C9992
Anti-Caveolin-2 antibody produced in rabbit
~1 mg/mL, affinity isolated antibody, buffered aqueous solution, suitable for western blot: 1 μg/mL
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About This Item
Recommended Products
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~20 kDa
species reactivity
pig (predicted), mouse, rat, canine, human (predicted)
concentration
~1 mg/mL
technique(s)
indirect immunofluorescence: suitable
western blot: 1-2 μg/mL using whole extract of mouse 3T3-L1 adipocytes or rat kidney NRK cells
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... CAV2(858)
mouse ... Cav2(12390)
rat ... Cav2(363425)
General description
Caveolin-2 is an isoform of caveolin, an integral transmembrane protein of the caveolae membranes. It has a molar mass of 20-22 kDa and is a major coat protein found in caveolae of most cell types. It exists as two isoforms α and β due to alternative splicing of the respective mRNAs. Caveolin-2α corresponds to the full-length protein (20 kDa, 162 amino acids), whereas caveolin-2β isoform lacks a 13 amino acid sequence at its N-terminus.
Immunogen
synthetic peptide corresponding to amino acids 1-20 located at the N-terminus of mouse caveolin-2, conjugated to KLH. This sequece is identical in rat caveolin-2, highly conserved (90% identity) in human, dog, and pig caveolin-2, and is not found in caveolin-1 and caveolin-3.
Biochem/physiol Actions
Caveolin-2 colocalizes and forms a hetero-oligomeric complex with caveolin-1 in vivo. Caveolins family members function as scaffolding proteins to organize and concentrate specific lipids such as cholesterol and glycosylphosphatidylinositol (GPI) and lipid modified signaling molecules within caveolae membranes. Caveolin-2 is phosphorylated on Ser23 and Ser36 and modulates caveolin-1-dependent caveola formation.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Romina Paula Bulacio et al.
Journal of cellular biochemistry, 120(4), 4966-4974 (2018-10-01)
Caveolin-2 (Cav-2) is expressed in a variety of cell tissue, and it has also been found in renal tissue. The expression of Cav-2 in proximal tubules is still unclear. The aim of this study was to carry out a complete
R G Anderson
Annual review of biochemistry, 67, 199-225 (1998-10-06)
The cell biology of caveolae is a rapidly growing area of biomedical research. Caveolae are known primarily for their ability to transport molecules across endothelial cells, but modern cellular techniques have dramatically extended our view of caveolae. They form a
S Li et al.
The Journal of biological chemistry, 271(1), 568-573 (1996-01-05)
Caveolin, a 22-24-kDa integral membrane protein, is a principal component of caveolar membranes in vivo. Caveolin has been proposed to function as a scaffolding protein to organize and concentrate signaling molecules within caveolae. Because of its unusual membrane topology, both
P E Scherer et al.
The Journal of biological chemistry, 272(46), 29337-29346 (1997-11-20)
Caveolae are microdomains of the plasma membrane that have been implicated in organizing and compartmentalizing signal transducing molecules. Caveolin, a 21-24-kDa integral membrane protein, is a principal structural component of caveolae membrane in vivo. Recently, we and other laboratories have
M Sargiacomo et al.
Proceedings of the National Academy of Sciences of the United States of America, 92(20), 9407-9411 (1995-09-26)
A 22-kDa protein, caveolin, is localized to the cytoplasmic surface of plasma membrane specializations called caveolae. We have proposed that caveolin may function as a scaffolding protein to organize and concentrate signaling molecules within caveolae. Here, we show that caveolin
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