodiments of the 6th aspect, the isolated antibody or antigen-binding fragment is characterized by a HCDR3 region deviating in composition from average HCDR3 regions. Preferably the isolated antibody or antigen-binding fragment is characterized by a HCDR3 region comprising between 10 and 34 % of tyrosine and / or at least one histidine, preferably between 2 and 20 % of histidine, most preferably between 7 and 20 % of histidine. In some embodiments A of the 10<com:Sup>th< / com:Sup> embodiments of the 6<com:Sup>th< / com:Sup> aspect, the isolated antibody or antigen- binding fragment comprises a HCDR3 having a) <com:Math><semantics>>0<annotation encoding="application / x-tex">> 0< / annotation>< / semantics>< / com:Math> and <com:Math><semantics><35%<annotation encoding="application / x-tex">< 35 \%< / annotation>< / semantics>< / com:Math>, <com:Math><semantics>>8<annotation encoding="application / x-tex">> 8< / annotation>< / semantics>< / com:Math> and <com:Math><semantics><34%<annotation encoding="application / x-tex">< 34 \%< / annotation>< / semantics>< / com:Math>, <com:Math><semantics>≥10<annotation encoding="application / x-tex">\ge 10< / annotation>< / semantics>< / com:Math> and <com:Math><semantics>≤34%<annotation encoding="application / x-tex">\le 34 \%< / annotation>< / semantics>< / com:Math>, or <com:Math><semantics>>15<annotation encoding="application / x-tex">> 15< / annotation>< / semantics>< / com:Math> and <com:Math><semantics><31%<annotation encoding="application / x-tex">< 31 \%< / annotation>< / semantics>< / com:Math> tyrosine (Y) residues, and / or b) <com:Math><semantics>>0<annotation encoding="application / x-tex">> 0< / annotation>< / semantics>< / com:Math> and <com:Math><semantics>≤16%<annotation encoding="application / x-tex">\le 16\%< / annotation>< / semantics>< / com:Math>, <com:Math><semantics>≥2<annotation encoding="application / x-tex">\ge 2< / annotation>< / semantics>< / com:Math> and <com:Math><semantics>≤20%<annotation encoding="application / x-tex">\le 20\%< / annotation>< / semantics>< / com:Math> or <com:Math><semantics>≥7<annotation encoding="application / x-tex">\ge 7< / annotation>< / semantics>< / com:Math> and <com:Math><semantics>≤20%<annotation encoding="application / x-tex">\le 20\%< / annotation>< / semantics>< / com:Math> histidine (H) residues, and c) preferably <com:Math><semantics>>0<annotation encoding="application / x-tex">> 0< / annotation>< / semantics>< / com:Math> and <com:Math><semantics>≤18<annotation encoding="application / x-tex">\le 18< / annotation>< / semantics>< / com:Math> %, <com:Math><semantics>≥7<annotation encoding="application / x-tex">\ge 7< / annotation>< / semantics>< / com:Math> and <com:Math><semantics>≤10<annotation encoding="application / x-tex">\le 10< / annotation>< / semantics>< / com:Math> % or <com:Math><semantics>≥0<annotation encoding="application / x-tex">\ge 0< / annotation>< / semantics>< / com:Math> and <com:Math><semantics>≤7<annotation encoding="application / x-tex">\le 7< / annotation>< / semantics>< / com:Math> % arginine (R) residues, and / or d) preferably <com:Math><semantics>>0<annotation encoding="application / x-tex">> 0< / annotation>< / semantics>< / com:Math> and <com:Math><semantics>≤25<annotation encoding="application / x-tex">\le 25< / annotation>< / semantics>< / com:Math> %, <com:Math><semantics>≥7<annotation encoding="application / x-tex">\ge 7< / annotation>< / semantics>< / com:Math> and <com:Math><semantics>≤16<annotation encoding="application / x-tex">\le 16< / annotation>< / semantics>< / com:Math> % or <com:Math><semantics>≥7<annotation encoding="application / x-tex">\ge 7< / annotation>< / semantics>< / com:Math> and <com:Math><semantics>≤13<annotation encoding="application / x-tex">\le 13< / annotation>< / semantics>< / com:Math> % aspartic acid (D) residues, and / or e) preferably no lysine (K) residues, and / or f) preferably no glutamic acid (E) residues. In some embodiments B of the 10<com:Sup>th< / com:Sup> embodiments of the 6<com:Sup>th< / com:Sup> aspect, which may be the same as or different from the embodiments A, the isolated antibody or antigen-binding fragment comprises a HCDR3 having a) <com:Math><semantics>>0<annotation encoding="application / x-tex">> 0< / annotation>< / semantics>< / com:Math> and <com:Math><semantics><47%<annotation encoding="application / x-tex">< 47 \%< / annotation>< / semantics>< / com:Math>, <com:Math><semantics>>22<annotation encoding="application / x-tex">> 22< / annotation>< / semantics>< / com:Math> and <com:Math><semantics><50%<annotation encoding="application / x-tex">< 50 \%< / annotation>< / semantics>< / com:Math>, <com:Math><semantics>>10<annotation encoding="application / x-tex">> 10< / annotation>< / semantics>< / com:Math> and <com:Math><semantics><34%<annotation encoding="application / x-tex">< 34 \%< / annotation>< / semantics>< / com:Math>, or <com:Math><semantics>>15<annotation encoding="application / x-tex">> 15< / annotation>< / semantics>< / com:Math> and <com:Math><semantics><47%<annotation encoding="application / x-tex">< 47 \%< / annotation>< / semantics>< / com:Math> charged amino acids, and / or b) <com:Math><semantics>>0<annotation encoding="application / x-tex">> 0< / annotation>< / semantics>< / com:Math> and <com:Math><semantics><32%<annotation encoding="application / x-tex">< 32 \%< / annotation>< / semantics>< / com:Math>, <com:Math><semantics>>8<annotation encoding="application / x-tex">> 8< / annotation>< / semantics>< / com:Math> and <com:Math><semantics><30%<annotation encoding="application / x-tex">< 30 \%< / annotation>< / semantics>< / com:Math>, or <com:Math><semantics>>10<annotation encoding="application / x-tex">> 10< / annotation>< / semantics>< / com:Math> and <com:Math><semantics><37%<annotation encoding="application / x-tex">< 37 \%< / annotation>< / semantics>< / com:Math> positively charged amino acids, and / or c) <com:Math><semantics>>0<annotation encoding="application / x-tex">> 0< / annotation>< / semantics>< / com:Math> and <com:Math><semantics><26%<annotation encoding="application / x-tex">< 26 \%< / annotation>< / semantics>< / com:Math>, <com:Math><semantics>≥7<annotation encoding="application / x-tex">\ge 7< / annotation>< / semantics>< / com:Math> and <com:Math><semantics><16%<annotation encoding="application / x-tex">< 16 \%< / annotation>< / semantics>< / com:Math>, or <com:Math><semantics>>7<annotation encoding="application / x-tex">> 7< / annotation>< / semantics>< / com:Math> and <com:Math><semantics><14%<annotation encoding="application / x-tex">< 14 \%< / annotation>< / semantics>< / com:Math> negatively charged amino acids. In some embodiments C of the 10<com:Sup>th< / com:Sup> embodiments of the 6<com:Sup>th< / com:Sup> aspect, which may be the same as or different from embodiments A and / or B, the isolated antibody or antigen-binding fragment comprises a HCDR3 having <com:Math><semantics>>0<annotation encoding="application / x-tex">> 0< / annotation>< / semantics>< / com:Math> and <com:Math><semantics>≤42<annotation encoding="application / x-tex">\le 42< / annotation>< / semantics>< / com:Math> %, <com:Math><semantics>≥10<annotation encoding="application / x-tex">\ge 10< / annotation>< / semantics>< / com:Math> and <com:Math><semantics>≤42<annotation encoding="application / x-tex">\le 42< / annotation>< / semantics>< / com:Math> % or <com:Math><semantics>≥36<annotation encoding="application / x-tex">\ge 36< / annotation>< / semantics>< / com:Math> and <com:Math><semantics>≤43<annotation encoding="application / x-tex">\le 43< / annotation>< / semantics>< / com:Math> % histidine and tyrosine residues in total. Each of the embodiments and descriptions disclosed for CCR8 according to aspect 10 is disclosed herein for chemokine receptor antibodies in general, e.g. with the necessary changes. The inventors believe that the sulfated TRD motif rather than the specific CCR8 sequence promotes the increased frequencies for tyrosine and / or histidine. According to some 11<com:Sup>th< / com:Sup> embodiments of the 6<com:Sup>th< / com:Sup> aspect, which may be and are suggested to be combined with the first, second, third, fourth, fifth, sixth, seventh, eighth, ninth, and / or 10<com:Sup>th< / com:Sup> embodiments of