8 results about "Transmembrane glycoprotein" patented technology

The present invention relates to a preparation method of a photoelectrochemical sensor for detecting the transmembrane glycoprotein CD44 on the surface of breast cancer cells. The preparation method is divided into three steps. First, a TiO2 nanoarray is loaded on the surface of FTO conductive glass by a hydrothermal method. Then, a Ag nano-layer is uniformly sputtered on the surface of the TiO2 nanoarray by using a magnetron sputtering technique. Finally, the TiO2-Ag is immersed in a sodium sulfide solution to realize the local sulfidation of Ag to obtain a photoelectric conversion body, a TiO2-Ag-Ag2S nano-composite array. Then, the extraction of the transmembrane glycoprotein CD44 on the surface of breast cancer cells MDA-MB-231 is realized by using the host-guest recognition between hyaluronic acid and the transmembrane glycoprotein CD44 and a DNA strand displacement reaction. Finally, through bioconjugation and covalent bonding, the assembly of the optoelectronic material and the target on the conductive interface is realized. The preparation method of this sensor has stronger controllability compared with other reported methods, especially obtaining a sensing interface with good signal output stability. The scheme and process mentioned in this method have important reference in the fields of material synthesis, photoelectrochemical sensing, cell detection, etc.

A chimeric antigen receptor (CAR) comprises an extracellular antigen binding domain, wherein the extracellular antigen binding domain comprises a polypeptide that binds to an oncostatin-M receptor (OSMR), a leukemia inhibitory factor receptor (LIFR), a heterodimer of a transmembrane glycoprotein 130 (gp130) receptor and OSMR, and / or a heterodimer of a gp130 receptor and LIFR.

The present disclosure provides monoclonal antibodies that recognize human Nectin-2 (Nectin-2, Poliovirus Receptor-Related Protein-2, Poliovirus Receptor-Like 2, CDI12, or PRR-2, is a single pass transmembrane glycoprotein with two Ig-like C2-type domains and an Ig-like V-type domain) with high affinity and specificity and inhibit its binding to TIGIT and / or CD112R. The antibodies recognize the Nectin-2 protein (CD112), prevent its binding to T cell immunoreceptor with Ig and ITIM domains (TIGIT) and CD112R (PVRIG) and inhibit suppressive activity on lymphocytes such as natural killer (NK) cells and T-cells. The disclosure further provides pharmaceutical and methods for use in cancer immunotherapy and in diagnosis. The disclosure finally further provides chimeric antigen receptor (CAR) comprising scFv antibody binding to Nectin-2.

A chimeric antigen receptor (CAR) comprises an extracellular antigen-binding domain, which comprises a polypeptide that binds to oncostatin M receptor (OSMR), leukemia inhibitory factor receptor (LIFR), a heterodimer between transmembrane glycoprotein 130 (gp130) receptor and OSMR, and / or a heterodimer between gp130 receptor and LIFR.

This invention discloses the application of the extracellular domain of the transmembrane glycoprotein NMB in the treatment and improvement of acute kidney injury, belonging to the field of medical technology, to study the therapeutic effect and mechanism of the extracellular domain of the transmembrane glycoprotein NMB on acute kidney injury. This invention utilizes the extracellular domain of the transmembrane glycoprotein NMB to treat a disease model of acute kidney injury, finding that the extracellular domain of the transmembrane glycoprotein NMB can effectively alleviate ischemia-reperfusion-induced acute kidney injury, promote kidney tissue repair, and inhibit the progression of acute kidney injury to chronic inflammation and fibrosis.

The present disclosure provides monoclonal antibodies that recognize human Nectin-2 (Nectin-2, Poliovirus Receptor-Related Protein-2, Poliovirus Receptor-Like 2, CD112, or PRR-2, is a single pass transmembrane glycoprotein with two Ig-like C2-type domains and an Ig-like V-type domain) with high affinity and specificity and inhibit its binding to TIGIT and / or CD112R. The antibodies recognize the Nectin-2 protein (CD112), prevent its binding to T cell immunoreceptor with Ig and ITIM domains (TIGIT) and CD112R (PVRIG) and inhibit suppressive activity on lymphocytes such as natural killer (NK) cells and T-cells. The disclosure further provides pharmaceutical and methods for use in cancer immunotherapy and in diagnosis. The disclosure finally further provides chimeric antigen receptor (CAR) comprising scFv antibody binding to Nectin-2.

The present application relates to the technical field of reagent kit, specifically a reagent kit for determining liver cancer through transmembrane glycoprotein and a use method thereof, the reagent kit for determining liver cancer through transmembrane glycoprotein comprises a box body and a box cover rotatably arranged on the box body, further comprising: a partition plate installed in the box body, and a plurality of through holes are formed in the partition plate; a plurality of sets of elastic limiting mechanisms are arranged on the bottom wall of the box body, and the elastic limiting mechanisms correspond to the through holes; a plurality of sets of elastic clamping mechanisms are arranged on the upper part of the partition plate, and the elastic clamping mechanisms are connected with trigger transmission mechanisms installed on the partition plate; the elastic limiting mechanisms and the elastic clamping mechanisms can stabilize the lower end and the upper end of the reagent bottle, ensure the stability of the reagent bottle in the reagent kit during the transfer process, and effectively avoid the risk of reagent leakage caused by damage of the reagent bottle.

CD95L is a transmembrane glycoprotein that acts through cell contact. After cleavage by metalloproteases, a soluble CD95L (cleaved CD95L or cl-CD95L) is released into the bloodstream. This soluble ligand contributes to aggravate chronic inflammatory disorders such as systemic lupus erythematosus (SLE) and may exert pro-oncogenic functions by promoting the survival of ovarian and breast cancers and chemotherapy resistance of lung cancers. The inventors hypothesized that monoclonal antibodies targeting the Metalloprotease-Cleavage Sites of CD95L (MCSCs) encompassing amino-acid residues 103 to 145 could prevent the access to metalloproteases and inhibit CD95L shedding. Therefore, they generated antibodies covering different epitopes within MCSC and two of them (i.e., 3C7 and 9F5), efficiently abrogated the cleavage of CD95L by MMP2 and MMP3. The results indicate that these MCSC-targeting mAbs can compete with MMPs and represent original and attractive therapeutic options to block the release of the inflammatory s-CD95L.