Caveolin 1, Caveolae Protein, 22kDa (CAV1) (AA 1-178) antibody

Antigen: Caveolin 1, Caveolae Protein, 22kDa (CAV1)

Synonyms: CAV, CGL3, BSCL3, VIP21, MSTP085, Cav, Cav-1, MGC187299, CAV1, fc07c04, wu:fc07c04, cav1a, cav1b, caveolin 1, cav, vip21, mstp085, MGC107940, Caveolin-1, cav1

Binding Site: AA 1-178

Clonality: Monoclonal (2234)

Host: Mouse

Reactivity: Chicken, Human

Conjugate: Un-conjugated

Application: Western Blotting (WB), Immunofluorescence (IF), Immunoprecipitation (IP)

Catalog no.: ABIN968001

Additional Information

Alternative name: Caveolin 1

Immunogen: RSV-CEF Caveolin

Format: Liquid

Isotype: IgG2a

Clone: 2234

Description: Identified as a tyrosine phosphorylated protein in Rous sarcoma virus-transformed chick embryo fibroblasts (CEF), caveolin is now known to be ubiquitously expressed. Caveolin (also known as VIP21) localizes to non-clathrin membrane invaginations (caveolae) on the inner surface of the plasma membrane. This transmembrane protein plays a structural role in these specializations. Caveolin is also present at the trans-Golgi network (TGN) and similar quantities are found in apically and basolaterally destined transport vesicles. Caveolin is part of a complex containing glycosylphosphatidylinositol (GPI)-linked molecules and cytoplasmic signaling proteins. Caveolin is a transmembrane adaptor molecule that can simultaneously recognize GPI-linked proteins and interact with downstream cytoplasmic signaling molecules, such as c-yes, Annexin II, and hetero-trimeric G proteins. Caveolin-1 can generate two forms, alpha and beta, due to alternate splicing of the mRNA. Caveolin-1 forms large lipid-binding homo-oligomers which are believed to play a role in caveolae formation. It may also function as a scaffolding protein which concentrates and organizes signaling molecules, a role supported by the fact that caveolin-1 interacts directly with inactive Ras and G-protein alpha subunits. This antibody is routinely tested by western blot analysis.

Characteristics: 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.

Molecular Weight: 22 kDa

Comments:

Related Products: ABIN967389, ABIN968554

Application Details

Concentration: 250 µg/ml

Purity: Purified

Purification: Purified from tissue culture supernatant or ascites by affinity chromatography.

Buffer: Aqueous buffered solution containing BSA, glycerol.

Preservative: 0.09% Sodium azide.

Storage: Store undiluted at -20°C.

Research Area: Cancer, Organelles, Signaling

Restrictions: For Research Use only

Images

Western blot analysis of Caveolin 1. Lane 1: 1:5000, lane 2: 1:10000, lane 3: 1:20000 dilution of Caveolin 1.

Human Fibroblast

Publications

Product: Scherer, Tang, Chun et al.: "Caveolin isoforms differ in their N-terminal protein sequence and subcellular distribution. Identification and epitope mapping of an isoform-specific monoclonal antibody probe." in: The Journal of biological chemistry, Vol. 270, Issue 27, pp. 16395-401, 1995 (PubMed).

Conrad, Smart, Ying et al.: "Caveolin cycles between plasma membrane caveolae and the Golgi complex by microtubule-dependent and microtubule-independent steps." in: The Journal of cell biology, Vol. 131, Issue 6 Pt 1, pp. 1421-33, 1996 (PubMed).

Schlegel, Arvan, Lisanti: "Caveolin-1 binding to endoplasmic reticulum membranes and entry into the regulated secretory pathway are regulated by serine phosphorylation. Protein sorting at the level of the endoplasmic reticulum." in: The Journal of biological chemistry, Vol. 276, Issue 6, pp. 4398-408, 2001 (PubMed).

Razani, Zhang, Bitzer et al.: "Caveolin-1 regulates transforming growth factor (TGF)-beta/SMAD signaling through an interaction with the TGF-beta type I receptor." in: The Journal of biological chemistry, Vol. 276, Issue 9, pp. 6727-38, 2001 (PubMed).

Oh, Schnitzer: "Segregation of heterotrimeric G proteins in cell surface microdomains. G(q) binds caveolin to concentrate in caveolae, whereas G(i) and G(s) target lipid rafts by default." in: Molecular biology of the cell, Vol. 12, Issue 3, pp. 685-98, 2001 (PubMed).