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The S1PR1 recombinant monoclonal antibody is produced using recombinant DNA technology and is suitable for detecting human S1PR1 protein in ELISA and WB applications. The cDNA of the S1PR1 antibody-producing hybridomas is sequenced and acts as the model for the synthesis of the S1PR1 monoclonal antibody gene. The hybridomas are created by fusing myeloma cells with B cells that have been isolated from an animal that was immunized with a synthesized peptide derived from human EDG1. The synthesized gene is inserted into a vector and then transfected into cells for cultivation. The resulting S1PR1 recombinant monoclonal antibody is purified using affinity chromatography from the cell culture supernatant.
The S1PR1 protein, also called EDG1, binds to the sphingolipid signaling molecule S1P, activating several downstream signaling pathways, including the phospholipase C (PLC)-protein kinase C (PKC) pathway, the ERK pathway, and the PI3K-Akt pathway. These signaling pathways are involved in various cellular processes such as cell migration, proliferation, survival, and differentiation. In the immune system, S1PR1 plays a critical role in the regulation of lymphocyte trafficking and immune cell activation. In endothelial cells, S1PR1 regulates vascular tone and endothelial barrier function. Dysfunction of S1PR1 has been implicated in various diseases such as autoimmune disorders, cardiovascular diseases, and cancer.
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