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The protein encoded by CAV2 is a major component of the inner surface of caveolae, small invaginations of the plasma membrane, and is involved in essential cellular functions, including signal transduction, lipid metabolism, cellular growth control and apoptosis. Additionally we are shipping Caveolin 2 Proteins (24) and Caveolin 2 Kits (4) and many more products for this protein.
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Human Monoclonal Caveolin 2 Primary Antibody for IF, IP - ABIN968108
Das, Lewis, Scherer, Lisanti: The membrane-spanning domains of caveolins-1 and -2 mediate the formation of caveolin hetero-oligomers. Implications for the assembly of caveolae membranes in vivo. in The Journal of biological chemistry 1999
Show all 6 references for ABIN968108
Human Monoclonal Caveolin 2 Primary Antibody for FM, IHC (f) - ABIN967595
Conner, Schmid: Regulated portals of entry into the cell. in Nature 2003
Show all 4 references for ABIN967595
Cow (Bovine) Polyclonal Caveolin 2 Primary Antibody for IHC, WB - ABIN2792220
Sowa, Xie, Xu, Sessa: Serine 23 and 36 phosphorylation of caveolin-2 is differentially regulated by targeting to lipid raft/caveolae and in mitotic endothelial cells. in Biochemistry 2008
Show all 2 references for ABIN2792220
Human Polyclonal Caveolin 2 Primary Antibody for EIA, WB - ABIN453555
Murata, Peränen, Schreiner, Wieland, Kurzchalia, Simons: VIP21/caveolin is a cholesterol-binding protein. in Proceedings of the National Academy of Sciences of the United States of America 1995
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Caveolin-2 expression is necessary for the control of E2-dependent cellular proliferation of MCF-7 cells.
variant in CAV2 is associated with increased age-of-onset of P. aeruginosa airway infection in cystic fibrosis (show S100A8 Antibodies) cohort.
The minor allele G of rs17588172 in the CAV1 (show CAV1 Antibodies)-CAV2 locus is associated with decreased expression of CAV1 (show CAV1 Antibodies) and CAV2 in some tissues, marginally with intraocular pressure elevation, and consequently with increased susceptibility to high-tension glaucoma.
Results present initial characterization of key proteins Cav2 and CFL1 (show VPS72 Antibodies) as cellular factors that colocalize with M in viral inclusions and filaments and ZNF502 (show ZNF502 Antibodies) protein which appears to interact with RSV M in the nucleus.
The implication of the caveolin genes, CAV1 (show CAV1 Antibodies)/CAV2, as a common genetic factor influencing both IOP variations and POAG may provide new insights of the underlying mechanism leading to glaucoma and glaucomatous visual field loss.
CAV1 (show CAV1 Antibodies)/CAV2 SNPs were associated significantly with primary open-angle glaucoma overall, particularly among women.
Our findings did not correspond with previous positive results, suggesting that CAV1 (show CAV1 Antibodies)-CAV2 variants studied in the present study are not important risk factors for Normal Tension Glaucoma.
This study does not support an association between CAV2 variation and kidney transplant survival.
The combination of the expression of the genes for PPARgamma (show PPARG Antibodies), STMN1 (show STMN1 Antibodies) and CAV2 was significantly predictive for early recurrence of non-muscle-invasive bladder cancer
CAV1 (show CAV1 Antibodies) and -2 potentiate epsilon-toxin induced cytotoxicity by promoting toxin oligomerization
We concluded that caveolin-2 is most probably involved in regulation of pro-inflammatory responses of BMDMs, triggered via activation of ERK1/2 (show MAPK1/3 Antibodies).
Cav-2 expressed in tumor microenvironment may potentially become a novel target for cancer therapy
In contrast to wild-type-Cav-2, retroviral re-expression of Y19/27F-Cav-2 in Cav-2 knockout endothelial cells did not affect anti-proliferative effect of TGF-beta (show TGFB1 Antibodies) compared to empty vector.
Data show that the balance between caveolin-1 (show CAV1 Antibodies) and caveolin-2 is important for iNOS (show NOS2 Antibodies) expression and ultimately for sepsis outcome.
The negative regulation of transforming growth factor-beta1 signaling and function by caveolin 2 is independent of caveolin 1 (show CAV1 Antibodies) expression levels and is not because of changing targeting of caveolin 1 (show CAV1 Antibodies) protein to plasma membrane lipid raft/caveolar domains.
Data suggest that Cav-2 negatively regulates lung endothelial cell proliferation and cell cycle progression.
Data show that amino acids K47-K57 of Cav-1 (show CAV1 Antibodies) are a highly conserved sequence in Cav-1 (show CAV1 Antibodies) and Cav-3 (show CAV3 Antibodies) proteins, and that expression of either K47-K57 deletion Cav-1 (show CAV1 Antibodies) mutant or wild-type Cav-2 that lacks this sequence exhibits a non-polarized distribution pattern.
Caveolin-2-deficient mice show evidence of severe pulmonary dysfunction without disruption of caveolae
Splice variant of mouse caveolin-2 mRNA, encoding an isoform lacking the C-terminal domain, localized to the endoplasmic reticulum, while the authentic caveolin-2 was distributed to the Golgi and the plasma membrane along with caveolin-1 (show CAV1 Antibodies).
Src (show SRC Antibodies)-induced phosphorylation of caveolin-2 on tyrosine 19.
miR (show MYLIP Antibodies)-29a mediated Caveolin 2 regulation, modulating the activation state of CDC42 (show CDC42 Antibodies), in intestinal Salmonella infection, is reported.
The interaction of caveolin-2 with caveolin-1 (show CAV1 Antibodies) could play an important role in caveolae biogenesis and shear stimulated mechano-signal transduction.
caveolin-2 is an integral component of the trafficking network in the intestinal cells of C. elegans
The protein encoded by this gene is a major component of the inner surface of caveolae, small invaginations of the plasma membrane, and is involved in essential cellular functions, including signal transduction, lipid metabolism, cellular growth control and apoptosis. This protein may function as a tumor suppressor. This gene and related family member (CAV1) are located next to each other on chromosome 7, and express colocalizing proteins that form a stable hetero-oligomeric complex. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene. Additional isoforms resulting from the use of alternate in-frame translation initiation codons have also been described, and shown to have preferential localization in the cell (PMID:11238462).
, caveolin 2
, caveolae protein, 20-kD
, caveolin 2 isoform a and b