749 results about "Sequence identity" patented technology

There is provided a fluorinase variant thereof having at least 70% sequence identity to a sequence MSDLGX6TDDSVAQCKGLMLSICPX24VX26IX28DX30CHX33MTPX37DVVEGARYIVDLPR X52FPEGTVFATTTYPATGTX70X71RSVAX76RX78KX80AALGGARGQX90AGSGX95GX97E RAEGX103YIYIAPNNGLLTX116VIEEHGYX124EAYEVSX131TX133VIPX137X138PEPTFYSR EMVAIPSAHLAAGFPLX163X164VGRX168LX170DX172EIVRFEX179X180KX182X183X184VX186G X188X189LX191GX193X194X195X196X197DHPFGNX204WTNX208HRTDLEKAGIX219YX221TX223X 224KX226VX228DGVLX233FX235LPLX239PTFADAX246X247X248GX250PVX253YX255NSRGYLX2 62X263ARNAAX269LAYPYNLX277AGX280SVX283VTX286A (SEQ ID NO: 1), wherein X is a natural amino acid, and wherein the variant comprises one or more mutations at a site selected from the group consisting of an ion-egress site, a S-Adenosyl-L-Methionine (SAM) binding site, an ion-binding site (IBS), and a conserved site. Also disclosed are polynucleotides encoding the variants, vectors comprising the polynucleotides encoding the variants, and host cells comprising the vectors thereof. Also disclosed are Methods for producing the variants, methods of catalyzing the fluorination of a compound, uses of the fluorinase variants, and methods of treatment using the fluorinase variants thereof.

The invention belongs to the technical field of gene engineering, and discloses an acid protease mutant as well as a coding gene and application thereof. Compared with parent acid protease with an amino acid sequence as shown in SEQ ID NO: 1, the acid protease mutant comprises mutant S60V; the acid protease mutant has at least 98% and less than 100% sequence identity with the parent acid protease. Compared with parent acid protease, the thermal stability of the acid protease mutant provided by the invention is remarkably improved, and the enzyme activity retention rate is greater than 63% after the acid protease mutant is treated at 75 DEG C for 3 minutes and can reach 90.6% to the maximum. The acid protease mutant provided by the invention is beneficial to the application of protease in industrial production.

The present disclosure is directed to an engineered lysin comprising: (a) a Gram-negative base lysin; and (b) one or more antimicrobial peptide (AMP) and / or cell penetrating peptide (CPP), and optionally an outer membrane binding motif and at least one linker, or an active fragment thereof, or a variant thereof having at least 80% sequence identity. Also disclosed herein are methods of treating a bacterial infection caused by at least one Gram-negative bacteria and methods of killing at least one Gram-negative bacteria, comprising administering the engineered lysin disclosed herein.

The invention belongs to the technical field of biological medicines, and particularly relates to an application of a Pucurbita pepo polypeptide Nacrein-LP20 in preparation of a medicine for promoting wound healing and a preparation method of the Pucurbita pepo polypeptide Nacrein-LP20. The amino acid sequence of the Hepu pearl polypeptide Nacrein-LP20 is as shown in SEQ ID NO: 1 (Sequence Identity Number 1). According to the present invention, the Pucurbita pepo active polypeptide Nacrein-LP20 has characteristics of strong DPPH free radical and hydroxyl free radical removing ability and excellent antioxidant activity, can significantly promote HaCaT cell proliferation in the high glucose environment, and can promote migration and repair of HaCaT cells in the high glucose environment; the traditional Chinese medicine composition has a remarkable healing promoting effect on full-cortical resection wound surfaces of normal rats and diabetic rats.

The invention provides formaldehyde lyase as well as a mutant and application thereof. The amino acid sequence of the formaldehyde lyase mutant is shown as SEQ ID NO.1, SEQ ID NO.4 or SEQ ID NO.6 and contains at least one of the following sites: S26, W86, N87 or Y87, L109 or M109, L110, H281, Q282 or E282 and A460, and the amino acid sequence is subjected to amino acid mutation and has a formaldehyde lyase activity function. The amino acid sequences of the formaldehyde lyase and the mutants of the formaldehyde lyase have at least 99% of sequence identity with SEQ ID NO.1-7. The formaldehyde lyase and the mutant thereof can catalyze formaldehyde to synthesize 1, 3-dihydroxyacetone, and a new way for converting formaldehyde into 1, 3-dihydroxyacetone is provided.