the 6<com:Sup>th< / com:Sup> aspect, the isolated antibody or antigen-binding fragment at least partially modulates CCR8 signaling. For example, an antibody according to the current invention can a) block G-protein independent signaling, and / or b) block G-protein dependent signaling, and / or c) block G-protein dependent and G-protein independent signaling, and / or d) increase G-protein independent signaling, and / or e) increase G-protein dependent signaling, and / or f) increase G-protein dependent and G-protein independent signaling. In the particular context, modulation refers to blocking of ligand induced G-protein independent signaling and induction of G-protein independent signaling. According to some preferred embodiments, the antibody or fragment does not modulate G protein independent signaling of the seven transmembrane receptor. According to some preferred embodiments, the antibody or fragment does not block ligand induced G-protein independent signaling of the target protein. According to some preferred embodiments, the antibody or fragment does not induce G-protein independent signaling. According to some preferred embodiments, the antibody or fragment blocks G protein dependent signaling. G protein dependent signaling can be analyzed by chemotaxis assay or preferably by calcium flux assay, as described elsewhere herein. According to some preferred embodiments, the antibody or fragment blocks G protein dependent signaling of the chemokine receptor but does not block G protein independent signaling of the chemokine receptor, cf. example 10.4. G protein independent signaling of the chemokine receptor is any signaling activity which is not G protein dependent signaling. According to some 12<com:Sup>th< / com:Sup> embodiments of the 6<com:Sup>th< / com:Sup> aspect, which may be and are suggested to be combined with the first, second, third, fourth, fifth, sixth, seventh, 8<com:Sup>th< / com:Sup>, 9<com:Sup>th< / com:Sup>, 10<com:Sup>th< / com:Sup> and 11<com:Sup>th< / com:Sup> embodiments of the 6<com:Sup>th< / com:Sup> aspect, the isolated antibody or antigen-binding fragment is a low internalizing or non-internalizing antibody or antigen binding fragment. Because overexpression may impact the internalization behavior and is less suited to model internalization in a therapeutic setting, internalization is preferably determined using a model cell line with endogenous expression of the target chemokine receptor, cf. example 10.5. For example, internalization can be determined over a time frame or for specific time points. Preferably internalization can be determined after 15 min, 30 min, 1h, 2h, 3h, 6h, 12h, 24h or 48h in a cell endogenously expressing the target. According to some embodiments A of the 12th embodiments of the 6th aspect, the antibody or antigen- binding fragment has an internalization rate in the same order of magnitude as the internalization rate of the isotype control. According to some embodiments B of the 12th embodiments of the 6th aspect, the antibody or antigen- binding fragment is characterized by an internalization into a cell with endogenous target expression which is lower than the 1.5, 2, 3, 4, 5, 6, 7, or 10-fold of the internalization of the isotype control. The isotype control for an antibody can be selected as known in the art to match the isotype of the antibody as closely as possible, but without binding to the target. According to some embodiments C of the 12th embodiments of the 6th aspect, the antibody or antigen- binding fragment is characterized by an internalization into a cell with endogenous target expression which is lower than 150 %, 175 %, 200 %, 300 %, 400 % or 500 % of the internalization of the isotype control e.g. after 15 min, 30 min, 1h, 2h, 3h, 6h, 12h, 24h or 48h. According to some 13<com:Sup>th< / com:Sup> embodiments of the 6<com:Sup>th< / com:Sup> aspect, which may be and are suggested to be combined with the first, second, third, fourth, fifth, sixth, seventh, 8th, 9th, 10th, 11th and / or 12th embodiments of the 6<com:Sup>th< / com:Sup> aspect, the isolated antibody or antigen-binding fragment induces ADCC and / or ADCP of cells expressing the target receptor of the antibody. In some preferred embodiments of the 13th embodiments of the 6th aspect, the antibody or antigen-binding fragment is afucosylated. In some embodiments A1 of the 13<com:Sup>th< / com:Sup> embodiments of the 6th aspect, the antibody or antigen-binding fragment binds to human Fc gamma receptor IIIA variant V176 (CD16a) with a dissociation constant (KD) lower than 530 nM, 500 nM, 450 nM, 400 nM, 300 nM or 200 nM. Preferably, the KD can be determined using surface plasmon resonance. In some embodiments B1 of the 13th embodiments of the 6th aspect, which may be the same as or different from the embodiments A1, the antibody or antigen-binding fragment induces antibody- dependent cell-mediated cytotoxicity (ADCC) in target cells expressing the target receptor via human effector cells, such as human NK cells. ADCC induction can be analyzed with an assay known in the art, for example as described according to examples 10.3.3 ff. or elsewhere herein. Preferably the assay is performed with Treg cells wherein at least 80 % or 85 % of the Treg cells express CCR8. In some embodiments C1 of the 13th embodiments of the 6th aspect, which may be the same as or different from the embodiments A1 or B1, the ADCC-induced maximal depletion of cells expressing the target receptor is at least 30 %, 35 %, 40 %, 45 %, 50 %, 55 %, 60 %, 70 %, 80 %, 90 %, 95 %, 98 % or 99 %. In some embodiments D1 of the 13<com:Sup>th< / com:Sup> embodiments of the 6th aspect, which may be the same as or different from the embodiments A1, B1 or C1, the EC50 for ADCC-induced depletion of target expressing cells is below 500 pM, 400 pM, 300 pM, 200 pM, 100 pM, 50 pM, 25 pM, 20 pM, 12.5 pM, 10 pM, 5 pM or 2.5 pM. In some embodiments A2 of the 13<com:Sup>th< / com:Sup> embodiments of the 6th aspect, which may or may not be the same as the embodiments A1, B1, C1 and / or D1, the antibody or antigen-binding fragment binds to human Fc gamma RIIA (CD32a) with a dissociation constant (KD) lower than 30 µM, 20 µM, 10 µM, 5 µM or 1 μM. In some embodiments B2 of the 13<com:Sup>th< / com:Sup> embodiments of the 6th aspect, which may be the same as the embodiments A1, B1, C1 and / or D1, and which may be the same as the embodiments A2, the antibody or antigen-binding fragment induces antibody-dependent cell-mediated phagocytosis (ADCP) in cells expressing the target receptor via human effector cells, such as human macrophages. For example, the human macrophages can be M2 or M1 macrophages. In some embodiments C2 of the 13<com:Sup>th< / com:Sup> embodiments of the 6th aspect, which may be the same as the embodiments A1, B1, C1 and / or D1, and which may be the same as the embodiments A2 and / or B2, the ADCP-induced maximal depletion of cells expressing the target receptor is at least 5, 10, 15, 20, 25, 30, 40 or 50 %. In some embodiments D2 of the 13<com:Sup>th< / com:Sup> embodiments of the 6th aspect, which may be the same as the embodiments A1, B1, C1 and / or D1, and which may be the same as the embodiments A2, B2, and / or C2, the EC50 for ADCP-induced depletion of activated human regulatory T cells is below 1500 pM, 1000 pM, 500 pM, 250 pM, 200 pM, 150 pM, 100 pM, 75 pM, 50 pM, 25 pM or 10 pM. In some preferred of the 13th embodiments of the 6th aspect, there is provided an isolated antibody or antigen-binding fragment thereof, specifically binding to a chemokine receptor, wherein the antibody or antigen-binding fragment a) binds to human Fc gamma receptor IIIA variant V176 (CD16a) with a dissociation constant (KD) lower than 530 nM, 500 nM, 450 nM, 400 nM, 300 nM or 200 nM, and / or b) binds to human Fc gamma RIIA (CD32a) with a dissociation constant (KD) lower than 30 μM, 20 <com:Math><semantics>μ<annotation encoding="application / x-tex">\mu< / annotation>< / semantics>< / com:Math>M, 10 <com:Math><semantics>μ<annotation encoding="application / x-tex">\mu< / annotation>< / semantics>< / com:Math>M, 5 <com:Math><semantics>μ<annotation encoding="application / x-tex">\mu< / annotation>< / semantics>< / com:Math>M or 1 <com:Math><semantics>μ<annotation