6 results about "Transmembrane peptide" patented technology

The invention relates to a fusion protein for detecting an anti-LGI1 antibody and application of the fusion protein. The invention particularly relates to a fusion protein for detecting an anti-LGI1 antibody, the fusion protein sequentially comprises a kappa chain signal peptide, an LGI1 protein and a PDGFR beta transmembrane peptide from an N terminal to a C terminal, and the amino acid sequence of the LGI1 protein is shown as SEQ ID NO.1. The kit prepared from the fusion protein has the advantages of simplicity, accuracy, high sensitivity and the like in LGI1 antibody detection.

This invention relates to hIL2 orthogonal ligands (“IL2 orthogonal homologs”) that specifically and selectively bind to transmembrane peptides comprising an extracellular domain (ECD) of a modified hCD122 polypeptide. The binding of the hIL2 orthogonal homolog to the modified hCD122 polypeptide participates in intracellular signal transduction pathways, resulting in biological activity associated with the native intracellular signal transduction pattern of hIL2 binding to intermediate- or high-affinity hIL2 receptors, but exhibiting selectivity for engineered hCD122 orthogonal receptors. Compared to its binding to the extracellular domain of wild-type hCD122, the hIL2 orthogonal homologs of this invention exhibit significantly reduced binding, either alone or when hCD122 is present in the form of an endogenous high- or intermediate-affinity hIL2 receptor.

The application discloses a kind of S3B polypeptide with SHP2 as action target point and its application in treating tumor and inflammation.The amino acid sequence of the polypeptide is RLLREEEYVAPPRGPLPTLQVVPL, the amino acid sequence of transmembrane peptide included in the polypeptide is TAT:YGRKKRRQRRR, the polypeptide can enter cell after being wrapped by liposome, inhibits QPCTL enzyme activity, promotes the degradation of SHP2 protein, thereby playing the role of inhibiting tumor cell proliferation, migration and growth, etc., to achieve the purpose of treating tumor and other diseases.The application provides a certain reference for treating SHP2 related tumor or immune inflammatory disease and developing new SHP2 degradation drug.

The application relates to the technical field of biological medicine engineering, and provides a preparation method and application of a scorpion toxin-derived transmembrane polypeptide. The OpiCalcin1 polypeptide is optimized in a truncation mode, two polypeptides Opi1 17-33 CSKKCKRRGTNPEKRCR and Opi1 23-33 RRGTNPEKRCR with excellent transmembrane function and low cytotoxicity are provided. Through experiment verification, the two cell transmembrane peptides have excellent transmembrane effect and low cytotoxicity, meanwhile, the defects of time-consuming and laborious in synthesizing the complete sequence of scorpion toxin OpiCalcin1 are overcome, the cell transmembrane peptides can be used for preparing drug, nuclear localization sequence and probe transport carriers, and the targeting efficiency is improved. Compared with traditional scorpion toxin medicine, the synthesis of the scorpion toxin to explore the transmembrane activity provides a new selection for the drug carrier.

The invention discloses a preparation method and application of a fatty acid transporter FATP transmembrane domain. The method comprises the following steps: fusing a gene for coding an FATP transmembrane domain with a TrpLE tag sequence, and performing high-efficiency expression in escherichia coli to form an inclusion body. Thirdly, primarily purifying the fusion protein by using nickel column affinity chromatography, and specifically releasing a target transmembrane peptide fragment through cyanogen bromide chemical cleavage; and finally, carrying out fine purification by adopting one-step reversed-phase high-performance liquid chromatography to obtain a milligram-grade high-purity peptide fragment. The purified peptide fragment can be successfully reconstructed in a plurality of membrane simulation systems such as Fos-choline-14 micelles or DMPC / DHPC (Dimethyl Polycarbonate / Dimethyl Hexaphthyl Polycarbonate) lipid saucers and the like. According to the method, high-level expression of the FATP transmembrane domain in escherichia coli is achieved, the purification process is simple, convenient and efficient, the final product is high in purity, the yield can reach the milligram level, and the method is suitable for stable isotope labeling and meets the requirements of fine structure research such as nuclear magnetic resonance.

This invention relates to hIL2 orthogonal ligands (“IL2 orthogonal homologs”) that specifically and selectively bind to transmembrane peptides comprising an extracellular domain (ECD) of a modified hCD122 polypeptide. The binding of the hIL2 orthogonal homolog to the modified hCD122 polypeptide participates in intracellular signal transduction pathways, resulting in biological activity associated with the native intracellular signal transduction pattern of hIL2 binding to intermediate- or high-affinity hIL2 receptors, but exhibiting selectivity for engineered hCD122 orthogonal receptors. Compared to its binding to the extracellular domain of wild-type hCD122, the hIL2 orthogonal homologs of this invention exhibit significantly reduced binding, either alone or when hCD122 is present in the form of an endogenous high- or intermediate-affinity hIL2 receptor.