Cavin-1 (D1P6W) Rabbit Monoclonal Antibody recognizes endogenous levels of total cavin-1 protein. Based on the sequence of the immunogenic peptide, this antibody is not expected to cross-react with other cavin family members.

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala177 of human cavin-1 protein.

Caveolae ("little caves") are 60-80 nm pits representing specialized plasma membrane domains in many cell types. The principal protein component of caveolae is caveolin, a small integral membrane protein composed of three family members, including the widely expressed caveolin-1 and -2, and the muscle-specific caveolin-3 (1). Caveolin proteins are required for caveolae formation and serve as scaffolding proteins for the recruitment of signaling proteins. Research studies in cavelolin-deficient mice implicate cavelolin proteins in several pathologies, including diabetes, cancer, cardiovascular diseases, atherosclerosis, pulmonary disease, and muscular dystrophies (2).
The cavin proteins (cavin-1, -2, -3, and -4 in mammals) are a family of caveolae-associated integral membrane proteins involved in the biogenesis and stability of caveolae. Cavin proteins form homo- or hetero-oligomers whose composition is tissue-specific, which may confer distinct functions of caveolae in various tissues (3). Cavin-1 (PTRF), which is widely expressed, is required for caveolae formation and is thought to play roles in lipid metabolism, adipocyte differentiation, and IGF-1 receptor signaling (4-6). Research studies involving prostate cancer suggest that expression of cavin-1 is related to tumor progression and angiogenesis/lymphangiogenesis (7-8).