33 results about "High affinity receptor" patented technology

A compound of general formula (1) wherein R1, R2, R3, R4, R5, R6, R7, R8, R9, R10, R11 and R12 are H or methyl, R13, R14, R15 and R16 are H or alkyl, wherein L1 and L2 are linkers selected from single bond, methyl, ethyl, wherein R19, R20 and R21 are H or —CH₂X, NT is selected from H, hydroxyl, alkyl, aminoacid, aminoacid analogue, polypeptide and functional group, CT is selected from hydrogen, hydroxyl, alkyl, aminoacid, aminoacid analogue, polypeptide and functional group shows high selectivity and high affinity for MC1-receptors in combination with effective stimulation or inhibiton of cAMP formation in MC1-receptor expressing cells but low affinity for other subtypes of MC-receptors and may be used to treat a wide range of inflammatory conditions. Also disclosed is a DNA molecule and a corresponding vector encoding the compound, a fusion protein comprising a copy of it, a vector comprising DNA encoding the fusion protein, and a pharmaceutical composition comprising the compound.

The present invention relates to compounds of formula I

wherein R¹ and R² are described hereinbelow. These compounds have high affinity to A_2A receptors and good selectivity to A₁ and A₃ receptors. These compounds are useful, inter alia, in the treatment of Alzheimer's disease, depression, Parkinson's disease and ADHD.

The present invention relates to methods for the control of virulence of infectious bacteria by modulating the extra-cellular concentration of bacterial cell signalling molecules. Derivatives of cell signalling molecules are conjugated to suitable carrier proteins and used to isolate high affinity receptors recognising the native signal molecule(s). By binding to signalling molecules, the receptors reduce and maintain extra-cellular concentrations of signal molecules below the threshold level that would otherwise result in certain opportunistic pathogens adopting a virulent form, and can transform virulent organisms to non-virulent states. These receptors have applications for the treatment of individuals with susceptibility to infection, the treatment of patients with existing infections, in disease monitoring and management, and in related applications where the host for infection is an animal or plant.

The invention belongs to the fields of molecular biology and immunology, and relates to chimeric chemokines receptors capable of making T cells tend to tumor locations. Specifically, the chimeric chemokines receptors are formed in a manner that a peptide fragment of a generated factor secreted by efficiently-combined tumor cells or tumor stromal cells is connected with a transmembrane region originated from a high-affinity receptor and a signal domain peptide fragment capable of making the T cells efficiently migrated through hinge structures. A membrane outer peptide fragment receives a corresponding factor signal and transfers the signal into cells, and a related path for promoting T cell chemotaxis is started through an intracellular region of the signal domain peptide fragment capable of promoting the migration of the T cells, so that the T cells modified by the chimeric chemokines receptors have a characteristic of migrating to the corresponding factor high concentration direction, and a normal tumor killing activity is not weaken, so as to ensure the tumor adoptive cell therapy effector T cells can efficiently reach the tumor nidus locations, and play a role in treatment.

The present invention is directed to an Assay for high capacity screening of substances interfering with the attachment of human IgE to its high affinity receptor and/or of substances capable of detaching already bound IgE from this receptor and for the differential analysis between autoimmune disorders and classical allergies.

The invention provides an interleukin 2 mutant, a fusion protein, an antibody or a conjugate containing the mutant, and a pharmaceutical composition containing the mutant, the fusion protein, the antibody or the conjugate. Compared with wild-type interleukin 2, the mutant eliminates binding with IL-2R[alpha], reduces binding with an IL-2R[beta][gamma] dimer, but keeps stimulating proliferation of tumor immune cells, including but not limited to proliferation of T cells and NK cells. According to the IL-2 mutant, the affinity to a high-affinity IL-2 receptor is eliminated, and meanwhile, the affinity to a medium-affinity IL-2 receptor is reduced. The interleukin 2 mutant provided by the invention is more suitable for the conjugate of the fusion protein and the antibody. The interleukin 2 mutant provided by the invention has extremely few mutation sites relative to wild type interleukin 2, so that the potential immunogenicity is extremely low. Meanwhile, various side effects caused by immunotherapy by using natural IL-2 are avoided.

