Mouse monoclonal primary
Caveolin-1 Monoclonal Antibody (EM40728)
Hela, HepG2, A549, Jurkat, F9, L929, human lung tissue, mouse lung tissue, mouse liver tissue, rat lung tissue, mouse bladder tissue
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*PBS (pH7.4), 0.2% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A purified.
Belongs to the caveolin family.
Skeletal muscle, liver, stomach, lung, kidney and heart (at protein level). Expressed in the brain.
Ubiquitinated. Undergo monoubiquitination and multi- and/or polyubiquitination. Monoubiquitination of N-terminal lysines promotes integration in a ternary complex with UBXN6 and VCP which promotes oligomeric CAV1 targeting to lysosomes for degradation.; The initiator methionine for isoform 2 is removed during or just after translation. The new N-terminal amino acid is then N-acetylated.; Phosphorylated at Tyr-14 by ABL1 in response to oxidative stress.
Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein. Membrane raft. Golgi apparatus, trans-Golgi network. Note=Colocalized with DPP4 in membrane rafts. Potential hairpin-like structure in the membrane. Membrane protein of caveolae.
May act as a scaffolding protein within caveolar membranes. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae. Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway (By similarity). Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation.