453 results about "Sequence identity" patented technology

The invention relates to a recombinant I-type humanized collagen with crosslinking property as well as a preparation method and application thereof, and belongs to the technical field of recombinant proteins. The invention relates to recombinant I-type humanized collagen with crosslinking property. The amino acid sequence of the recombinant I-type humanized collagen comprises an amino acid sequence as shown in SEQ ID No.1 or a derivative amino acid sequence with the sequence identity of more than 90% with the sequence as shown in SEQ ID No.1; the recombinant I-type humanized collagen has a triple helix structure. A complete triple helix structure can be efficiently expressed, and the hydrogel has efficient cross-linking capability, so that the hydrogel can be efficiently and stably formed through cross-linking.

The invention belongs to the technical field of biological medicine, and particularly relates to a T cell receptor capable of recognizing KRAS G12V antigen oligopeptide, a compound, a pharmaceutical composition and application. The T cell receptor can be used for recognizing a KRAS G12V-HLA-A * 11: 01 compound with high affinity; the T cell receptor is an alpha-beta heterodimer consisting of an alpha chain and a beta chain; the amino acid sequence of the alpha chain is as shown in SEQ ID NO.10, or an amino acid sequence with at least 90% of sequence identity with the alpha chain; the amino acid sequence of the beta chain is as shown in SEQ ID NO.14, or has an amino acid sequence with at least more than 90% of sequence identity with the beta chain. The T cell receptor provided by the invention can be used for preparing medicines for treating tumors or other immune diseases.

The invention relates to a recombinant elastin and a preparation method thereof as well as a recombinant elastin raw material and application thereof, and belongs to the technical field of recombinant proteins. The amino acid sequence of the recombinant elastin is an amino acid sequence as shown in SEQ ID No.1 or a derivative amino acid sequence of which the sequence identity with the SEQ ID No.1 is more than 90%. The protein is high in expression level, high in purity and relatively high in biological activity, and has the effects of supplementing skin collagen, resisting aging and repairing skin barriers.

The present invention pertains to protein oligomers for active immunization. Specifically, the invention relates to protein oligomers comprising at least a first monomer and a second 5 monomer, said at least first and second monomer comprising, in N- to C-terminal order, at least one first RBD, an immunoglobulin Fc (Ig Fc), and at least one second RBD, wherein a) Ig Fc has enhanced affinity for the neonatal Fc receptor (FcRn) at mucosal pH, compared to wildtype Ig Fc; and b) RBD is a receptor binding domain from or derived from SARS-CoV-2 spike protein, wherein the receptor binding domain comprises the amino acid sequence of SEQ ID NO. 13, or a fragment thereof, or an amino acid sequence having at least 80%, 85%, 90%, or 95% sequence identity to SEQ ID NO. 13. The invention further relates to a vaccine comprising said protein oligomer, preferably for use in active immunization and / or booster vaccination in a subject.

The present disclosure provides adenosine deaminase, fusion proteins, base editor systems and uses, and specifically provides an adenosine deaminase polypeptide having an amino acid sequence having at least about 70%, 75%, at least about 80%, at least about 85%, at least about 90%, at least about 95%, or at least about 99% sequence identity to SEQ ID NO: 13. Also provided are novel nucleic acid modified enzymes having improved efficiency, compositions of base editors comprising the same, and methods and uses for editing target sequences using these adenosine deaminase variants.

The invention relates to the technical field of biology, and particularly discloses polypeptide, recombinant XIX type humanized collagen and application of the recombinant XIX type humanized collagen. The amino acid sequence of the polypeptide comprises n repetitive units; the repetitive unit comprises any one of the following amino acid sequences or variant sequences thereof: (1) an amino acid sequence as shown in any one of SEQ ID NO.1-2; (2) an amino acid sequence having at least 50%, 60%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98% or 99% sequence identity with the amino acid sequence as shown in any one of SEQ ID NO.1-2; (3) a variant sequence obtained by performing mutation of one or more amino acid residues on the amino acid sequence as shown in any one of SEQ ID NO.1-2; wherein n is an integer greater than or equal to 1. The polypeptide provided by the invention has a collagen triple helix structure, has good cell adhesion activity, can carry out functions of human collagen, is free of immunological rejection and anaphylactic reaction, and can be used in various fields of cartilage repair, biological dressing, tissue filling and the like.