encoding="application / x-tex">\mu< / annotation>< / semantics>< / com:Math>M. In some preferred of the 13<com:Sup>th< / com:Sup> embodiments of the 6th aspect, there is provided an isolated antibody or antigen-binding fragment thereof, specifically binding to a chemokine receptor, wherein the antibody or antigen-binding fragment a) induces antibody-dependent cell-mediated cytotoxicity (ADCC) in target cells expressing the human chemokine receptor via human effector cells, such as human NK cells, and / or b) induces antibody-dependent cell-mediated phagocytosis (ADCP) in target cells expressing the human chemokine receptor via human effector cells, such as human macrophages. In some preferred of the 13<com:Sup>th< / com:Sup> embodiments of the 6th aspect, there is provided an isolated antibody or antigen-binding fragment thereof, specifically binding to a chemokine receptor, wherein a) the ADCC-induced maximal depletion in target cells expressing the human chemokine receptor is at least 25 %, 30 %, 35 %, 40 %, 45 %, 50 %, 55 %, 60 %, 70 %, 80 %, 90 %, 95 %, 98 % or 99 %, and / or b) the ADCP-induced maximal depletion in target cells expressing the human chemokine receptor is at least 5 %, 10 %, 15 %, 20 %, 25 %, 30 %, 40 % or 50 %, and / or c) the maximal depletion of target cells expressing the human chemokine receptor, is at least 30 %, 35 %, 40 %, 45 %, 50 %, 55 %, 60 %, 70 %, 80 %, 90%, 95 % or 99 %. In some preferred of the 13th embodiments of the 6th aspect, there is provided an isolated antibody or antigen-binding fragment thereof, specifically binding to a chemokine receptor, wherein a) the EC50 for ADCC-induced depletion of target cells expressing the human chemokine receptor is below 200 pM, 100 pM, 50 pM, 25 pM, 12.5 pM, 10 pM or 5 pM and / or b) the EC50 for ADCP-induced depletion of target cells expressing the human chemokine receptor is below 500 pM, 250 pM, 200 pM, 150 pM, 100 pM, 75 pM, 50 pM or 25 pM. According to some 14<com:Sup>th< / com:Sup> embodiments of the 6<com:Sup>th< / com:Sup> aspect, which may be and are suggested to be combined with the first, second, third, fourth, fifth, sixth, seventh, 8th, 9th, 10th, 11th, 12th and / or 13th embodiments of the 6<com:Sup>th< / com:Sup> aspect, the isolated antibody or antigen-binding fragment comprises a human, rat or murine IgG antibody, preferably a human IgG1 antibody or a murine IgG2a antibody, cf. example 6 and 8. According to some 15th embodiments of the 6<com:Sup>th< / com:Sup> aspect, which may be and are suggested to be combined with the first, second, third, fourth, fifth, sixth, seventh, 8th, 9th, 10th, 11th, 12th 13th and / or 14th embodiments of the 6<com:Sup>th< / com:Sup> aspect, the isolated antibody or antigen-binding fragment is an scFv, Fab, Fab' or a F(ab')2 fragment, cf. example 6. The antibodies according to the current aspect can be conjugated, e.g. as discussed elsewhere herein. The antibodies according to the current aspect can be used in the treatment of a tumor or a disease characterized by the involvement of cells expressing the seven transmembrane receptor, e.g. as discussed elsewhere herein. The antibodies according to the current aspect can be used as a diagnostic agent in vivo or in vitro, e.g. as discussed elsewhere herein. Furthermore, there is provided a kit comprising an antibody according to the current aspect with instructions for use. PREFERRED COMBINATIONS ACCORDING TO THE 6<com:Sup>TH< / com:Sup> ASPECT The following embodiments disclose preferred combinations of the sixth aspect, thereby emphasizing the modular nature of the invention. Provided according to a preferred embodiment I is an isolated antibody or antigen-binding fragment thereof, specifically binding to a first isolated sulfated polypeptide which comprises the tyrosine rich domain (TRD) of a seven transmembrane receptor, and optionally its LID domain, wherein at least 25 %, at least 50 % or at least 75 % of the tyrosine residues of the TRD are sulfated. Provided according to a preferred embodiment II is the isolated antibody or antigen-binding fragment according to preferred embodiment I, wherein the cysteine between the TRD and the LID domain has been removed or has been exchanged into a different amino acid. Provided according to a preferred embodiment III is the isolated antibody or antigen-binding fragment according to preferred embodiment I or II, wherein the seven transmembrane receptor is a human, cynomolgus or mouse seven transmembrane receptor. Provided according to a preferred embodiment IV is the isolated antibody or antigen-binding fragment according to any of preferred embodiments I, II or III, wherein the seven transmembrane receptor is a) a CC chemokine receptor, preferably CCR1, CCR2, CCR3, CCR4, CCR5, CCR6, CCR7, CCR8, CCR9 or CCR10, b) a CXC chemokine receptor, preferably CXCR1, CXCR2, CXCR3, CXCR4, CXCR5, or CXCR6, or c) CX3CR1 or CXCR1. Provided according to a preferred embodiment V is an isolated antibody or antigen-binding fragment according to any of preferred embodiments I, II, III or IV, said first isolated sulfated polypeptide comprising or consisting of a sequence according to a. SEQ ID NO:1, SEQ ID NO:4, SEQ ID NO:2, SEQ ID NO:5, SEQ ID NO:3 or SEQ ID NO:6, preferably wherein at least Y10 and / or Y18 have been sulfated, or b. SEQ ID NO:7, SEQ ID NO:10, SEQ ID NO:8 or SEQ ID NO:11, preferably wherein at least Y26 has been sulfated, or C. SEQ ID NO:9 or SEQ ID NO:12, preferably wherein at least Y37 and / or Y39 has been sulfated, or d. SEQ ID NO:13 or SEQ ID NO:16, preferably wherein Y16 and / or Y17 have been sulfated, or e. SEQ ID NO:14 or SEQ ID NO:17, preferably wherein Y16 has been sulfated, or f. SEQ ID NO:15 or SEQ ID NO:18 preferably wherein Y20 and / or Y22 have been sulfated, or g. SEQ ID NO:19, SEQ ID NO:22, SEQ ID NO:20, SEQ ID NO:23, SEQ ID NO:21 or SEQ ID NO:24, preferably wherein at least Y22 has been sulfated and preferably furthermore Y16, Y19 and / or Y20 have been sulfated, or h. SEQ ID NO:25, SEQ ID NO:28, SEQ ID NO:26 or SEQ ID NO:29, preferably wherein two, three or all of Y3, Y10, Y14 and Y15 have been sulfated, or i. SEQ ID NO:27 or SEQ ID NO:30, preferably wherein two or three of Y10, Y12 and Y16 have been sulfated, or 1. SEQ ID NO:31 or SEQ ID NO:34, preferably wherein at least two or three of Y18, Y26 and Y27 have been sulfated, or k. SEQ ID NO:32 or SEQ ID NO:35, preferably wherein at least two or three of Y23, Y31 and Y32 have been sulfated, or 1. SEQ ID NO:33 or SEQ ID NO:36, preferably wherein at least two or three of Y13, Y18 and Y19 have been sulfated, or m. SEQ ID NO:37, SEQ ID NO:40, SEQ ID NO:38 or SEQ ID NO:41, preferably wherein one or both of Y8 and Y17 have been sulfated, or n. SEQ ID NO:39 or SEQ ID NO:42, preferably wherein one or both of Y8 and Y17 and optionally Y20 have been sulfated, or o. SEQ ID NO:43, SEQ ID NO:44, SEQ ID NO:46 or SEQ ID NO:47, preferably wherein at least two or all of Y3, Y15 and Y17 have been sulfated, or p. SEQ ID NO:45 or SEQ ID NO:48, preferably wherein at least two or all of Y3, Y14 and Y15 have been sulfated, or q. SEQ ID NO:61, SEQ ID NO:64, SEQ ID NO:62 or SEQ ID NO:65, preferably wherein at least Y28, and preferably also Y17 and / or Y37 has been sulfated, or r. SEQ ID NO:63 or SEQ ID NO:66, preferably wherein at least Y28 has been sulfated, and preferably also Y19 has been sulfated, or S. SEQ ID NO:67, SEQ ID NO:70, SEQ ID NO:68 or SEQ ID NO:71, preferably wherein at least one or both of Y14 and Y22 has been sulfated, or t. SEQ ID NO:69 or SEQ ID NO:72, preferably wherein at least one, two or all of Y14, Y17 and Y22 has been sulfated, or u. SEQ ID NO:73 or SEQ ID NO:76, preferably wherein Y27 has been sulfated, or <com:Math><semantics>𝑽<annotation encoding="application / x-tex">\mathbf{V}< / annotation>< / semantics>< / com:Math>. SEQ ID NO:74 or SEQ ID NO:77, preferably wherein at least one of Y14 and Y28 has been sulfated, or w. SEQ ID NO:75 or SEQ ID NO:78, preferably wherein at least Y6 has been sulfated, or X. SEQ ID NO:79 or SEQ ID NO:82, preferably wherein Y23 and / or Y25 have been sulfated, or У. SEQ ID NO:80 or SEQ ID NO:83, preferably wherein Y20 and / or Y22 have been sulfated, or <com:Math><semantics>Z<annotation encoding="application / x-tex">Z< / annotation>< / semantics>< / com:Math>. SEQ ID NO:81 or SEQ ID NO:84, preferably wherein Y24 has been sulfated, or aa. SEQ ID NO:85, SEQ ID NO:88, SEQ ID NO:86, SEQ ID NO:89, SEQ ID NO:87 or SEQ ID NO:90, preferably wherein at least one or both of Y27 and Y29 have been sulfated, or bb. SEQ ID NO:91, SEQ ID NO:94, SEQ ID NO:92 or SEQ ID NO:95, preferably wherein at least Y12 and / or Y21 have been sulfated, or cc. SEQ ID NO:93 or SEQ ID NO:96, preferably wherein at least Y23 and / or Y14 have been sulfated, or dd. SEQ ID NO:97, SEQ ID NO:100, SEQ ID NO:98 or SEQ ID NO:101, preferably wherein at least one of Y3 and Y27 have been sulfated, or ee. SEQ ID NO:99 or SEQ ID NO:102, preferably wherein at least Y3 and / or Y14 and / or Y20 and / or Y26 have been sulfated, or ff. SEQ ID NO:103 or SEQ ID NO:106, preferably wherein at least one or both of Y6 and Y10 has been sulfated, or gg. SEQ ID NO:104 or SEQ ID NO:107, preferably wherein at least two or all of Y4, Y7 and Y39 have been sulfated, or hh. SEQ ID NO:105 or SEQ ID NO:108, preferably wherein at least one or both of Y11 and Y15 have been sulfated, or ii. SEQ ID NO:157 or SEQ ID NO:160, preferably wherein at least Y14 has been sulfated, or ]]. SEQ ID NO:158, preferably wherein at least Y20 has been sulfated, or kk. SEQ ID NO:161, preferably wherein at least Y20 or Y22 has been sulfated, or 11. SEQ ID NO:159 or SEQ ID NO:162, preferably wherein at least Y15 has been sulfated, or mm. SEQ ID NO:163 or SEQ ID NO:166, preferably wherein at least Y27 has been sulfated, or nn. SEQ ID NO:164, preferably wherein at least Y14 has been sulfated or oo. SEQ ID NO:167, preferably wherein at least Y14 or Y28 has been sulfated, or pp. SEQ ID NO:165 or SEQ ID NO:168, preferably wherein at least Y6 has been sulfated. Provided according to a preferred embodiment VI is the isolated antibody or antigen-binding fragment according to any of preferred embodiments I, II, III, IV or V, wherein the dissociation constant or the EC50 of the antibody for binding the first isolated sulfated polypeptide and / or for said seven transmembrane receptor is below 150 nM, 100 nM, 10 nM, 5 nM, 2.5 nM, 1 nM, 0.5 or 0.25 nM. Provided according to a preferred embodiment VII is an isolated antibody or antigen-binding fragment according to any of preferred embodiments I to VI, wherein the isolated antibody or antigen-binding fragment specifically binds to a second isolated sulfated polypeptide which comprises the TRD of a seven transmembrane receptor, preferably wherein the seven transmembrane receptor of the TRD comprised by the second isolated sulfated polypeptide a. is different from the seven transmembrane receptor of the TRD comprised by the first isolated sulfated polypeptide, or b. is the corresponding seven transmembrane receptor of the TRD comprised by the first isolated sulfated polypeptide but from a different species. Provided according to a preferred embodiment VIII is the isolated antibody or antigen-binding fragment according to preferred embodiment VII, wherein the dissociation constant or the EC50 of the antibody for binding the second isolated sulfated polypeptide and / or for binding the second seven transmembrane receptor is below 10 nM, 5 nM, 2.5 nM, 1 nM, 0.5 or 0.25 nM. Provided according to a preferred embodiment IX is an isolated antibody or antigen-binding fragment according to any of preferred embodiments I to VIII, wherein the dissociation constant (KD) of the antibody for binding the first isolated sulfated polypeptide is lower than the dissociation constant (KD) of the antibody for binding a first isolated non-sulfated polypeptide having the same sequence as the first isolated sulfated polypeptide. Provided according to a preferred embodiment X is the isolated antibody or antigen-binding fragment according to preferred embodiment IX, wherein the dissociation constant and / or EC50 of the antibody for binding the first isolated non-sulfated polypeptide is higher than 150 nM, 250 nM, 500 nM, 1 µM, 2 µM or 3 µM, or is not detectable. Provided according to a preferred embodiment XI is the isolated antibody or antigen- binding fragment according to any of preferred embodiments IX or X, wherein the dissociation constant or the EC50 of the antibody or fragment for binding the first isolated sulfated polypeptide is below 10 nM, 5 nM, 2.5 nM, 1 nM, 0.5 nM or 0.25 nM, and wherein the dissociation constant of the antibody or fragment for binding the first isolated non-sulfated polypeptide is higher than 10 nM, 25 nM, 50 nM, 100 nM, 250 nM or 500 nM, or is not detectable. Provided according to a preferred embodiment XII is the isolated antibody or antigen-binding fragment according to any of preferred embodiments I to XI, wherein the antibody comprises human, rat or mouse derived CDRs. Provided according to a preferred embodiment XIII is the isolated antibody or antigen-binding fragment according to any of preferred embodiments I to XII, wherein the antibody a. comprises human derived CDRs, and / or b. is cross reactive for human and cynomolgus, and / or C. is characterized by a HCDR3 region comprising between 10 and 34 % of tyrosine and / or between 2 and 20 % of histidine, and / or d. does not modulate G protein independent signaling of the seven transmembrane receptor, and / or e. is a non-internalizing antibody or is characterized by an internalization into a cell with endogenous target expression which is lower than the 1.5, 2, 3, 4, 5, 6, 7, or 10-fold of the internalization of the isotype control, and / or f. induces ADCC and / or ADCP g. is a human, rat or murine IgG antibody, preferably a human IgG1 antibody or a murine IgG2a antibody, and / or h. is an scFv, Fab, Fab' or a F(ab')2 fragment. Provided according to a preferred embodiment XIV is a conjugate comprising an antibody or antigen- binding fragment according to any of preferred embodiments I to XIII, preferably wherein the conjugate comprises a. a radioactive element, b. a cytotoxic agent, such as an auristatin, a maytansinoid, a kinesin-spindle protein inhibitor, a nicotinamide phosphoribosyltransferase inhibitor or a pyrrolobenzodiazepine derivative, C. a further antibody or antigen-binding fragment, or d. a chimeric antigen receptor. Provided according to a preferred embodiment XV is an antibody or antigen-binding fragment according to any of preferred embodiments I to XIII or a conjugate according to preferred embodiment XIV for use in the treatment of a tumor or a disease characterized by the involvement of cells expressing the seven transmembrane receptor, optionally in combination with an antibody targeting a checkpoint inhibitor. Provided according to a preferred embodiment XVI is the antibody or antigen-binding fragment according to any of preferred embodiments I to XIII or a conjugate according to preferred embodiment XIV for use as a diagnostic agent in vivo or in vitro. Provided according to a preferred embodiment XVII is a kit comprising an antibody or antigen-binding fragment according to any of preferred embodiments I to XIII or a conjugate according to preferred embodiment XIV with instructions for use. ANTIBODIES BINDING CCR8 The following aspects 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17 and 18 relate to antibodies specifically binding to CCR8. While each aspect is described individually, the different structural or functional aspects may be combined and are suggested to be combined with each other, except where obviously incompatible. Furthermore, each embodiment in each aspect may be combined with each embodiment in the same or in a different aspect, except where obviously incompatible. If not explicitly stated otherwise, the CCR8 may be from any species e.g. human, monkey, macaca fascicularis (cynomolgus monkey), macaca mulatta (rhesus macaque), rodent, mouse, rat, horse, bovine, pig, dog, cat and camel CCR8. Antibodies binding CCR8 from at least two species, wherein one species is human, are highly preferred, and are suggested to be combined with each embodiment disclosed for these aspects. Antibodies having human derived CDRs are highly preferred and are suggested to be combined with each embodiment disclosed for these aspects. According to the current aspects, antibodies having a HCDR3 domain