10 results about "HECT domain" patented technology

A fusion protein comprising at least one first polypeptide moiety and at least one second polypeptide moiety wherein the first polypeptide moiety is a single-chain polypeptide capable of binding to a target entity and the second polypeptide moiety is a stabilizing polypeptide and comprises a single-chain alpha-helix-containing domain, wherein the second polypeptide moiety has no binding affinity for the target entity. The presence of the second polypeptide moiety may improve at least one property of the fusion protein as compared to the property of the first polypeptide moiety alone, where the improved property is selected from the group consisting of: alkaline stability, recombinant protein expression, and coupling to a vector.

This disclosure provides peptides which have an affinity for the focal adhesion targeting (FAT) domain of focal adhesion kinase (FAK). In particular, the peptides are modified and derived from the sequence of the LD2 alpha helical domain of paxillin (e.g., LD2 peptides), the LD4 domain of paxillin (e.g., LD4 peptides), and CD8 peptides. These peptides are capable of blocking an interaction between paxillin and FAK, thereby inhibiting FAK activity related to FAK-paxillin interaction. The invention further provides uses for such peptides as therapeutics for the treatment of cancer and other diseases characterized with FAK activity and / or expression (e.g., fibrosis).

The present application relates to the field of medical diagnosis, and provides a combined marker for predicting the curative effect of target immune drug for primary liver cancer and application thereof, wherein the combined marker is folate receptor gamma gene FOLR3, stratified protein gene SFN and coiled-coil domain containing 9 gene CCDC9 derived from peripheral blood leukocyte mRNA.The present application performs combined detection based on multiple peripheral blood leukocyte markers, and compared with a single molecular marker, can reduce errors caused by individual expression difference of a single index to some extent, so that the detection result is more accurate.The curative effect prediction model constructed based on detection of peripheral blood leukocyte mRNA level change can specifically recognize and detect in the early stage of tumor formation, has high sensitivity and high specificity, provides an important means for reasonable use of target immune drug for liver cancer patients sensitive or resistant to target immune drug, and has great significance for effective treatment of liver cancer in China.

The present disclosure provides a protein having luciferase activity comprising a secondary structural arrangement H1-L1-H2-L2-B1-L3-B2-L4-H3-L5-B3-L6-L4-L7-L5-L8-B6 wherein (i) "H" is a helical domain, "L" is a loop domain, and "B" is a beta chain domain wherein the length of the B5 domain is at least 11, 12, 13, or 14 amino acids, and wherein "L" is a cyclic domain, and "B" is a beta chain domain. And residue 11 of the B5 domain is F, Y or L; and the length of the B4 domain is at least 12 amino acids, and the residue 10 of the B4 domain is F, Y, L, I, K or M; and / or residue 12 of the B4 domain is F, L, R, D, M, Q or V; (ii) the H1 domain is at least 18 or 19 amino acids in length; the residue 9 of the H1 domain is T, S, H, R, C, L, D, V, A, Q, G, E, K, I, N or M; (iii) the length of the B3 domain is at least 6, 7, 8, 9 or 10 amino acids, and the residue 1 of the B3 domain is W or H; (iv) the length of the B4 domain is at least 12 amino acids, and the residue 10 of the B4 domain is F, Y, L, I, K or M; or (v) the length of the B4 domain is at least 12 amino acids, and the residue 12 of the B4 domain is L, R, D, M, Q, or V. Additional proteins disclosed herein are illustrated in the claims. Also provided herein are luciferase substrates, assay buffers, and kits comprising one or more of a protein having luciferase activity or a nucleic acid encoding the protein, an assay buffer, and a luciferase substrate.

The present application relates to a kind of recombinant human type III collagen and its preparation method and application, belong to the field of bioengineering technology.The amino acid sequence of the recombinant human type III collagen described in the present application is as shown in SEQ ID No.7, is through the directional arrangement of five characteristic triple helix domain and the expansion of polymerization, combined with high-density fermentation process of Pichia pastoris, successfully break through the technical barrier of 4.5g / L target protein concentration.The present application research shows that the recombinant protein at 0.5% concentration not only maintains more than 80% cell viability, more exhibits significant synergistic effect-promote fibroblast migration rate to increase more than 29% compared with blank control group, keratinocyte proliferation rate increases 40.62%, adhesion rate increases 6.53%, provides innovative solution for developing new collagen product with high-efficiency expression and multiple biological activities.