Disclosed herein is a mutant, non-naturally occurring or transgenic plant or plant part having reduced or inhibited expression or activity of NtNTP2-T, or reduced or inhibited expression or activity of NtNTP2-T and NtNTP2-S, the NtNTP2-T and NtNTP2-S comprising or consisting of: (i) a polynucleotide sequence of NtNTP2-S comprising at least one of a nucleotide sequence of NtNTP2-S and a nucleotide sequence of NtNTP2-S comprising at least one of a nucleotide sequence of NtNTP2-S, a nucleotide sequence of NtNTP2-S, a nucleotide sequence of NtNTP2-S, and a nucleotide sequence of NtNTP2-S comprising at least one of a nucleotide sequence of NtNTP2-S, and a nucleotide sequence of NtNTP2-S; a nucleotide sequence comprising, consisting or consisting essentially of a sequence having at least 70% sequence identity to SEQ ID NO: 3; or (ii) an NtNTP2-T polynucleotide sequence comprising, consisting or consisting essentially of a sequence having at least 70% sequence identity to SEQ ID NO: 11; or (iii) a polypeptide encoded by the polynucleotide shown in (i) or (ii); or (iv) an NtNTP2-S polypeptide having at least 77% sequence identity to SEQ ID NO: 7; or (v) an NtNTP2-T polypeptide having at least 77% sequence identity to SEQ ID NO: 12; wherein the expression or activity of NtNTP2-T or the expression or activity of NtNTP2-T and NtNTP2-S is reduced or inhibited as compared to a control plant.

A deaminase, a fusion protein and the use thereof. The deaminase contains an amino acid sequence having at least 50% sequence identity to any one of SEQ ID NOs: 1-6, 39-164 and 297-312, and the deaminase can deaminize at least one nucleotide in a target polynucleotide. The deaminase can be fused with a nucleic acid-binding polypeptide to obtain various base editors for the sequence-specific base conversion of the target polynucleotide. The performance of the editors can be further improved by means of fusing one or two UGIs, fusing a Gam protein and other strategies.

The invention relates to the technical field of gene isolation and plant improvement, in particular to a late blight resistance gene, a biological material and application. The Rpi-card1 nucleic acid molecule provided by the invention comprises a nucleotide sequence as shown in any one of SEQ ID NO: 1-4; a nucleotide sequence encoding the amino acid sequence represented by SEQ ID NO: 5 or 6; the nucleotide sequence has at least 75% sequence identity with the nucleotide sequence. The invention provides an important gene resource for potato late blight resistance breeding, overcomes the problem of disease resistance loss of potato varieties, and provides a new guarantee for lasting disease resistance of potatoes.

The present invention provides an anti-CCR9 antibody or antigen binding fragment thereof comprising a variable light chain comprising SEQ ID NO:1 or a variant thereof having at least 95% sequence identity to SEQ ID NO:1, wherein the variable light chain comprises a CDR-L1 comprising the amino acid sequence RSSQSLXHSNGXTFLH (SEQ ID NO: 2), a CDR-L2 comprising the amino acid sequence KVSNRFS (SEQ ID NO: 3) and a CDR-L3 comprising the amino acid sequence SQTTHXPWT (SEQ ID NO: 4), wherein X can be any amino acid. Also provided is the anti-CCR9 antibody or antigen binding fragment thereof for use in the treatment or prevention of a disease, as well as methods of diagnosis and antibody drug conjugates.

The invention relates to the field of biological medicine, and provides a monoclonal antibody for recognizing Profilin-1 and application of the monoclonal antibody. The antibody provided by the invention is selected from at least one of the following: (1) light chain CDR sequences as shown in SEQ ID NO: 5, 6 and 7, and heavy chain CDR sequences as shown in SEQ ID NO: 8, 9 and 10; (2) light chain CDR sequences as shown in SEQ ID NO: 11, 12 and 13, and heavy chain CDR sequences as shown in SEQ ID NO: 14, 15 and 16; or an amino acid sequence having at least 80% sequence identity compared with (1) or (2). In addition, the invention also discloses an enzyme immunoassay kit prepared by using the antibody, and the enzyme immunoassay kit has relatively high sensitivity and specificity.