characterized by a frequency of at least 21 % tyrosine residues and / or at least 2 %, 7 % or 10 % histidine are highly preferred and are suggested to be combined with each embodiment disclosed for the current aspect. According to the current aspects, antibodies inducing both, ADCC and ADCP, such as afucosylated antibodies, are highly preferred, and are suggested to be combined with each embodiment disclosed for these aspects. According to the current aspects, low internalizing or non- internalizing antibodies or fragments are highly preferred and are suggested to be combined with each embodiment disclosed for these aspects. Some highly preferred characterizing features which are applicable for each of the described aspects are described under section "Preferred combinations according to 'all aspects'". ASPECT 7 – CCR8 ANTIBODY BINDING SULFATED TRD The extracellular domains of human CCR8 can be structured into four regions: (i) an N-terminal domain which can be subdivided into a) the membrane-distal tyrosine-rich domain (TRD), formed by amino acids 1 to 24 (SEQ ID NO:43) b) a cysteine at amino acid position 25, and c) a LID domain, formed by amino acids 26 to 35 (SEQ ID NO:49) (iii) an extracellular domain 1 (ECL1) according to SEQ ID NO:52, (iii) an extracellular domain 2 (ECL2) according to SEQ ID NO:55, and (iv) an extracellular domain 3 (ECL3) according to SEQ ID NO:58. According to a 7th aspect, which may be or may not be the same as the 6<com:Sup>th< / com:Sup> aspect, there is provided an isolated antibody or antigen-binding fragment thereof, specifically binding to the sulfated tyrosine rich domain of CCR8. For example, the antibody or antigen-binding fragment binds to a first isolated sulfated polypeptide which comprises a) the tyrosine rich domain (TRD) of CCR8 or b) the N term of CCR8 including the TRD, optionally wherein at least the cysteine between the TRD and the LID domain has been removed or has been exchanged into a different amino acid. A sulfated polypeptide according to the current aspect is a polypeptide wherein preferably at least 25 %, at least 50 % or at least 75 % of the tyrosine residues of the TRD are sulfated. Where the polypeptide comprises the N term of CCR8 including the TRD, preferably the cysteine between the TRD and the LID domain has been exchanged into a serine or has been removed. Without being bound by theory, the specific recognition of the provided sulfation pattern for CCR8 seems to influence if the antibody competes with CCL1, the natural ligand for CCR8, and also if and how the antibody agonizes or antagonizes the CCR8 signaling, e.g. as described according to the 11<com:Sup>th< / com:Sup> aspect. In some preferred embodiments according to the current aspect, the inventive antibody binds sulfated TRD of human and / or cynomolgus CCR8 with a KD value of < 5E-8 M, < 4E-8 M, < 3E-8 M, < 2E-8 M, <com:Math><semantics><1E−8M,<9E−9M,<8E−9M,<7E−9M,<6E−9M,<5E−9M,<4E−9M,<3E−9M,<2.5E−9M,<2E−9M,<8E−9M,<8E−9M,<8E−9M,<8E−9M,<8E−9M,<8E−9M,<8E−9M,<8E−9M,<8E−9M,<8E−9M,<8E−9M,<8E−9M<annotation encoding="application / x-tex">< 1E-8 M, < 9E-9 M, < 8E-9 M, < 7E-9 M, < 6E-9 M, < 5E-9 M, < 4E-9 M, < 3E-9 M, < 2.5E-9 M, < 2E-9 M, < 8E-9 M, < 8E-9 M, < 8E-9 M, < 8E-9 M, < 8E-9 M, < 8E-9 M, < 8E-9 M, < 8E-9 M, < 8E-9 M, < 8E-9 M, < 8E-9 M, < 8E-9 M< / annotation>< / semantics>< / com:Math> 9 M, < 1.5E-9 M, < 1E-9 M, < 9E-10 M, < 8E-10 M, < 7E-10 M, < 6E-10 M, < 5E-10 M, < 4E-10 M, < 3E-10 M, < 2.5E-10 M, < 2E-10 M, < 1.5E-10 M, < 1E-10 M, or < 9E-11 M. For example, the inventive antibody may bind sulfated TRD of human and / or cynomolgus CCR8 with a KD value between < 8E-9 M and > 4E-10 M. For example, the inventive antibody may bind sulfated TRD of human and / or cynomolgus CCR8 with a KD value between < 8E-9 M and > 5.5E-10 M. In some further preferred of these embodiments, the inventive antibody binds the sulfated N term (i.e. comprising the aforementioned sulfated TRD) of human and / or cynomolgus CCR8 with substantially the same KD value. In some most preferred of these embodiments, the inventive antibody does substantially not bind non-sulfated TRD of human and / or cynomolgus CCR8. In some preferred embodiments according to the current aspect, the inventive antibody binds sulfated N term of human and / or cynomolgus CCR8 with a KD value of < 5E-8 M, < 4E-8 M, < 3E-8 M, < 2E-8 M, <com:Math><semantics><1E−8M<annotation encoding="application / x-tex">< 1E-8 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><9E−9M<annotation encoding="application / x-tex">< 9E-9 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><8E−9M<annotation encoding="application / x-tex">< 8E-9 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><7E−9M<annotation encoding="application / x-tex">< 7E-9 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><6E−9M<annotation encoding="application / x-tex">< 6E-9 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><5E−9M<annotation encoding="application / x-tex">< 5E-9 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><4E−9M<annotation encoding="application / x-tex">< 4E-9 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><3E−9M<annotation encoding="application / x-tex">< 3E-9 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><2.5E−9M<annotation encoding="application / x-tex">< 2.5E-9 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><2E−9M<annotation encoding="application / x-tex">< 2E-9 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><3E−9M<annotation encoding="application / x-tex">< 3E-9 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><3E−9M<annotation encoding="application / x-tex">< 3E-9 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><3E−9M<annotation encoding="application / x-tex">< 3E-9 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><3E−9M<annotation encoding="application / x-tex">< 3E-9 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><3E−9M<annotation encoding="application / x-tex">< 3E-9 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><3E−9M<annotation encoding="application / x-tex">< 3E-9 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><3E−9M<annotation encoding="application / x-tex">< 3E-9 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><3E−9M<annotation encoding="application / x-tex">< 3E-9 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><<annotation encoding="application / x-tex"><< / annotation>< / semantics>< / com:Math> 9 M, < 1.5E-9 M, < 1E-9 M, < 9E-10 M, < 8E-10 M, < 7E-10 M, < 6E-10 M, < 5E-10 M, < 4E-10 M, < <com:Math><semantics>3E−10M<annotation encoding="application / x-tex">3E-10 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><2.5E−10M<annotation encoding="application / x-tex">< 2.5E-10 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><2E−10M<annotation encoding="application / x-tex">< 2E-10 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><1.5E−10M<annotation encoding="application / x-tex">< 1.5E-10 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><1E−10M<annotation encoding="application / x-tex">< 1E-10 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><9E−11M<annotation encoding="application / x-tex">< 9E-11 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><8E−11M<annotation encoding="application / x-tex">< 8E-11 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><7E−11M<annotation encoding="application / x-tex">< 7E-11 M< / annotation>< / semantics>< / com:Math>, <com:Math><semantics><6E−10M<annotation encoding="application / x-tex">< 6E-10 M< / annotation>< / semantics>< / com:Math> 11 M, or < 5E-11 M. For example, the inventive antibody may bind sulfated N term of human and / or cynomolgus CCR8 with a KD value between < 8E-9 M and > 8E-11 M. For example, the inventive antibody may bind sulfated N term of human and / or cynomolgus CCR8 with a KD value between < 8E-9 M and > 7.5E-11 M. In some further preferred of these embodiments, the inventive antibody binds sulfated TRD (i.e., a subsequence of the aforementioned sulfated N term) of human and / or cynomolgus CCR8 with substantially the same KD value or a KD value within the same order of magnitude. In some most preferred of these embodiments, the inventive antibody does substantially not bin...

