13 results about "N-terminus" patented technology

The application provides an anti-digoxin antibody or antigen binding fragment thereof and application thereof, and relates to the technical field of antibodies. The anti-digoxin antibody or antigen binding fragment thereof comprises a heavy chain variable region and a light chain variable region; the heavy chain variable region comprises VHCDR1 of the 17th-24th amino acid residues at the N terminus of the amino acid sequence shown in SEQ ID NO. 1, VHCDR2 of the 42nd-49th amino acid residues, and VHCDR3 of the 88th-98th amino acid residues; and the light chain variable region comprises VLCDR1 of the 27th-37th amino acid residues at the N terminus of the amino acid sequence shown in SEQ ID NO. 2, VLCDR2 of the 55th-57th amino acid residues, and VLCDR3 of the 94th-102th amino acid residues. The antibody or antigen binding fragment thereof can be used for immunological detection, and has been verified to have good specific binding capacity.

The application provides an mRNA vaccine and a preparation method and application thereof. Specifically, the application provides application of GMCSF as an immune adjuvant in preparation of an mRNA vaccine, and further provides an mRNA molecule, which encodes a GMCSF-antigen-FC1 fusion protein, wherein the GMCSF-antigen-FC1 fusion protein comprises, from an N terminus to a C terminus, an amino acid sequence of GMCSF, an amino acid sequence of an antigen and an amino acid sequence of FC1 in sequence, wherein the antigen is an antigen from a virus. The mRNA molecule of the application can be used for preparing a vaccine for preventing infection of novel coronavirus BA2 and BA5 mutant strains, and can induce a strong immune response.

Provided is a novel production method with which a heteromultimeric protein such as a bispecific antibody can be produced. The production method of the present disclosure is a method for producing a heteromultimeric protein, and includes a complex formation step and a generation step. The complex formation step is a step of forming a first complex of two proteins by bringing the two proteins into contact with each other. In the complex formation step, the two proteins includes a first protein and a second protein. The first protein includes a first binding tag, a first cleavable domain, and a first domain in this order from the N terminus to the C terminus. The second protein includes a first binding partner capable of binding to the first binding tag, a second cleavable domain, and a second domain in this order from the N terminus to the C terminus.

A method of preventing or treating or controlling a respiratory disease in a bovine by delivering to a lung or trachea of the bovine a composition including a polyplex having one or more mRNA encoded with a molecule selected from lycosylphosphatidylinositol (GPI) complex, antibody immunoglobulin G (IgG), antibody immunoglobulin A (IgA), antibody immunoglobulin M (IgM), antimicrobial peptide Bactenecin 5 (Bac5), antimicrobial peptide Bactenecin 7 (Bac7), bovine myeloid antimicrobial peptide (BMAP-28), lipoxin inducing enzymes, resolvin inducing enzymes, cytokines, CRISPR associated protein 13 (Cas13) enzymes, nanoluciferase (NLuc) proteins, and gene activator, catalytically dead CRISPR-associated protein 9 fused to an activator selected from the group consisting of VP64-p65-Rta transactivation domain (dCas9-VPR), VP64, and VP64-p65-HSF1 on the N terminus and SS18 on the C-terminus, and a polymer prepared by polymerizing a diacrylate monomer; one or more linker monomers; and one or more branching monomers; and end-capping the polymer.

Provided are a recombinant collagen having a skin penetration effect, a preparation method therefor, and the use thereof, belonging to the technical fields of protein engineering and genetic engineering. A novel recombinant collagen is designed and obtained by means of methods such as screening, replacement, splicing, etc.; the nucleotide sequence thereof is optimized for codon preference of Komagataella pastoris, and then a cell-penetrating peptide is introduced at the N terminus of the sequence; a corresponding genetically-engineered yeast strain is constructed and obtained, and fermentation is performed to successfully prepare the recombinant collagen. Compared with commercially available recombinant collagens, the prepared recombinant collagen has better free radical scavenging performance and skin penetration performance, thereby effectively solving the problem of poor skin penetration of existing collagens, and further improving the biological activity and efficacy of same.

Soluble, multi-polypeptide multispecific protein for recruiting an immune cell to a target cell presenting a target peptide major histocompatibility complex (pMHC), for therapeutic use against diseases such as cancer Protein comprising (i) a pMHC binding arm comprising a dimer of a first portion and a second portion, (ii) an immune cell engager moiety, and (iii) an Fc region comprising a dimer of a first Fc portion and a second Fc portion, wherein the first portion of the pMHC binding arm is linked at its N terminus to the immune cell engager moiety, and wherein the second portion of the pMHC binding arm is linked at its N terminus to a C terminus of the first Fc portion, and an N terminus of the Fc region is linked to a C terminus of the pMHC binding arm.

