Caveolin 1, Caveolae Protein (CAV1) (1st Cytoplasmic Domain) antibody

Antigen: Caveolin 1, Caveolae Protein (CAV1)

Binding Site: 1st Cytoplasmic Domain

Clonality: Polyclonal

Host: Rabbit

Application: Immunohistochemistry (IHC), Western Blotting (WB)

Catalog no.: ABIN350195

Additional Information

Alternative name: Caveolin-1 (CAV1, CAV)

UniProt: Q03135

Immunogen: A synthetic peptide from the 1t cytoplasmic domain of human Caveolin-1 (CAV1, CAV) conjugated to an immunogenic carrier protein was used as the immunogen. The antigen is homologous in many other species including rat, mouse.

Format: Lyophilized

Description: FUNCTION: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass membrane protein. Cell membrane; Single-pass membrane protein. Note: Potential hairpin-like structure in the membrane. Membrane protein of protein of caveolae. TISSUE SPECIFICITY: In muscle and lung, less so in liver, brain and kidney. Also known as: CAV1, CAV.

Specificity: Appears to be specific for Caveolin-1.

Application Details

Application Notes: IHC, WB. A dilution of 1 : 300 to 1 : 2000 is recommended. The optimal dilution should be determined by the end user. Not tested in other applications.

Purity: whole serum

Storage: Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.

Restrictions: For Research Use only

Images

WB on rat brain lysate using Rabbit antibody to 1t cytoplasmic domain of Caveolin-1 (CAV1, CAV): whole serum (ABIN350195) at 1 : 1000 dilution. Pre-absorption of the antibody with the immunising peptide completely abolishes the detected band.

Publications

Eberle, Serrano, Fuellekrug et al.: "Identification and characterization of a novel human plant pathogenesis-related protein that localizes to lipid-enriched microdomains in the Golgi complex." in: Journal of cell science, Vol. 115, Issue Pt 4, pp. 827-38, 2002 (PubMed).

Aboulaich, Vainonen, Strålfors et al.: "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes." in: The Biochemical journal, Vol. 383, Issue Pt 2, pp. 237-48, 2004 (PubMed).

Schilling, Opitz, Wiesenthal et al.: "Translocation of endothelial nitric-oxide synthase involves a ternary complex with caveolin-1 and NOSTRIN." in: Molecular biology of the cell, Vol. 17, Issue 9, pp. 3870-80, 2006 (PubMed).

Olsen, Blagoev, Gnad et al.: "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." in: Cell, Vol. 127, Issue 3, pp. 635-48, 2006 (PubMed).

Dephoure, Zhou, Villén et al.: "A quantitative atlas of mitotic phosphorylation." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 105, Issue 31, pp. 10762-7, 2008 (PubMed).