Anti-TRPC6

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Transient receptor potential cation channel, subfamily C, member 6, also known as TRP6, is a transient receptor potentialion channel. Northern blot analysis revealed that TRPC6 is expressed primarily in placenta, lung, spleen, ovary, and small intestine. The protein is a nonselective cation channel that is activated by diacylglycerol (DAG) in a membrane-delimited fashion, independently of protein kinase C. Although TRPC3, the closest structural relative of TRPC6, is activated in the same manner, human TRPC1 and mouse Trpc4 and Trpc5 were unresponsive to DAG. Immunofluorescence studies showed that most TRPC6 expression is confined to podocytes. It is also expressed in glomerular endothelial cells. Cardiac-specific overexpression of the protein in transgenic mice resulted in heightened sensitivity to stress, a propensity for lethal cardiac growth and heart failure, and an increase in Nfat-dependent expression of beta-myosin heavy chain(MYH7), a marker for pathologic hypertrophy. Studies of Trpc6 -/- mice showed that it has a role in regulation of smooth muscle tone in blood vessels and lung. Protein function: Thought to form a receptor-activated non-selective calcium permeant cation channel (PubMed:19936226, PubMed:23291369). Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG) in a membrane-delimited fashion, independently of protein kinase C (PubMed:26892346). Seems not to be activated by intracellular calcium store depletion. [The UniProt Consortium]