Disclosed herein are nucleic acid compositions and methods of use. The nucleic acid compositions may have a therapeutic nucleic acid sequence operably linked to a nuclear targeting sequence that increases expression of the therapeutic nucleic acid in a cell by at least 1.25 fold; at least 80% sequence identity to SEQ ID NO: 6; or a first regulatory element comprising a promoter sequence operably linked to a hemoglobin subunit gamma intron (hBGi) sequence, and a second regulatory element comprising a woodchuck hepatitis posttranscriptional regulatory element (WPRE) sequence. The nucleic acid compositions with these features may enhance therapeutic nucleic acid transfection and expression. Also disclosed herein are transgenes optimized for gene therapy applications, including novel FVIII transgene sequences, in which the B domain may be non-naturally occurring the A1 and / or A3 domain may include at least one amino acid substitution.

A glycosylated p75NTR neurotrophin binding protein (NBP)-Fc fusion protein, comprising: a p75NTR(NBP) portion, having at least 85% sequence identity with Seq ID No. 3; and an immunoglobulin Fc portion. wherein, the p75NTR(NBP) and Fc portions are connected via a linker, the linker comprises a peptide of formula Gx, where x is 1, 2, 3, 4, 5 or 6 wherein the linker does not comprise or consist of the sequence GGGGS.

A process for the manufacture of glycosylated p75NTR neurotrophin binding protein (NBP)-Fc fusion protein, comprising: a p75NTR(NBP) portion, having at least 85% sequence identitywith Seq ID No. 2; and an immunoglobulin Fc portion. wherein, the p75NTR(NBP) and Fc portions are connected via a linker, the linker comprises a peptide of formula Gx, where x is 1, 2, 3, 4, 5 or 6 wherein the linker does not comprise or consist of the sequence GGGGS, characterised by expression from CHO cells, wherein cells are harvested within earlier of 30 hours of cell culture viability reaching 75% or, 12 days post inoculation.

The present invention pertains to pharmaceutical compositions comprising protein oligomers for passive immunization and therapy. Specifically, the present invention relates to a pharmaceutical composition comprising a protein oligomer comprising at least a first and a second monomer, said at least first and second monomer comprising, in N- to C-terminal order, at least one first receptor binding domain (RBD), an immunoglobulin Fc (Ig Fc), and at least one second receptor binding domain (RBD), wherein a) Ig Fc has enhanced affinity for the neonatal Fc receptor (FcRn) at mucosal pH, compared to wildtype Ig Fc; and b) RBD is a receptor binding domain from or derived from SARS-CoV-2 spike protein, wherein the receptor binding domain comprises the amino acid sequence of SEQ ID NO. 13, or an amino acid sequence having at least 80%, 85%, 90%, or 95% sequence identity to SEQ ID NO. 13.

Variants having cutinase activity of a parent cutinase, the variants comprising alterations at one or more (e.g., several) positions corresponding to positions 181, 182, 115, 161, 1, 2, 43, 55, 79, or 5 of SEQ ID NO: 2, where the alterations are substitutions for positions 181, 115, 161, 43, 55, 79, and 5, and deletions for positions 1, 2, and 182, and where the variants have at least 75% but less than 100% sequence identity to a mature polypeptide of SEQ ID NO: 2. Polynucleotides encoding the variants; nucleic acid constructs, vectors, and host cells including the polynucleotides; as well as methods for obtaining the variants and methods for producing the variants. Comprising the variants, and methods for using the variants.

The present invention relates to immunoglobulin single variable domains (ISVDs) for the treatment of diseases by the enteral, e.g. oral, delivery. In particular, the present invention provides ISVDs comprising sequences with a high percentage of sequence identity to SEQ ID NO: 1 for such enteral administration. Such sequences were identified as extraordinarily stable in the gastrointestinal tract, which prevents their degradation and thereby allows them to exert a strong therapeutic effect.

The invention provides an isolated or engineered polynucleotide (10) comprising a coding sequence (12), wherein the coding sequence (12) encodes a protein (20), wherein an amino acid sequence of the protein (20) has at least 85% sequence identity with a reference amino acid sequence in a sequence alignment between the amino acid sequence and the reference amino acid sequence, wherein the reference amino acid sequence is selected from the group consisting of SEQ ID NO:8 11 14 1720, and wherein the protein (20) is a cannabinoid acid synthase (25).

