Preparation And Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- 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.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
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, α and β, due to alternate splicing of the mRNA. The α isoform has been reported to be observed at 24 kD and the β isoform at 21 kD. 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 andorganizes signaling molecules, a role supported by the fact that caveolin-1 interacts directly with inactive Ras and G-protein α subunits.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.
Development References (5)
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Breton S, Lisanti MP, Tyszkowski R, McLaughlin M, Brown D. Basolateral distribution of caveolin-1 in the kidney. Absence from H+-atpase-coated endocytic vesicles in intercalated cells. J Histochem Cytochem. 1998; 46(2):205-214. (Clone-specific: Immunohistochemistry, Western blot). View Reference
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Conrad PA, Smart EJ, Ying YS, Anderson RG, Bloom GS. Caveolin cycles between plasma membrane caveolae and the Golgi complex by microtubule-dependent and microtubule-independent steps. J Cell Biol. 1995; 131(1):1421-1433. (Biology). View Reference
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Galbiati F, Volonte D, Brown AM, et al. Caveolin-1 expression inhibits Wnt/beta-catenin/Lef-1 signaling by recruiting beta-catenin to caveolae membrane domains. J Biol Chem. 2000; 275(30):23368-23377. (Clone-specific: Western blot). View Reference
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Ushio-Fukai M, Hilenski L, Santanam N, et al. Cholesterol depletion inhibits epidermal growth factor receptor transactivation by angiotensin II in vascular smooth muscle cells: role of cholesterol-rich microdomains and focal adhesions in angiotensin II signaling. J Biol Chem. 2001; 276(51):48269-48275. (Clone-specific: Immunoprecipitation, Western blot). View Reference
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Woodman SE, Park DS, Cohen AW, et al. Caveolin-3 knock-out mice develop a progressive cardiomyopathy and show hyperactivation of the p42/44 MAPK cascade. J Biol Chem. 2002; 277(41):38988-38997. (Clone-specific: Immunofluorescence, Western blot). View Reference
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For Research Use Only. Not for use in diagnostic or therapeutic procedures.