Claims

CLAIMS:

1. An isolated anti-CCR8 antibody or antigen-binding fragment thereof comprising six CDR sequences wherein each CDR has an amino acid sequence set forth in one of (a) to (r): a. SEQ ID NO:420, SEQ ID NO:421, SEQ ID NO:422, SEQ ID NO:424, SEQ ID NO:425 and SEQ ID NO:426, b. SEQ ID NO:600, SEQ ID NO:601, SEQ ID NO:602, SEQ ID NO:604, SEQ ID NO:605 and SEQ ID NO:606, c. SEQ ID NO:618, SEQ ID NO:619, SEQ ID NO:620, SEQ ID NO:622, SEQ ID NO:623 and SEQ ID NO:624, d. SEQ ID NO:661, SEQ ID NO:662, SEQ ID NO:663, SEQ ID NO:665, SEQ ID NO:666 and SEQ ID NO:667, e. SEQ ID NO:681, SEQ ID NO:682, SEQ ID NO:683, SEQ ID NO:685, SEQ ID NO:686 and SEQ ID NO:687, f. SEQ ID NO:703, SEQ ID NO:704, SEQ ID NO:705, SEQ ID NO:707, SEQ ID NO:708 and SEQ ID NO:709, g. SEQ ID NO:723, SEQ ID NO:724, SEQ ID NO:725, SEQ ID NO:727, SEQ ID NO:728 and SEQ ID NO:729, h. SEQ ID NO:743, SEQ ID NO:744, SEQ ID NO:745, SEQ ID NO:747, SEQ ID NO:748 and SEQ ID NO:749, i. SEQ ID NO:763, SEQ ID NO:764, SEQ ID NO:765, SEQ ID NO:767, SEQ ID NO:768 and SEQ ID NO:769, SEQ ID NO:783, SEQ ID NO:784, SEQ ID NO:785, SEQ ID NO:787, SEQ ID NO:788 and SEQ ID NO:789, k. SEQ ID NO:803, SEQ ID NO:804, SEQ ID NO:805, SEQ ID NO:807, SEQ ID NO:808 and SEQ ID NO:809, 1. SEQ ID NO:827, SEQ ID NO: 828, SEQ ID NO: 829, SEQ ID NO: 831, SEQ ID NO:832 and SEQ ID NO:833, m. SEQ ID NO:847, SEQ ID NO: 848, SEQ ID NO: 849, SEQ ID NO: 851, SEQ ID NO:852 and SEQ ID NO:853, n. SEQ ID NO:867, SEQ ID NO: 868, SEQ ID NO: 869, SEQ ID NO: 871, SEQ ID NO:872 and SEQ ID NO:873, Ο. SEQ ID NO:887, SEQ ID NO: 888, SEQ ID NO: 889, SEQ ID NO: 891, SEQ ID NO:892 and SEQ ID NO:893, p. SEQ ID NO:907, SEQ ID NO: 908, SEQ ID NO: 909, SEQ ID NO: 911, SEQ ID NO:912 and SEQ ID NO:913, q. SEQ ID NO:927, SEQ ID NO: 928, SEQ ID NO: 929, SEQ ID NO: 931, SEQ ID NO:932 and SEQ ID NO:933, and r. SEQ ID NO:947, SEQ ID NO: 948, SEQ ID NO: 949, SEQ ID NO: 951, SEQ ID NO:952 and SEQ ID NO:

953.

2. The isolated anti-CCR8 antibody or antigen-binding fragment thereof of claim 1 further comprising a variable heavy chain sequence and / or a variable light chain sequence having an amino acid sequence set forth in one of (a) to (r): a. a variable heavy chain sequence according to SEQ ID NO:419 and / or a variable light chain sequence according to SEQ ID NO:423, b. a variable heavy chain sequence according to SEQ ID NO:599 and / or a variable light chain sequence according to SEQ ID NO:603, c. a variable heavy chain sequence according to SEQ ID NO:617 and / or a variable light chain sequence according to SEQ ID NO:621, d. a variable heavy chain sequence according to SEQ ID NO:660 and / or a variable light chain sequence according to SEQ ID NO:664, e. a variable heavy chain sequence according to SEQ ID NO:680 and / or a variable light chain sequence according to SEQ ID NO:684, f. a variable heavy chain sequence according to SEQ ID NO:702 and / or a variable light chain sequence according to SEQ ID NO:706, g. a variable heavy chain sequence according to SEQ ID NO:722 and / or a variable light chain sequence according to SEQ ID NO:726, h. a variable heavy chain sequence according to SEQ ID NO:742 and / or a variable light chain sequence according to SEQ ID NO:746, i. a variable heavy chain sequence according to SEQ ID NO:762 and / or a variable light chain sequence according to SEQ ID NO:766, J. a variable heavy chain sequence according to SEQ ID NO:782 and / or a variable light chain sequence according to SEQ ID NO:786, k. a variable heavy chain sequence according to SEQ ID NO:802 and / or a variable light chain sequence according to SEQ ID NO:806, 1. a variable heavy chain sequence according to SEQ ID NO:826 and / or a variable light chain sequence according to SEQ ID NO:830, m. a variable heavy chain sequence according to SEQ ID NO:846 and / or a variable light chain sequence according to SEQ ID NO:850, n. a variable heavy chain sequence according to SEQ ID NO:866 and / or a variable light chain sequence according to SEQ ID NO:870, 0. a variable heavy chain sequence according to SEQ ID NO:886 and / or a variable light chain sequence according to SEQ ID NO:890, p. a variable heavy chain sequence according to SEQ ID NO:906 and / or a variable light chain sequence according to SEQ ID NO:910, q. a variable heavy chain sequence according to SEQ ID NO:926 and / or a variable light chain sequence according to SEQ ID NO:930, or r. a variable heavy chain sequence according to SEQ ID NO:946 and / or a variable light chain sequence according to SEQ ID NO:

950.

3. The isolated anti-CCR8 antibody or antigen-binding fragment thereof of claim 1 further comprising a heavy chain sequence and a light chain sequence having an amino acid sequence set forth in one of (a) to (r): a. a heavy chain according to SEQ ID NO:435 and a light chain according to SEQ ID NO:436, b. a heavy chain according to SEQ ID NO:615 and a light chain according to SEQ ID NO:616, c. a heavy chain according to SEQ ID NO:633 and a light chain according to SEQ ID NO:634, d. a heavy chain according to SEQ ID NO:676 and a light chain according to SEQ ID NO:677, e. a heavy chain according to SEQ ID NO:696 and a light chain according to SEQ ID NO:697, f. a heavy chain according to SEQ ID NO:718 and a light chain according to SEQ ID NO:719, g. a heavy chain according to SEQ ID NO:738 and a light chain according to SEQ ID NO:739, h. a heavy chain according to SEQ ID NO:758 and a light chain according to SEQ ID NO:759, i. a heavy chain according to SEQ ID NO:778 and a light chain according to SEQ ID NO:779, j. a heavy chain according to SEQ ID NO:798 and a light chain according to SEQ ID NO:799, k. a heavy chain according to SEQ ID NO:818 and a light chain according to SEQ ID NO:819, 1. a heavy chain according to SEQ ID NO:842 and a light chain according to SEQ ID NO:843, m. a heavy chain according to SEQ ID NO:862 and a light chain according to SEQ ID NO:863, n. a heavy chain according to SEQ ID NO:882 and a light chain according to SEQ ID NO:883, 0. a heavy chain according to SEQ ID NO:902 and a light chain according to SEQ ID NO:903, p. a heavy chain according to SEQ ID NO:922 and a light chain according to SEQ ID NO:923, q. a heavy chain according to SEQ ID NO:942 and a light chain according to SEQ ID NO:943, and r. a heavy chain according to SEQ ID NO:962 and a light chain according to SEQ ID NO:

963.

4. A polynucleotide encoding an antibody or antigen-binding fragment according to claim 1; wherein the antibody or antigen-binding fragment comprises six CDR sequences wherein each CDR has an amino acid sequence set forth in one of (a) to (r): a. SEQ ID NO:420, SEQ ID NO:421, SEQ ID NO:422, SEQ ID NO:424, SEQ ID NO:425 and SEQ ID NO:426, b. SEQ ID NO:600, SEQ ID NO:601, SEQ ID NO:602, SEQ ID NO:604, SEQ ID NO:605 and SEQ ID NO:606, c. SEQ ID NO:618, SEQ ID NO:619, SEQ ID NO:620, SEQ ID NO:622, SEQ ID NO:623 and SEQ ID NO:624, d. SEQ ID NO:661, SEQ ID NO:662, SEQ ID NO:663, SEQ ID NO:665, SEQ ID NO:666 and SEQ ID NO:667, e. SEQ ID NO:681, SEQ ID NO:682, SEQ ID NO:683, SEQ ID NO:685, SEQ ID NO:686 and SEQ ID NO:687, f. SEQ ID NO:703, SEQ ID NO:704, SEQ ID NO:705, SEQ ID NO:707, SEQ ID NO:708 and SEQ ID NO:709, g. SEQ ID NO:723, SEQ ID NO:724, SEQ ID NO:725, SEQ ID NO:727, SEQ ID NO:728 and SEQ ID NO:729, h. SEQ ID NO:743, SEQ ID NO:744, SEQ ID NO:745, SEQ ID NO:747, SEQ ID NO:748 and SEQ ID NO:749, i. SEQ ID NO:763, SEQ ID NO:764, SEQ ID NO:765, SEQ ID NO:767, SEQ ID NO:768 and SEQ ID NO:769, J. SEQ ID NO:783, SEQ ID NO:784, SEQ ID NO:785, SEQ ID NO:787, SEQ ID NO:788 and SEQ ID NO:789, k. SEQ ID NO:803, SEQ ID NO:804, SEQ ID NO:805, SEQ ID NO:807, SEQ ID NO:808 and SEQ ID NO:809, 1. SEQ ID NO:827, SEQ ID NO: 828, SEQ ID NO: 829, SEQ ID NO: 831, SEQ ID NO:832 and SEQ ID NO:833, m. SEQ ID NO:847, SEQ ID NO: 848, SEQ ID NO: 849, SEQ ID NO: 851, SEQ ID NO:852 and SEQ ID NO:853, n. SEQ ID NO:867, SEQ ID NO: 868, SEQ ID NO: 869, SEQ ID NO: 871, SEQ ID NO:872 and SEQ ID NO:873, 0. SEQ ID NO:887, SEQ ID NO: 888, SEQ ID NO: 889, SEQ ID NO: 891, SEQ ID NO:892 and SEQ ID NO:893, p. SEQ ID NO:907, SEQ ID NO: 908, SEQ ID NO: 909, SEQ ID NO: 911, SEQ ID NO:912 and SEQ ID NO:913, q. SEQ ID NO:927, SEQ ID NO: 928, SEQ ID NO: 929, SEQ ID NO: 931, SEQ ID NO:932 and SEQ ID NO:933, and r. SEQ ID NO:947, SEQ ID NO: 948, SEQ ID NO: 949, SEQ ID NO: 951, SEQ ID NO:952 and SEQ ID NO:

953.