The invention discloses an anti-human FcepsilonRIalpha subunit monoclonal antibody and application thereof. A hybridoma cell strain producing the monoclonal antibody is collected in China Center for Type Culture Collection, and the collection number thereof is CCTCC NO:201211. The anti-human FcepsilonRIalpha subunit monoclonal antibody prepared by the invention can be combined with a human IgE high-affinity receptor FcepsilonRIalpha, and can be used for detecting FcepsilonRIalpha expression on the surface of a cell; and the monoclonal antibody is of great significance for prevention and treatment of mast cell and basophilic granulocyte related diseases such as allergic dermatitis, dermatomyositis, psoriasis and the like, and has great clinical application value. The hybridoma cell strain provided by the invention is favorable in cell strain growth vigor, uniform in cell body size, muddy or transparent and vigorous in division, and has a proliferative potential of infinite division.

The present disclosure relates to hIL2 orthogonal ligands (“IL2 orthologs”) that specifically and selectively bind to the extracellular domain (ECD) a transmembrane polypeptide comprising of a modified hCD122 polypeptide. The binding of the hIL2 ortholog to the modified hCD122 polypeptide participates in the transduction pathway of intracellular signaling resulting in a biological activity of the native intracellular signaling patterns associated with hIL2 binding to either the intermediate or high affinity hIL2 receptor but which exhibits selectivity to an engineered cell expressing an hCD122 orthogonal receptor. The hIL2 orthologs of the present invention exhibit significantly reduced binding relative to their binding to the extracellular domain of wild type hCD122, either alone or when hCD122 is present in the form of an endogenous high or intermediate affinity hIL2 receptors.

The invention relates to a human interleukin-2 variant or a derivative thereof, in particular to IL-2 with one or more mutant amino acids or a derivative of the IL-2 with one or more mutant amino acids. The human interleukin-2 variant or the derivative thereof has eliminated or reduced affinity with a high-affinity receptor (IL-2Ralpha/beta/gamma), and the affinity with a medium-affinity receptor(IL-2Rbeta/gamma) is kept. According to the human interleukin-2 variant or the derivative thereof, a good basis is provided for protein patent medicines.

In accordance with the present invention, a composition and method is provided that allows for the administration of a biologically-active factors to a human or animal. The present invention can be used to treat a disease with a biologically-active factor or combination of biologically-active factors, or can be used to safely vaccinate a human or animal against a biologically-active factor. It can also be used as a method for the delivery of biologically-active factors for the treatment of disease. Additionally, the present invention also includes a method of targeted drug delivery for the treatment of disease through the administration of custom complexes containing of one or more biologically active factors bound to a colloidal metal where at least one of the biologically-active factors is capable of binding a high affinity receptor on a cell surface.

The present invention provides a polynucleotide comprising all or a part of the nucleotide sequence identified as SEQ ID NO:1 that regulates transcription of the human high-affinity IgE receptor (FcεRl) β-chain gene, and a method for regulating transcription of the FcεRl β-chain gene which comprises the step of promoting binding between a transcription regulatory complex containing MZF-1 and the transcription regulatory region of the FcεRl β-chain gene that contains the nucleotide sequence identified as SEQ ID NO: 1. In addition, the present invention provides a screening method and a kit therefor that utilizes the method for regulating transcription of the FcεRl β-chain gene having the step of promoting binding between a transcription regulatory complex containing MZF-1 and the transcription regulatory region of the FcεRl β-chain gene that contains the nucleotide sequence identified as SEQ ID NO:1, thereby enabling development of a novel agent for the prevention and treatment of allergic diseases.

The present invention provides a chimeric protein comprising: a) a single chain variable fragment (scFv) that binds to a mammalian IgE at an epitope within the amino acid sequence VDGQKATNIFPYTAPGTK (SEQ ID NO:1) of canine IgE or at an epitope within the corresponding amino acid sequence of a different mammalian species; b) a linker peptide; and c) an amino acid sequence comprising an IgE high affinity receptor alpha chain, and methods of use thereof.