The present invention provides a C-terminal CDNF fragment sequence or a sequence which has at least 80% homology or sequence identity to said sequence. The C-terminal CDNF fragment protects ER stressed neurons, motoneurons and dopaminergic neurons and the fragment is capable of penetrating neuronal cell membrane as well as the blood-brain-barrier. The present invention further provides said fragment and pharmaceutical compositions comprising said fragment for use in treatments of degenerative diseases and disorders including central nervous system diseases, diabetes and retinal disorders. The present invention is also providing a C-terminal MANF fragment sequence or a sequence which has at least 80% homology or sequence identity to the said sequence and pharmaceutical compositions comprising said MANF fragment for use in the treatment of degenerative diseases and disorders including central nervous system diseases, diabetes and retinal disorders.

A transformed microorganism having an ability to produce a polyhydroxyalkanoate copolymer containing 3-hydroxyalkanoate monomer units having 8 or more carbon atoms includes: an exogenous gene encoding a polyhydroxyalkanoate synthase having an amino acid sequence of any one of SEQ ID NOS: 1 to 4; or an exogenous gene encoding a protein that has an amino acid sequence having a sequence identity of at least 90% with the amino acid sequence of any one of SEQ ID NOS: 1 to 4 and that has polyhydroxyalkanoate synthase activity.

A composition including a gene therapy delivery system and an alpha-galactosidase (GLA) polynucleotide encoding a GLA polypeptide, wherein the GLA polypeptide has at least 95% sequence identity to one of SEQ ID NOS. 1-40, 44-45, 51-52, 57, 61-173 or 212. Also provided are compositions, formulations, fusion proteins, and methods for the treatment of Fabry disease.

The present invention relates to a method for obtaining a detergent composition comprising introducing (a) a variant of a parent lipase having at least 60% sequence identity with SEQ ID NO:2, having a substitution at a position D254 of the mature polypeptide corresponding to SEQ ID NO:2, and having lipase activity; and (b) an anionic surfactant, wherein the composition has increased stability compared to a corresponding composition containing the parent lipase.

A variant polypeptide of xylanase, and a fusion protein and an enzyme composition comprising the variant polypeptide, a recombinant host cell for production of the variant polypeptide, methods for using it and its use, is disclosed comprising an amino acid sequence having at least 79%, but less than 100% amino acid sequence identity with amino acids 1-191 of SEQ ID NO: 1, wherein the amino acid sequence has xylanase activity, at least one disulfide bridge between two Cys residues in the 1-191 amino acid region, and an amino acid substitution at the position 23 or 28, or at the positions 23 and 28, the positions corresponding to the positions 23 and 28 of the SEQ ID NO: 1.

The present invention relates to an antibody or binding fragment thereof that binds to a protein, preferably a T cell receptor, comprising an epitope comprising or consisting of an amino acid sequence having at least 80 %, such as 83 %, preferably at least 90 %, for instance 100 % sequence identity to the amino acid sequence set forth in SEQ ID NO: 62 (EVPKXiR), wherein Xi is selected from Alanine (A), Arginine (R), Asparagine (N), Aspartic acid (D), Cysteine (C), Glutamine (Q), Glutamic acid (E), Glycine (G), Histidine (H), Isoleucine (I), Leucine (L), Lysine (K), Methionine (M), Phenylalanine (F), Proline (P), Serine (S), Threonine (T), Tryptophan (W), Tyrosine (Y), Valine (V). Further, the invention relates to pharmaceutical compositions comprising such an antibody or binding fragment thereof and to the use of such an antibody or binding fragment thereof for use as a medicament or for use as a screening agent.

The invention relates to a thermostable FGF10 polypeptide possessing FGF10 activity and having or comprising at least 85% sequence identity to SEQ ID NO:3 that has or comprises an amino acid sequence from Ser69 to Ser208 of SEQ ID NO:1, or to SEQ ID NO:5 that has or comprises an amino acid sequence from Leu40 to Ser208 of SEQ ID NO:1, or the fragments thereof, comprising at least an amino acid substitution L152F. Preferably, any of amino acid substitutions V123I, Q175E, and N181D can be further included. The invention further discloses the use of subjected thermostable FGF10 polypeptides in regenerative medicine or other related medical applications or cosmetics. Further, it discloses a culture medium comprising subjected thermostable FGF10 polypeptides suitable for proliferation and differentiation of the human embryonic stem cells or formation and differentiation of spheroids and organoids.