5. A vector or an isolated cell comprising the polynucleotide according to claim 4.

6. A pharmaceutical composition comprising the isolated anti-CCR8 antibody or antigen-binding fragment of any one of claims 1 to 3 and a pharmaceutically acceptable excipient.

7. The isolated anti-CCR8 antibody or antigen-binding fragment thereof of claim 1, wherein the heavy chain variable region (VH) comprises CDRs 1, 2 and 3 with the amino acid sequences set forth in SEQ ID NOs: 618, 619, and 620, respectively, and the light chain variable region (VL) comprises CDRs 1, 2, 3 with the amino acid sequences set forth in SEQ ID NOs: 622, 623, and 624, respectively.

8. The isolated anti-CCR8 antibody or antigen-binding fragment thereof of any one of claims 1 to 3, wherein the heavy chain variable region (VH) comprises an amino acid sequence at least 98% identical to the amino acid sequence set forth in SEQ ID NO: 617 and the light chain variable region (VL) comprises an amino acid sequence at least 98% identical to the amino acid sequence set forth in SEQ ID NO:

621.

9. The isolated anti-CCR8 antibody or antigen-binding fragment thereof of claim 8, wherein the VH comprises an amino acid sequence set forth in SEQ ID NO: 617 and the VL comprises an amino acid sequence set forth in SEQ ID NO:

621.

10. The isolated anti-CCR8 antibody or antigen-binding fragment thereof of any one of claims 1 to 3, wherein the heavy chain comprises an amino acid sequence at least 98% identical to the amino acid sequence set forth in SEQ ID NO: 633 and the light chain comprises an amino acid sequence at least 98% identical to the amino acid sequence set forth in SEQ ID NO:

634.

11. The isolated anti-CCR8 antibody or antigen-binding fragment thereof of claim 10, wherein the heavy chain comprises an amino acid sequence set forth in SEQ ID NO: 633 and the light chain comprises an amino acid sequence set forth in SEQ ID NO:

634.

12. Use of the isolated anti-CCR8 antibody or antigen-binding fragment thereof of any one of claims 1 to 3 for inducing antibody-dependent cellular phagocytosis (ADCP) in a target cell expressing CCR8 in a human patient having a tumor; optionally wherein the isolated anti-CCR8 antibody or antigen-binding fragment thereof comprises six CDR sequences that have the amino acid sequences set forth in SEQ ID NO:618, SEQ ID NO:619, SEQ ID NO:620, SEQ ID NO:622, SEQ ID NO:623 and SEQ ID NO:

624.

13. Use of an isolated anti-CCR8 antibody having ADCC activity and / or ADCP activity for treating a tumor characterized by activated CCR8-expressing Treg cells or CCR8-expressing tumor cells in a patient in need thereof; wherein the isolated anti-CCR8 antibody comprises six CDR sequences wherein each CDR has an amino acid sequence set forth in one of (a) to (r): a. SEQ ID NO:420, SEQ ID NO:421, SEQ ID NO:422, SEQ ID NO:424, SEQ ID NO:425 and SEQ ID NO:426, b. SEQ ID NO:600, SEQ ID NO:601, SEQ ID NO:602, SEQ ID NO:604, SEQ ID NO:605 and SEQ ID NO:606, c. SEQ ID NO:618, SEQ ID NO:619, SEQ ID NO:620, SEQ ID NO:622, SEQ ID NO:623 and SEQ ID NO:624, d. SEQ ID NO:661, SEQ ID NO:662, SEQ ID NO:663, SEQ ID NO:665, SEQ ID NO:666 and SEQ ID NO:667, e. SEQ ID NO:681, SEQ ID NO:682, SEQ ID NO:683, SEQ ID NO:685, SEQ ID NO:686 and SEQ ID NO:687, f. SEQ ID NO:703, SEQ ID NO:704, SEQ ID NO:705, SEQ ID NO:707, SEQ ID NO:708 and SEQ ID NO:709, g. SEQ ID NO:723, SEQ ID NO:724, SEQ ID NO:725, SEQ ID NO:727, SEQ ID NO:728 and SEQ ID NO:729, h. SEQ ID NO:743, SEQ ID NO:744, SEQ ID NO:745, SEQ ID NO:747, SEQ ID NO:748 and SEQ ID NO:749, i. SEQ ID NO:763, SEQ ID NO:764, SEQ ID NO:765, SEQ ID NO:767, SEQ ID NO:768 and SEQ ID NO:769, j. SEQ ID NO:783, SEQ ID NO:784, SEQ ID NO:785, SEQ ID NO:787, SEQ ID NO:788 and SEQ ID NO:789, k. SEQ ID NO:803, SEQ ID NO:804, SEQ ID NO:805, SEQ ID NO:807, SEQ ID NO:808 and SEQ ID NO:809, 1. SEQ ID NO:827, SEQ ID NO: 828, SEQ ID NO: 829, SEQ ID NO: 831, SEQ ID NO:832 and SEQ ID NO:833, m. SEQ ID NO:847, SEQ ID NO: 848, SEQ ID NO: 849, SEQ ID NO: 851, SEQ ID NO:852 and SEQ ID NO:853, n. SEQ ID NO:867, SEQ ID NO: 868, SEQ ID NO: 869, SEQ ID NO: 871, SEQ ID NO:872 and SEQ ID NO:873, 0. SEQ ID NO:887, SEQ ID NO: 888, SEQ ID NO: 889, SEQ ID NO: 891, SEQ ID NO:892 and SEQ ID NO:893, p. SEQ ID NO:907, SEQ ID NO: 908, SEQ ID NO: 909, SEQ ID NO: 911, SEQ ID NO:912 and SEQ ID NO:913, q. SEQ ID NO:927, SEQ ID NO: 928, SEQ ID NO: 929, SEQ ID NO: 931, SEQ ID NO:932 and SEQ ID NO:933, and r. SEQ ID NO:947, SEQ ID NO: 948, SEQ ID NO: 949, SEQ ID NO: 951, SEQ ID NO:952 and SEQ ID NO:953, and further wherein the use occurs by anti-CCR8 antibody induced depletion of the activated CCR8- expressing Treg cells or CCR8-expressing tumor cells.

14. The use according to claim 13, further comprising use of an antibody targeting and / or inhibiting a checkpoint protein in combination with the isolated anti-CCR8 antibody.

15. The use according to claim 14, wherein the checkpoint protein is PD1, PD-L1 or CTLA-4; or wherein the antibody targeting and / or inhibiting a checkpoint protein is nivolumab, pembrolizumab, atezolizumab, avelumab, durvalumab, cemiplimab, dostarlimab or ipilimumab.

16. The use of claim 15, wherein the antibody targeting and / or inhibiting a checkpoint protein is pembrolizumab; optionally wherein the isolated anti-CCR8 antibody is afucosylated.