Novel genetic variants of the Fc Fragment Of Ige, High Affinity I, Receptor For; Alpha Polypeptide (FCER1A) gene are described. Various genotypes, haplotypes, and haplotype pairs that exist in the general United States population are disclosed for the FCER1A gene. Compositions and methods for haplotyping and/or genotyping the FCER1A gene in an individual are also disclosed. Polynucleotides defined by the haplotypes disclosed herein are also described.

The invention discloses an anti-human Fc epsilon RI alpha subunit monoclonal antibody and application thereof. A hybridoma cell strain capable of producing the monoclonal antibody is preserved in China Center for Type Culture Collection and has the preservation number of CCTCC NO. C201326. The anti-human Fc epsilon RI alpha monoclonal antibody prepared by the invention can be bound with high-affinity receptor Fc epsilon RI alpha of human IgE and can be applied in detecting the expression of cell surface Fc epsilon RI alpha. The monoclonal antibody has important significance and relatively large clinical value for prevention and treatment of mast cell and basophilic granulocyte-related diseases, such as allergic dermatitis, dermatomyositis and psoriasis. The hybridoma cell strain disclosed by the invention grows well, and is bright and transparent, the cell body is uniform, the division is strong and the hybridoma cell strain has indefinitely divided proliferative capability.

Antibodies and antibody fragments which are anti-idiotypic to an antibody that interferes with the binding of the C epsilon 3 region of IgE to its high affinity receptor (mimobodies), particularly, which are anti-idiotypic to BSW17 (BSW17-mimobodies) are described, as well as their use as pharmaceuticals, especially vaccines, in the treatment of IgE-mediated diseases.

The invention relates to the technical field of biology, and particularly discloses a preparation method and application of a dermatophagoides pteronyssinus allergen specific IgG Fab antibody fragment. The method comprises the following steps: 1) collecting and diluting serum, and filtering to obtain a serum sample; loading the sample on a protein A affinity chromatography column, and then eluting a serum IgG antibody to obtain a serum total IgG antibody; 2) adding dermatophagoides pteronyssinus to a affinity chromatographic column for coupling, adding the serum total IgG antibody in the step 1), and eluting the dermatophagoides pteronyssinus specific IgG antibody; and 3) adding agarose-linked papain into the house dust mite specific IgG antibody, uniformly mixing, incubating, centrifuging, and taking supernatant, thereby obtaining the house dust mite specific immunoglobulin G. The dermatophagoides pteronyssinus allergen specific IgG Fab antibody fragment can compete with IgE to bind to dermatophagoides pteronyssinus and reduce the formation of a dermatophagoides pteronyssinus-IgE compound, so that the binding of the dermatophagoides pteronyssinus-IgE compound to effector cells expressing IgE low-affinity receptors and IgE high-affinity receptors is reduced, the activation of sensitized cells is reduced, and the occurrence of inflammatory response is controlled.

Non-human transgenic animal models and cells derived therefrom are provided for RabGEF1 function. RabGEF1 is a negative regulator of FcεRI-dependent mast cell activation and T cell activation via the T cell receptor and a lack of RabGEF1 results in the development of skin inflammation in vivo. The mast cells derived from such animals exhibit enhanced Ras-mediated signaling and functional responses when activated through high affinity IgE receptors. These cells show significant potentiation of IgE and antigen-dependent secretion of 3 classes of mast cell mediators, providing a useful source of mast cells for screening assays. The animals and cells derived therefrom are also useful for screening biologically active agents that may modulate RabGEF1 function, including therapeutic agents for the treatment of skin disorders, such as eczema, psoriasis, and the like, or for the treatment of other mast cell-associated disorders, including allergic disorders, such as asthma and hay fever, and certain autoimmune disorders, such as rheumatoid arthritis and multiple sclerosis. Inhibiting RabGEF1 function may be useful in those conditions in which it is desirable to enhance T cell and/or mast cell function, such as in AIDS or other immune deficiency disorders.