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Western blot analysis of Caveolin 2 on a RSV-3T3 cell lysate. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of the mouse anti-Caveolin 2 antibody.
Immunofluorescence staining of FHs cells (Normal human fetal lung fibroblasts; ATCC HTB-157).
BD Transduction Laboratories™ Purified Mouse Anti-Caveolin 2
BD Transduction Laboratories™ Purified Mouse Anti-Caveolin 2
Regulatory Status Legend
Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
Preparation And Storage
Recommended Assay Procedures
Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- 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.
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. Although caveolin 2 is similar to caveolin 1 in distribution and tissue expression, caveolin 2 is most abundant in adipose tissue and its expression is up-regulated upon differentiation. This antibody has been reported to recognize an epitope located within region 79-88 of caveolin 2.
Development References (6)
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Das K, Lewis R, Scherer P, Lisanti M. The membrane-spanning domains of caveolins-1 and -2 mediate the formation of caveolin hetero-oligomers. J Biol Chem. 1999; 274(26):18721-18728. (Immunogen).
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Kiss AL, Turi A, Mullner N, Timar J. Caveolin isoforms in resident and elicited rat peritoneal macrophages. Eur J Cell Biol. 2000; 79(5):343-349. (Biology: Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western blot). View Reference
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Scherer PE, Okamoto T, Chun M, Nishimoto I, Lodish HF, Lisanti MP. Identification, sequence, and expression of caveolin-2 defines a caveolin gene family. Proc Natl Acad Sci U S A. 1996; 93(1):131-135. (Biology). View Reference
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Tauchi-Sato K, Ozeki S, Houjou T, Taguchi R, Fujimoto T. The surface of lipid droplets is a phospholipid monolayer with a unique Fatty Acid composition. J Biol Chem. 2002; 277(46):44507-44512. (Biology: Electron microscopy, 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. (Biology: Immunofluorescence, Western blot). View Reference
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Zschocke J, Manthey D, Bayatti N, van der Burg B, Goodenough S, Behl C. Estrogen receptor alpha-mediated silencing of caveolin gene expression in neuronal cells. J Biol Chem. 2002; 277(41):38772-38780. (Biology: Immunofluorescence, Immunohistochemistry, Western blot). View Reference
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