17. The use according to claim 13, wherein the isolated anti-CCR8 antibody further comprises a variable heavy chain sequence and / or a variable light chain sequence having at least 98% sequence identity with a. a variable heavy chain sequence according to SEQ ID NO:419 and / or a variable light chain sequence according to SEQ ID NO:423, b. a variable heavy chain sequence according to SEQ ID NO:599 and / or a variable light chain sequence according to SEQ ID NO:603, c. a variable heavy chain sequence according to SEQ ID NO:617 and / or a variable light chain sequence according to SEQ ID NO:621, d. a variable heavy chain sequence according to SEQ ID NO:660 and / or a variable light chain sequence according to SEQ ID NO:664, e. a variable heavy chain sequence according to SEQ ID NO:680 and / or a variable light chain sequence according to SEQ ID NO:684, f. a variable heavy chain sequence according to SEQ ID NO:702 and / or a variable light chain sequence according to SEQ ID NO:706, g. a variable heavy chain sequence according to SEQ ID NO:722 and / or a variable light chain sequence according to SEQ ID NO:726, h. a variable heavy chain sequence according to SEQ ID NO:742 and / or a variable light chain sequence according to SEQ ID NO:746, i. a variable heavy chain sequence according to SEQ ID NO:762 and / or a variable light chain sequence according to SEQ ID NO:766, j. a variable heavy chain sequence according to SEQ ID NO:782 and / or a variable light chain sequence according to SEQ ID NO:786, k. a variable heavy chain sequence according to SEQ ID NO:802 and / or a variable light chain sequence according to SEQ ID NO:806, 1. a variable heavy chain sequence according to SEQ ID NO:826 and / or a variable light chain sequence according to SEQ ID NO:830, m. a variable heavy chain sequence according to SEQ ID NO:846 and / or a variable light chain sequence according to SEQ ID NO:850, n. a variable heavy chain sequence according to SEQ ID NO:866 and / or a variable light chain sequence according to SEQ ID NO:870, 0. a variable heavy chain sequence according to SEQ ID NO:886 and / or a variable light chain sequence according to SEQ ID NO:890, p. a variable heavy chain sequence according to SEQ ID NO:906 and / or a variable light chain sequence according to SEQ ID NO:910, q. a variable heavy chain sequence according to SEQ ID NO:926 and / or a variable light chain sequence according to SEQ ID NO:930, or r. a variable heavy chain sequence according to SEQ ID NO:946 and / or a variable light chain sequence according to SEQ ID NO:

950.

18. The use according to claim 13, wherein the isolated anti-CCR8 antibody further comprises a heavy chain sequence and a light chain sequence having at least 95% sequence identity with a. a heavy chain according to SEQ ID NO:435 and a light chain according to SEQ ID NO:436, b. a heavy chain according to SEQ ID NO:615 and a light chain according to SEQ ID NO:616, c. a heavy chain according to SEQ ID NO:633 and a light chain according to SEQ ID NO:634, d. a heavy chain according to SEQ ID NO:676 and a light chain according to SEQ ID NO:677, e. a heavy chain according to SEQ ID NO:696 and a light chain according to SEQ ID NO:697, f. a heavy chain according to SEQ ID NO:718 and a light chain according to SEQ ID NO:719, g. a heavy chain according to SEQ ID NO:738 and a light chain according to SEQ ID NO:739, h. a heavy chain according to SEQ ID NO:758 and a light chain according to SEQ ID NO:759, i. a heavy chain according to SEQ ID NO:778 and a light chain according to SEQ ID NO:779, j. a heavy chain according to SEQ ID NO:798 and a light chain according to SEQ ID NO:799, k. a heavy chain according to SEQ ID NO:818 and a light chain according to SEQ ID NO:819, 1. a heavy chain according to SEQ ID NO:842 and a light chain according to SEQ ID NO:843, m. a heavy chain according to SEQ ID NO:862 and a light chain according to SEQ ID NO:863, n. a heavy chain according to SEQ ID NO:882 and a light chain according to SEQ ID NO:883, 0. a heavy chain according to SEQ ID NO:902 and a light chain according to SEQ ID NO:903, p. a heavy chain according to SEQ ID NO:922 and a light chain according to SEQ ID NO:923, q. a heavy chain according to SEQ ID NO:942 and a light chain according to SEQ ID NO:943, and r. a heavy chain according to SEQ ID NO:962 and a light chain according to SEQ ID NO:

963.

19. The use according to claim 13, wherein the isolated anti-CCR8 antibody has a heavy chain variable region (VH) that comprises CDRs 1, 2 and 3 with the amino acid sequences set forth in SEQ ID NOs: 618, 619, and 620, respectively, and has a light chain variable region (VL) that comprises CDRs 1, 2, 3 with the amino acid sequences set forth in SEQ ID NOs: 622, 623, and 624, respectively; or wherein the isolated anti-CCR8 antibody comprises a heavy chain variable region (VH) comprising an amino acid sequence at least 95% identical to the amino acid sequence set forth in SEQ ID NO: 617 and a light chain variable region (VL) comprising an amino acid sequence at least 95% identical to the amino acid sequence set forth in SEQ ID NO: 621; or wherein the isolated anti-CCR8 antibody comprises a heavy chain comprising an amino acid sequence set forth in SEQ ID NO: 633 and a light chain comprising an amino acid sequence set forth in SEQ ID NO:

634.

20. Use of an isolated anti-CCR8 antibody for treating a cancer exhibiting a tumor characterized by activated CCR8-expressing Treg cells or CCR8-expressing tumor cells in a patient in need thereof; wherein the cancer is selected from the group consisting of breast cancer, head and neck cancer, gastric cancer, lung cancer, squamous cell carcinoma, esophageal cancer, B cell lymphoma, T cell lymphoma, and melanoma; and wherein the isolated anti-CCR8 antibody comprises six CDR sequences wherein each CDR has an amino acid sequence set forth in one of (a) to (r): a. SEQ ID NO:420, SEQ ID NO:421, SEQ ID NO:422, SEQ ID NO:424, SEQ ID NO:425 and SEQ ID NO:426, b. SEQ ID NO:600, SEQ ID NO:601, SEQ ID NO:602, SEQ ID NO:604, SEQ ID NO:605 and SEQ ID NO:606, c. SEQ ID NO:618, SEQ ID NO:619, SEQ ID NO:620, SEQ ID NO:622, SEQ ID NO:623 and SEQ ID NO:624, d. SEQ ID NO:661, SEQ ID NO:662, SEQ ID NO:663, SEQ ID NO:665, SEQ ID NO:666 and SEQ ID NO:667, e. SEQ ID NO:681, SEQ ID NO:682, SEQ ID NO:683, SEQ ID NO:685, SEQ ID NO:686 and SEQ ID NO:687, f. SEQ ID NO:703, SEQ ID NO:704, SEQ ID NO:705, SEQ ID NO:707, SEQ ID NO:708 and SEQ ID NO:709, g. SEQ ID NO:723, SEQ ID NO:724, SEQ ID NO:725, SEQ ID NO:727, SEQ ID NO:728 and SEQ ID NO:729, h. SEQ ID NO:743, SEQ ID NO:744, SEQ ID NO:745, SEQ ID NO:747, SEQ ID NO:748 and SEQ ID NO:749, i. SEQ ID NO:763, SEQ ID NO:764, SEQ ID NO:765, SEQ ID NO:767, SEQ ID NO:768 and SEQ ID NO:769, j. SEQ ID NO:783, SEQ ID NO:784, SEQ ID NO:785, SEQ ID NO:787, SEQ ID NO:788 and SEQ ID NO:789, k. SEQ ID NO:803, SEQ ID NO:804, SEQ ID NO:805, SEQ ID NO:807, SEQ ID NO:808 and SEQ ID NO:809, 1. SEQ ID NO:827, SEQ ID NO: 828, SEQ ID NO: 829, SEQ ID NO: 831, SEQ ID NO:832 and SEQ ID NO:833, m. SEQ ID NO:847, SEQ ID NO: 848, SEQ ID NO: 849, SEQ ID NO: 851, SEQ ID NO:852 and SEQ ID NO:853, n. SEQ ID NO:867, SEQ ID NO: 868, SEQ ID NO: 869, SEQ ID NO: 871, SEQ ID NO:872 and SEQ ID NO:873, 0. SEQ ID NO:887, SEQ ID NO: 888, SEQ ID NO: 889, SEQ ID NO: 891, SEQ ID NO:892 and SEQ ID NO:893, p. SEQ ID NO:907, SEQ ID NO: 908, SEQ ID NO: 909, SEQ ID NO: 911, SEQ ID NO:912 and SEQ ID NO:913, q. SEQ ID NO:927, SEQ ID NO: 928, SEQ ID NO: 929, SEQ ID NO: 931, SEQ ID NO:932 and SEQ ID NO:933, and r. SEQ ID NO:947, SEQ ID NO: 948, SEQ ID NO: 949, SEQ ID NO: 951, SEQ ID NO:952 and SEQ ID NO:953, and further wherein the treatment occurs by anti-CCR8 antibody induced depletion of the activated CCR8- expressing Treg cells or CCR8-expressing tumor cells.

21. The use of claim 20, wherein the cancer is triple-negative breast cancer, non-small cell lung cancer, head and neck squamous cell carcinoma, or melanoma.

22. The use according to claim 20 or 21, wherein the isolated anti-CCR8 antibody is afucosylated.