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 invention discloses a monoclonal antibody against abrus precatorius toxin and application thereof, belongs to the field of biological medicine, and provides a monoclonal antibody against abrus precatorius toxin, which has at least 95%, at least 96%, at least 97%, at least 98% and at least 99% sequence identity with amino acid sequences shown as SEQ ID NO: 1, SEQ ID NO: 2 and SEQ ID NO: 3, of heavy chain variable region complementarity determining regions CDR1, CDR2 and CDR3. The light chain variable region complementarity determining regions CDR1, CDR2 and CDR3 have at least 95%, at least 96%, at least 97%, at least 98% and at least 99% of amino acid sequences shown as SEQ ID NO: 9, 10 and 11. The invention further provides application of the antibody to preparation of an antibody for detecting and treating abrus precatorius toxin poisoning and having a long-time treatment effect and related products.

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.

A Cas12 protein and a use thereof. The amino acid sequence of the Cas12 protein comprises or is a sequence having at least 50% sequence identity to SEQ ID NO: 1, and the amino acid sequence of the Cas12 protein comprises or is a sequence different from SEQ ID NO: 1 in amino acids at one, two or more positions. The amino acid sequence of the Cas12 protein comprises or is an amino acid sequence having at least 50% identity to SEQ ID NO: 18, and a PAM sequence identified by the Cas12 protein is A. By carrying out rational and non-rational mutation on the amino acid sequence of a natural Cas12 protein, the gene editing efficiency of the natural Cas12 protein in mammalian cells is improved. The Cas12 protein achieves higher editing efficiency and / or a lower off-target rate, and the PAM sequence is a single A base, so that many target sequences which are previously difficult to edit can be edited, thereby greatly expanding the editing range.

Provided herein are versikine nucleic acid molecules comprising at least 90% sequence identity to SEQ ID NO: 1. Also provided herein are pharmaceutical compositions comprising any one of the versikine nucleic acid molecules described herein, and a lipid nanoparticle, wherein the versikine nucleic acid molecule is encapsulated in the lipid nanoparticle. Any of the versikine compositions described herein can be used for the treatment of cancer.

The present invention inter alia relates to a T-cell expressing a chimeric CD 95 receptor comprising a polypeptide, wherein said polypeptide comprises at least one CD 95-derived polypeptide region having at least 60% sequence identity with a polypeptide domain, a polypeptide region or a polypeptide motif of a human CD 95 wildtype receptor, wherein said human CD 95 polypeptide region comprises a CD 95 extracellular ligand binding domain; further wherein said polypeptide comprises at least one non-CD 95-derived co- stimulatory cytoplasmic polypeptide domain, region or motif of a tumor necrosis factor receptor superfamily protein comprising CD40, CD40L, CD27, HVEM, GITR, CD30, OX40, and / or LTBR, an immunoglobulin superfamily (IgSF) protein, a Toll-like-receptor, and / or an IL6-receptor family protein; wherein the T-cell further expresses an engineered T-cell receptor. The present invention also relates to a vector comprising nucleic acids encoding for the CD 95 receptor and the engineered T-cell receptor, as well as to a kit for preparing the T-cells of the present invention, and a pharmaceutical composition comprising the T-cells. The invention also relates to a method for preparing a T-cell for immunotherapy, and to a method for treating a patient having a disease comprising administering the pharmaceutical composition.

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 discloses a preparation method of rebaudioside D and rebaudioside M and an application of beta-1, 2-glucosyltransferase in the rebaudioside D and rebaudioside M. The beta-1, 2-glucosyltransferase has an amino acid sequence as shown in SEQ ID NO: 4, or has a mutant amino acid sequence which has at least 99% sequence identity compared with the amino acid sequence as shown in SEQ ID NO: 4. According to the invention, the yield of an intermediate product rebaudioside D when the beta-1, 2-glucosyltransferase catalyzes rebaudioside A to generate rebaudioside M is improved, and the yield of a final product rebaudioside M is correspondingly improved.