This invention discloses a short peptide and its derivatives that mimic the N-terminus of RhoE, and their pharmaceutical applications in the treatment of myocardial hypertrophy, belonging to the field of biomedical technology. This short peptide precisely mimics the amino acid sequence from position 1 to 20 of RhoE, specifically binding to the WW domain of WWP2 and competitively blocking the interaction between the N-Loop and C-Loop of its HECT domain. This causes the WWP2 conformation to change from a self-inhibited "closed" state to an activated "open" state, activating E3 ligase activity. The short peptide retains its binding ability to the cardiomyocyte membrane cavernin CAV3, allowing it to efficiently enter the cardiomyocyte cytoplasm via the cavernin endocytosis pathway, overcoming the deficiency of traditional drugs in clearing intracellular pathogenic proteins. Peptide derivatives constructed by fusing transmembrane peptides such as TAT ​​and T7 further improve intracellular delivery efficiency. Experiments have demonstrated that this short peptide and its derivatives can significantly promote WWP2 self-ubiquitination, enhance cardiomyocyte autophagic flux, clear intracellular pathogenic proteins, and effectively inhibit cardiomyocyte hypertrophy, making it suitable for the preparation of anti-myocardial hypertrophy drugs.

The invention is a divisional application of an invention patent application of which the application date is November 7, 2024, the application number is 202411581372.8, and the invention name is'a recombinant elastin-like protein as well as a preparation method and application thereof '. The invention relates to a recombinant elastin-like protein as well as a preparation method and application thereof, and belongs to the technical field of biomacromolecules. The invention provides a recombinant elastin-like protein. The recombinant elastin-like protein comprises an elastin-like protein motif and a collagen III functional motif, the amino acid sequence of the elastin-like motif is VPGXG; the amino acid sequence of the III type collagen functional motif is as shown in SEQ ID NO. 1. The invention provides the recombinant elastin-like protein which is fused with the collagen motif and the elastin motif of the triple helix structural domain with the activity of promoting cell adhesion, and the recombinant elastin-like protein has the temperature-sensitive characteristic, the pH response characteristic and the gel characteristic, and has the effects of resisting aging, resisting inflammation and repairing the skin barrier.

This invention relates to a recombinant human type XVII collagen, its preparation method, and its applications, belonging to the field of bioengineering technology. The amino acid sequence of the recombinant human type XVII collagen is shown in SEQ ID No. 4. It is formed by constructing recombinant monomers through the directional arrangement of two characteristic triple-helix domains, and then further formed by the tandem connection of eight monomer units. The collagen retains its natural active sites while enhancing its mechanical strength. Combined with high-density fermentation technology using Pichia pastoris, high-expression, high-purity recombinant collagen was successfully obtained. This recombinant protein not only maintains over 85% cell viability at a concentration of 0.5%, but also exhibits multiple biological activities—promoting fibroblast migration rate by over 57%, keratinocyte proliferation rate by 20.97%, and showing significant hair growth effects. This invention provides an innovative solution for developing novel collagen products with both high-efficiency expression and multiple biological activities.

The invention relates to the technical field of biology, in particular to extracellular matrix polymer protein and a preparation method and application thereof. The invention also relates to a recombinant protein composition, a polynucleotide composition, a carrier composition, a recombinant cell composition and an active additive or preparation used in the fields of tissue engineering, pharmacy or beauty and skin care related to the extracellular matrix multimeric protein. The extracellular matrix polymer protein comprises a first subunit and a second subunit, the first subunit comprises a first coiled-coil domain and at least one extracellular matrix protein fragment; the second subunit comprises a second coiled-coil domain and at least one extracellular matrix protein fragment; the first subunit and the second subunit are non-covalently bound via the first coiled helical domain and the second coiled helical domain. The extracellular matrix polymer protein overcomes at least one of the defects of rigid multi-module assembly structure, insufficient activity retention and low yield after fusion of the traditional artificially prepared extracellular matrix protein.

The invention relates to recombinant human XVII type collagen as well as a preparation method and application thereof, and belongs to the technical field of bioengineering. The amino acid sequence of the recombinant human XVII type collagen is shown as SEQ ID No.4, and the recombinant human XVII type collagen is formed by constructing a recombinant monomer through directional arrangement of two characteristic triple helical structural domains and further connecting eight monomer units end to end in series; the collagen not only retains natural active sites, but also enhances the mechanical strength. And the recombinant collagen with high expression quantity and high purity is successfully obtained by combining a pichia pastoris high-density fermentation technology. The recombinant protein not only keeps more than 85% of cell activity at the concentration of 0.5%, but also shows multiple biological activities, the fibroblast migration rate is promoted to be improved by over 57%, the keratinocyte proliferation improvement rate is 20.97%, and the recombinant protein has a remarkable hair growth effect; the invention provides an innovative solution for developing a novel collagen product with efficient expression and multiple biological activities.