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 α and β, share a distinct but overlapping cellular distribution and differ by an amino-terminal 31 amino acid sequence which is absent from the β 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.

Caveolin 1; Caveolin1; CAV1; CAV

q03135

Human,Mouse,Rat

WB,IF,ICC

WB 1:500-1:1000
IF 1:50-1:200
ICC 1:100-1:400

~ 20, 25 kDa

Rabbit

This antibody detects endogenous levels of Caveolin-1 protein.

Synthetic peptide, corresponding to amino acids 150-200 of Human Caveolin-1.

Polyclonal

Rabbit IgG

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

PBS with 0.02% sodium azide, 50% glycerol, pH7.2

1mg/ml

Store at 4℃ short term,and store at -20℃ long term. Avoid freeze-thaw cycles.