This peptide, or a pharmaceutically acceptable salt thereof, contains a substructure having an amino acid sequence selected from the group consisting of (1) and (2). (1) Amino acid sequence represented by formula (I): RYRYYGHNLIAYGFY (SEQ ID NO: 1); (2) Amino acid sequence represented by formula (I) with 1 to 6 amino acids substituted, where, when the arginine at the N terminus is defined as the first amino acid residue, the first amino acid residue is optionally substituted with a basic amino acid other than arginine and histidine; the second amino acid residue is optionally substituted with an aromatic amino acid other than tyrosine and histidine; the third amino acid residue is optionally substituted with a basic amino acid other than arginine and histidine; the fourth amino acid residue is optionally substituted with an aromatic amino acid other than tyrosine and histidine; the fifth amino acid residue is optionally substituted with an aromatic amino acid other than tyrosine and histidine or an amino acid containing a hydroxy group; the sixth amino acid residue is optionally substituted with alanine or an analog thereof, or a glycine analog; the seventh amino acid residue is optionally substituted with an amino acid other than cysteine, lysine, proline, arginine, threonine, valine, and tryptophan; the eighth amino acid residue is optionally substituted with aspartic acid, glycine, tyrosine, phenylalanine, serine, histidine, glutamic acid, glutamine, alanine, leucine, or analogs thereof, or an asparagine analog; the ninth amino acid residue is optionally substituted with an amino acid other than glycine, proline, and tryptophan; the tenth amino acid residue is optionally substituted with a branched chain amino acid other than isoleucine; the eleventh amino acid residue is optionally substituted with an amino acid other than glycine, proline, and tryptophan; the twelfth amino acid residue is optionally substituted with a tyrosine analog or a phenylalanine analog; the thirteenth amino acid residue is optionally substituted with alanine or an analog thereof, or a glycine analog; the fourteenth amino acid residue is optionally substituted with histidine, leucine, tyrosine, tryptophan, or analogs thereof, or a phenylalanine analog; and the fifteenth amino acid residue is optionally substituted with an aromatic amino acid other than tyrosine and histidine.

To improve the coaggregation of the PPR protein, the A6 amino acid of the 1st PPR motif from the N terminus (M1) is made more hydrophilic. Further, the A9 amino acid of M1 is made a hydrophilic amino acid or glycine. The A6 amino acid is preferably asparagine or aspartic acid, and the A9 amino acid is preferably glutamine, glutamic acid, lysine or glycine. A protein containing such a PPR motif as the M1 motif not only improves coaggregation, but also can have high binding to a target nucleic acid.

The invention belongs to the technical field of biology, and particularly relates to a THSD7A recombinant antigen and a preparation method and application thereof. The invention provides a THSD7A recombinant antigen, the THSD7A recombinant antigen comprises a region 1 and a region 2 which are connected in sequence from an N terminal to a C terminal, and the C terminal is connected or not connected with a label; the region 2 is epitope peptides which are connected in series; the N-terminal dominant epitope structural domains of the THSD7A antigen are connected in series, so that the THSD7A recombinant antigen with a specific structure is formed, the THSD7A recombinant antigen is used for detecting the THSD7A antibody in a sample, and the THSD7A recombinant antigen not only has higher stability, but also has higher activity.

The present application relates to the technical field of genetic engineering, and discloses a heat-resistant high-yield T7 RNA polymerase mutant, a preparation method and application thereof.The T7 RNA polymerase mutant of the present application is a protein as described in A1) or A2) below: A1) a protein obtained by substituting amino acids at at least four positions of V185, H205, K206, M226, D388, S430, H523 and I581 of a wild-type T7 RNA polymerase; wherein the amino acid sequence of the wild-type T7 RNA polymerase is shown in SEQ ID NO:1; A2) a fusion protein obtained by connecting a tag to the N terminus and / or C terminus of the amino acid sequence described in A1).Compared with the wild-type T7 RNA polymerase, the T7 RNA polymerase mutant of the present application exhibits better heat resistance and transcription activity.

The present invention relates to multi-domain binding molecules. The molecules comprise i) a peptide-major histocompatibility complex (pMHC) binding domain comprising a first variable region linked to a constant region (VC1) and a second variable region linked to a constant region (VC2), wherein VC1 and VC2 dimerise to form the pMHC binding domain; ii) an immune cell engaging domain comprising an antibody light chain variable domain (TCE-VL) linked to an antibody heavy chain variable domain (TCE-VH); and iii) a half-life extending domain comprising a first portion of an IgG Fc region (FC1) and a second portion of an IgG1 Fc region (FC2); wherein the multi-domain binding molecule comprises: a first polypeptide chain in which the immune cell engaging domain is linked to the N terminus of VC1; a second polypeptide chain in which VC2 is linked via its C terminus to the N terminus of FC1; and a third polypeptide chain comprising FC2; and wherein the pMHC binding domain and the immune cell engaging domain are capable of binding to a pMHC complex and a T cell respectively. The binding molecules can be used to treat diseases such as cancer, autoimmune diseases and infectious diseases.

The invention belongs to the technical field of molecular biology, and provides an NPL three-modification tag and application thereof in improving the exosome secretion level of a target protein. According to the technical scheme, an N-myristic acylation modification tag (N-Myr), a PPXY tag (P) and an LYP (X) nL tag (L) are sequentially connected to the N end of the target protein to form an NPL three-modification tag, an expression vector carrying coding nucleic acid of the tag is constructed, host cells are transfected, and then separation and purification are performed to obtain the exosome containing the high-secretion-level target protein. The tag can remarkably improve the exosome packaging efficiency of the target protein, the synergistic interaction effect of the three tags is far better than that of single or double tag modification, the natural form and the targeted delivery capacity of the exosome are not affected, an efficient and universal technical scheme is provided for exosome-mediated drug delivery, and the application prospect is wide. The important application value is realized in the fields of tumor treatment, gene therapy and the like.

The present application relates to a bifunctional fusion protein targeting CCR5 and gp41 and its application in the preparation of anti-human immunodeficiency virus drugs, and belongs to the technical field of biological medicine. The present application provides a bifunctional fusion protein targeting CCR5 and gp41, wherein the bifunctional fusion protein comprises: a fusion protein obtained by connecting a polypeptide 2P23 to the N terminus and / or C terminus of the light chain and / or heavy chain of an antibody PRO 140 or a PRO 140 mutant through a connecting peptide; or a fusion protein obtained by connecting a tag to the N terminus and / or C terminus of the above-mentioned fusion protein. The novel bifunctional fusion protein constructed in the present application not only overcomes the limitation that the original PRO 140 antibody is invalid for CXCR4 tropic strains, but also significantly improves the inhibitory activity and broad spectrum for CCR5 tropic strains, and has a higher drug resistance barrier.