The present invention is directed to phage therapy for the treatment and control of bacterial infections, in particular urinary tract infections caused by Escherichia coli. More specifically, the present invention is directed to novel bacteriophage strains, cocktails thereof and variants thereof; and to methods using the same in the treatment, reduction or prevention of bacterial infections. The cocktail is used as a first line treatment against urinary tract infections, in particular in cancer patients, diabetic patients, or patients with a weakened immune system. Disclosed herein is a pharmaceutical composition comprising one or more purified strains of bacteriophage, each purified strain having a genome with at least 98% sequence identity to a nucleotide sequence selected from SEQ. ID No. 1, SEQ ID NO. 4, SEQ ID NO. 5 and SEQ ID NO. 6 and / or variants thereof. The pharmaceutical composition may also be used in combination with other therapies for urinary tract infections such as antibiotics. The pharmaceutical composition may also be used in a method of diagnosis of the causative agent of a bacterial infection. A bacteriophage comprising at least 95% sequence identity with SEQ. ID No. 1, SEQ ID NO. 5 or SEQ ID NO. 6 is also disclosed.

The invention relates to the technical field of biological medicine, and relates to a polypeptide in targeted combination with SOX2 protein and application thereof, the polypeptide has an amino acid sequence as shown in SEQ ID NO.1, or has at least 85%, 90%, 95% or more than 99% of sequence identity with the amino acid sequence; the polypeptide inhibits phase separation of SOX2, liquid drops formed by phase separation of SOX2 can be avoided, then the situation that the liquid drops wrap chemotherapeutic drugs, influence the curative effect of the chemotherapeutic drugs and cause tolerance of tumor cells to the chemotherapeutic drugs is avoided, and the polypeptide does not influence the transcription activation function of SOX2 serving as a transcription factor; the polypeptide can inhibit the phase separation of the SOX2, so that the regulation of normal physiological functions, such as high expression in organs such as eyes of a human body, of the SOX2 as a transcription factor is not influenced, and therefore, the polypeptide disclosed by the invention can reverse chemotherapy drug resistance of tumors such as squamous carcinoma by inhibiting the phase separation of the SOX2, can be used for adjuvant therapy of the tumors such as squamous carcinoma, and has no obvious toxic or side effect on each organ of an organism.

The present invention relates to a composition ("TSP-DNA Oligo") comprising: a thermostable peptide ("TSP"), wherein the peptide comprises: an amino acid sequence as set forth in SEQ ID NO: 1 or SEQ ID NO: 2 or SEQ ID NO: 3 or SEQ ID NO: 4, or an amino acid sequence with at least about 92% sequence identity to a sequence as set forth in SEQ ID NO; 1, or SEQ ID NO: 2, or SEQ ID NO: 3 or SEQ ID NO: 4; and a "DNA Oligo" linked to the thermostable peptide through a linker, wherein the linker comprises: an azide group, an alkyne group, an isocyanate group, or a tetrazole group; wherein the "DNA oligo" comprises a promoter sequence for a T7, T3, SP6 RNA polymerase, or a known variant of said promoter sequence, or a sequence complementary to said promoter sequence or said variant.

The purpose of the present invention is to provide a novel mutant gene that imparts perpetual flowering properties to roses. Specifically, the present invention pertains to a KSN mutant gene comprising a base sequence (a) or (b): (a) a base sequence represented by SEQ ID NO: 1; and (b) a base sequence that is at least 90% identical in sequence to the base sequence represented by SEQ ID NO: 1, and maintains a transposon comprising the base sequence from position 729 to position 5812 in the base sequence represented by SEQ ID NO: 1.

In an aspect, provided is a DNA polymerase with an amino acid sequence of at least 80% sequence identity with SEQ ID NO: 1 and having one or more amino acid substitution, wherein the one or more amino acid substitution is selected from the group consisting of A83S, N91I, R96H, R96C, M97V, G108D, G111V, R113H, V118S, S122N, L126I, P127L, A134T, D145V, D145N, D147V, H149R, H149L, Q171L, Q171S, I173V, L178K, I179L, Q180M, F181L, K182D, D186T, G197S, D200K, S215P, K220N, V222I, W232Y, M336L, D341K, D341I, D341L, S349R, S349G, T368Y, D398I, V399R, Q560H, and any combination of two or more of the foregoing. Also provided are a kit including the polymerase, a polynucleotide encoding the polymerase, a method of synthesizing a polynucleotide using the polymerase, and a method of sequence a polynucleotide synthesized by the polynucleotide.

