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Anti-phospho-Caveolin-1 (Ser37) from rabbit, purified by affinity chromatography

ITEM#: 3042-ABS1007

MFR#: ABS1007

Caveolin-1 (UniProt: Q03135) is encoded by the CAV1 (also known as CAV) gene (Gene ID: 857) in human. Three caveolin genes are expressed in mammals and are designated as caveolin-1, -2, and -3. Most mammalian tissues express at least one of these iso

Caveolin-1 (UniProt: Q03135) is encoded by the CAV1 (also known as CAV) gene (Gene ID: 857) in human. Three caveolin genes are expressed in mammals and are designated as caveolin-1, -2, and -3. Most mammalian tissues express at least one of these isoforms. Caveolin-1 is expressed in skeletal muscle, liver, stomach, lung, brain, kidney and heart. Caveolin-1 and -2 are usually co-expressed and assemble into hetero-oligomers in the endoplasmic reticulum and Golgi apparatus. Two isoforms of caveolin-1 have been reported that are produced by alternative initiation. It has two cytoplasmic domains (aa 2-104 and 126-178) and an intramembrane domain (aa 105-125). The primary structure of caveolin-1 contains two serine residues, both residing in a phosphorylation consensus sequence and flanked by a regulatory scaffolding domain. Serine 37 site represents a PKC consensus site, while Serine 88 is believed to be phosphorylated by CK II alpha. Caveolin-1 acts as a scaffolding protein within caveolar membranes and is shown to interact directly with G-protein alpha subunits to functionally regulate their activity. It is also involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. It can bind to DPP4 and induce T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Mutations in CAV1 gene are known to cause Congenital generalized lipodystrophy 3 that is characterized by a near complete absence of adipose tissue, extreme insulin resistance, hypertriglyceridemia, and early onset of diabetes. Some mutations have also been linked to primary pulmonary hypertension with plexiform lesions of proliferating endothelial cells in pulmonary arterioles leading to elevated pulmonary arterial pression, right ventricular failure, and death. (Ref.: Liu, P., et al. (2002). J. Biol. Chem. 277 (44); 41295-41298; Garver, WS., et al. (1999). Biocheim. Biophys. Acta 143 (1453); 193-206).