Recombinant Rabbit monoclonal primary
Caveolin-2 Recombinant Rabbit Monoclonal Antibody [SY22-05] (ET1607-15)
Synthetic peptide within human caveolin-2 aa 1-50 / 162.
HUVEC, Hela, human cervix uteri tissue, human uterus tissue.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A purified.
CAV antibody; CAV2 antibody; CAV2_HUMAN antibody; Caveolae protein 20 kD antibody; Caveolin 2 antibody; Caveolin 2 isoform a and b antibody; Caveolin-2 antibody; MGC12294 antibody; OTTHUMP00000025032 antibody; OTTHUMP00000195982 antibody
Belongs to the caveolin family.
Expressed in endothelial cells, smooth muscle cells, skeletal myoblasts and fibroblasts.
Phosphorylated on serine and tyrosine residues. CAV1 promotes phosphorylation on Ser-23 which then targets the complex to the plasma membrane, lipid rafts and caveolae. Phosphorylation on Ser-36 appears to modulate mitosis in endothelial cells (By similarity). Phosphorylation on both Tyr-19 and Tyr-27 is required for insulin-induced 'Ser-727' phosphorylation of STAT3 and its activation. Phosphorylation on Tyr-19 is required for insulin-induced phosphorylation of MAPK1 and DNA binding of STAT3. Tyrosine phosphorylation is induced by both EGF and insulin (By similarity).
Cytoplasm, Nucleus, Membrane.
Caveolae (also known as plasmalemmal vesicles) are 50-100 nM flask-shaped membranes that represent a subcompartment of the plasma membrane. On the basis of morphological studies, caveolae have been implicated to function in the transcytosis of various macromolecules (including LDL) across capillary endothelial cells, uptake of small molecules via potocytosis and the compartmentalization of certain signaling molecules including G protein-coupled receptors. Three proteins, caveolin-1, caveolin-2 and caveolin-3, have been identified as principal components of caveolae. Two forms of caveolin-1, designated a and b, share a distinct but overlapping cellular distribution and differ by an N-terminal 31 amino acid sequence that is absent from the b isoform. Caveolin-1 shares 31% identity with caveolin-2 and 65% identity with caveolin-3 at the amino acid level. Functionally, the three proteins differ in their interactions with heterotrimeric G protein isoforms.