The invention discloses a specific monoclonal antibody for resisting a Nipah virus Post-F protein, the monoclonal antibody comprises a heavy chain variable region and a light chain variable region, the heavy chain variable region comprises HCDR1, HCDR2 and HCDR3, and the light chain variable region comprises LCDR1, LCDR2 and LCDR3; wherein the HCDR1, the HCDR2 and the HCDR3 respectively comprise the HCDR1, the HCDR2 and the HCDR3 in a heavy chain variable region of which the amino acid sequence is any one of SEQ ID NO: 4, 13, 20, 25, 30, 34 or 42, or respectively have at least 85% sequence identity with the HCDR1, the HCDR2 and the HCDR3; and / or the LCDR1, the LCDR2 and the LCDR3 respectively comprise LCDR1, LCDR2 and LCDR3 in a light chain variable region with the amino acid sequence of any one of SEQ ID NO: 9, 16, 23, 28, 32, 37 or 46, or respectively have at least 85% sequence identity with the LCDR1, the LCDR2 and the LCDR3. The anti-Nipah virus Post-F protein monoclonal antibody disclosed by the invention can be specifically combined with a Post-F conformation protein, and has the application potential of being developed into a Nipah virus antibody detection kit or a virus neutralizing antibody drug.

Disclosed are use of a polynucleotide, protein, and biological material in the regulation and control of plant tuber development, and related products and production methods thereof. The tuber plant or part thereof, comprising a sequence encoding a polypeptide comprising a sequence having at least 92% sequence identity to SEQ ID NO: 2, wherein the polypeptide is inhibited-expressed, loss-function, or overexpressed, and the development of plant tuber is changed. The polynucleotide is an identity gene of a tuber, and can control whether a tuber is formed, the formation time, the tuber size etc. by regulating and controlling a protein function, an expression quantity etc.

Provided are polynucleotides comprising a transcriptional control element comprising a promoter sequence having at least 80% sequence identity to SEQ ID NO: 1. SEQ ID NO:2. SEQ ID NO:3 or SEQ ID NO:4 and a cell- or tissue-specific enhancer element. Also provided are compositions (e.g., vectors, viruses, host cells, and pharmaceutical compositions) comprising said polynucleotides, methods that are useful for expressing a target gene in a host cell, and methods that are useful for expressing a target gene in a subject in need thereof.

The invention belongs to the technical field of biology, and relates to a method for large-scale preparation of high-purity hydrolyzed corac acid or a salt thereof. The method comprises the following steps: 1) adding a solution containing corac acid or a salt thereof into a corac acid degrading enzyme containing an amino acid sequence as shown in SEQ ID NO: 1 or having at least 90% sequence identity with the SEQ ID NO: 1; terminating in the step 2) is achieved through a terminating agent, a boiling water bath and / or an ice bath, the terminating agent is selected from one or more of activated carbon, absolute ethyl alcohol, methyl alcohol, EDTA, trichloroacetic acid and sodium carbonate, and preferably, the activated carbon is used for achieving terminating in the step 2); and further obtaining the hydrolyzed corac acid or the salt thereof. The molecular structure of the hydrolyzed sodium currate prepared by the method provided by the invention has acetylation and pyruvic acid modification, the preparation condition is mild, the production cost is low, continuous production can be realized, and industrial amplification is easy.

There is provided an interleukin-21 (IL-21) variant, wherein in comparison to wild-type IL-21 that comprises an amino acid sequence according to SEQ ID NO: 6 or an amino acid sequence comprising at least 70% sequence identity to SEQ ID NO: 6, the IL-21 variant comprises an amino acid modification at one or more of the following amino acid positions: 29, 33, 36 and / or 71.

There is disclosed a mutant, non-naturally occurring or transgenic tobacco plant or part thereof having modulated expression or activity of lysine ketoglutarate reductase (LKR) comprising, consisting of, or consisting essentially of: (i) a polynucleotide, the present invention relates to a protein comprising, consisting or consisting essentially of a sequence having at least 88% sequence identity to SEQ ID NO: 1 (NtLKR-S) and / or a sequence having at least 86% sequence identity to SEQ ID NO: 3 (NtLKR-T); (ii) a polypeptide encoded by the polynucleotide set forth in (i); (iii) a polypeptide comprising, consisting or consisting essentially of a sequence having at least 89% sequence identity to SEQ ID NO: 2 (NtLKR-S) and / or a sequence having at least 88% sequence identity to SEQ ID NO: 4 (NtLKR-T); or (iv) a construct, vector or expression vector comprising the isolated polynucleotide set forth in (i) wherein the plant or part thereof comprises at least one modification as compared to a control plant or part thereof wherein the expression of the polynucleotide or the activity of the polypeptide is not modified, the at least one modification is capable of modulating: (a) expression of the polynucleotide in the plant or part thereof; or (b) the activity of the polypeptide in the plant or part thereof.

Described are lipopeptides that inhibit coronavirus fusion to a host cell. Thus a therapeutic for treating or preventing the common cold is described along with methods of inhibiting and / or treating an alphacoronavirus infection. The lipopeptides comprise a peptide unit comprising an amino acid sequence having a high degree of sequence identity to a sequence from the C-terminal heptad repeat of a betacoronavirus S protein, such as that of SARS-CoV-2.

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 invention relates to a process for producing three recombinases capable of hydrolyzing organophosphorus, carbamate and pyrethroid insecticides, and preparations containing these enzymes. The present invention provides recombinant plasmid DNA vectors in which the protein secretion system has been modified to improve the ability of recombinant proteins to secrete into the space around the plasmid or culture medium. A nucleotide sequence for coding a PelB (butyric acid lyase B) signal sequence is deleted and substituted by a nucleotide sequence for coding a LamB (maltodextrin or phage lambda receptor) signal sequence, so that the secretion efficiency of the recombinant protein is higher. The invention discloses three recombinant plasmid DNA (deoxyribonucleic acid) vectors which are constructed by utilizing the improved plasmid DNA vectors and are used for expressing recombinant proteins. The recombinant protein comprises (a) a recombinant organophosphate hydrolase having at least 80% sequence identity with the amino acid sequence of methyl parathion hydrolase (MPH) (Protein Database (PDB) ID: 1P9E) as shown in SEQ ID NO: 1, wherein the recombinant organophosphate hydrolase has hydrolytic activity on organophosphate insecticides; (b) a recombinant carbamate hydrolase having at least 80% sequence identity with the amino acid sequence of L-aminopeptidase-D-Ala-esterase / amidase (aryl amidase) (MAH) (PDB ID: 1B65), as shown in SEQ ID NO: 2, wherein the recombinant carbamate hydrolase has hydrolytic activity on carbamate insecticides; and (c) a recombinant pyrethroid hydrolase having at least 80% sequence identity with the amino acid sequence of the pyrethroid hydrolytic carboxylesterase (EstA) (PDB ID: 4CCY) as shown in SEQ ID NO: 3, wherein the recombinant pyrethroid hydrolase has hydrolytic activity on a pyrethroid insecticide. The embodiment of the invention further provides three recombinant bacterial strains, an escherichia coli strain BL21 (DE3) is used as a host cell, and each recombinant plasmid DNA vector is used for transformation. The invention also discloses culture conditions of the recombinant strain, wherein the culture conditions comprise culture medium composition, induction conditions and enzyme harvesting and enzyme activity detection methods. In addition, the embodiment of the invention also provides a preparation which contains the three recombinases as functional components.

Provided is a heat-resistant D-allulose-3-epimerase. A polypeptide shown in any one of the following (1) to (3):(1) a polypeptide consisting of an amino acid sequence having one or two or more amino acid substitutions selected from the group consisting of A56E, N57H, R58G and F111W in SEQ ID NO:1;(2) a polypeptide consisting of the amino acid sequence having substitution, addition, insertion or deletion of one or several amino acid residues in the amino acid sequence described in (1) above, having D-allulose-3-epimerase activity and retaining one or two or more amino acid substitutions selected from the group consisting of A56E, N57H, R58G, and F111W; and(3) a polypeptide having a 90% or more sequence identity to the amino acid sequence described in (1) above, having D-allulose-3-epimerase activity and retaining one or two or more amino acid substitutions selected from the group consisting of A56E, N57H, R58G, and F111W.

A composition comprising, for example, chemically modified RNA (cmRNA) encoding CST6 or a polypeptide with at least 80% amino acid sequence identity thereto, and methods of making and using the cmRNA, are provided.

An isolated polynucleotide encoding a modified luciferase polypeptide and substrates. The OgLuc variant polypeptide has at least 60% amino acid sequence identity to SEQ ID NO: 1 and at least one amino acid substitution at a position corresponding to an amino acid in SEQ ID NO: 1. The OgLuc variant polypeptide has at least one of enhanced luminescence, enhanced signal stability, and enhanced protein stability relative to the corresponding polypeptide of the wild-type Oplophorus luciferase.