The present invention relates to a modified MARCH gene, the wildtype of which comprises SEQ ID No. 1 and SEQ ID No. 3, or comprises a homologous sequence having at least 70% sequence identity to SEQ ID No. 1 and / or SEQ ID No. 3, which modified gene leads to resistance to downy mildew. The modification may leads to an altered gene expression, such as a reduced gene expression. In particular, the modified MARCH gene comprises a modification in SEQ ID No. 3, or in a homologous sequence having at least 70% sequence identity to SEQ ID No. 3. In one embodiment, the modification is on position 77 of SEQ ID No. 3, or on the corresponding position of a homologous sequence having at least 70% sequence identity. In one embodiment, the modified MARCH gene comprises SEQ ID No. 4. The invention further relates to a polynucleotide comprising a modified MARCH gene and a modified Malectin-like-RLK gene, preferably comprising SEQ ID No. 4 and SEQ ID No. 7. The invention further relates to a plant comprising a modified MARCH gene and to a marker for the identification of a modified MARCH gene.

To provide a new agent for controlling soil-borne plant diseases, containing a microorganism as an active ingredient.SOLUTION: An agent for controlling a soil-borne plant disease, comprising, as an active ingredient, a Pseudomonad bacterium having a 16SrRNA genome comprising a nucleotide sequence having 96% or more sequence identity to a nucleotide sequence represented by SEQ ID NO: 1, a Pseudomonad bacterium having a 16SrRNA genome comprising a nucleotide sequence having 98% or more sequence identity to a nucleotide sequence represented by SEQ ID NO: 2, or a combination thereof.SELECTED DRAWING: None

The present invention relates to polynucleotide comprising a lncRNA gene according to SEQ ID No: 2, or according to a sequence having at least 50% sequence identity to SEQ ID No: 2, and an AP2c gene according to SEQ ID No: 3, or according to a sequence having at least 50% sequence identity to SEQ ID No: 3, which polynucleotide confers an increased density of type IV trichomes. The invention further relates to a plant comprising said polynucleotide and a SlASAT4 gene according to SEQ ID No. 21, or comprising a homologous sequence having at least 99.6% sequence identity to SEQ ID No. 21 wherein the presence of the polynucleotide leads to increased density of type IV trichomes and wherein the presence of said SlASAT4 gene leads to an increased ratio of S4:17 / S3:15 acyl sugars produced in glandular trichomes present on said plant when compared to a control plant lacking the polynucleotide and the SlASAT4 gene. Such a plant also was found to be resistant to Bemisia tabaci. The invention also discloses markers for the identification of the polynucleotide and the SlASAT4 gene and their use for the identification and development of Solanum lycopersicum plants. Also methods for identifying, producing and selecting of plants and seed are disclosed.

The present disclosure provides a polypeptide fragment comprising a polypeptide of a modified hemagglutinin protein, wherein said modified hemagglutinin protein comprises a linker peptide replacing the polypeptide in the cytoplasmic domain of hemagglutinin protein, wherein the hemagglutinin protein is obtained from at least one seasonal strain of influenza virus, wherein said polypeptide of the modified hemagglutinin protein is having at least 80%, or at least 90%, or at least 95%, or at least 97% sequence identity to at least one sequence selected from the group consisting of SEQ ID NO: 2, SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8, SEQ ID NO: 10, SEQ ID NO: 12, SEQ ID NO: 14, SEQ ID NO: 16, SEQ ID NO: 18, SEQ ID NO: 20, SEQ ID NO: 22, SEQ ID NO: 24, SEQ ID NO: 26, SEQ ID NO: 28, and SEQ ID NO: 30.

The present disclosure relates generally to polypeptides capable of hydrolyzing amido linkages in polyamides, and more particularly to polypeptides comprising the amino acid sequence of amino acid residues 2-398 of SEQ ID NO: 2 or an amino acid sequence having at least 70% sequence identity thereto; or a polypeptide comprising the amino acid sequence of amino acid residues 2-394 of SEQ ID NO: 88 or an amino acid sequence having at least 75% sequence identity thereto. The disclosure also extends to methods of using the polypeptides. In another embodiment, the disclosed polypeptides are capable of hydrolyzing nylon 6, 6 oligomers to produce adipic acid and hexamethylenediamine.