Rabbit Polyclonal Caveolin-1 phospho Y14 antibody. Suitable for WB and reacts with Mouse samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Human CAV1 phospho Y14.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.87% Sodium chloride
WB | |
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Mouse | Tested |
Species | Dilution info | Notes |
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Species Mouse | Dilution info 1/500 - 1/1000 | Notes - |
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May act as a scaffolding protein within caveolar membranes (PubMed:11751885). Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae (PubMed:19262564). Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (PubMed:17287217). Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway (By similarity). Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation (PubMed:25893292). Binds 20(S)-hydroxycholesterol (20(S)-OHC) (By similarity).
CAV, CAV1, Caveolin-1
Rabbit Polyclonal Caveolin-1 phospho Y14 antibody. Suitable for WB and reacts with Mouse samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Human CAV1 phospho Y14.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.87% Sodium chloride
The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
Caveolin-1 also known as Cav-1 is an integral membrane protein with a molecular weight of approximately 22 kDa. It functions mechanically as a scaffolding protein in caveolae which are tiny invaginations in the plasma membrane of many cell types. These structures are particularly abundant in adipocytes endothelial cells and muscle cells. Caveolin-1 anchors itself to the cell membrane and plays a role in organizing and concentrating certain signaling molecules.
Caveolae provide a platform for various signaling pathways and involve caveolin-1 as a major component. Caveolin-1 interacts with multiple signaling molecules such as G-protein coupled receptors and Src family kinases to modulate signal transduction. This protein forms part of a larger caveolar complex contributing to cellular processes including endocytosis and lipid regulation. Its presence as a marker in caveolae highlights its significance in cellular functions.
Caveolin-1 influences the insulin signaling and nitric oxide (NO) signaling pathways. In the insulin signaling pathway caveolin-1 interacts with insulin receptors to modulate glucose uptake. It also associates with eNOS (endothelial nitric oxide synthase) in the NO signaling pathway impacting vascular function. These relationships highlight its role in cellular communication and regulatory mechanisms within the human body.
Caveolin-1 is involved in cancer and cardiovascular diseases. In cancer altered expression of caveolin-1 contributes to tumor progression while in cardiovascular diseases it affects endothelial function through its interaction with eNOS. The connection of caveolin-1 to proteins like insulin receptors and eNOS reveals its critical influence in these conditions providing potential targets for therapeutic intervention.
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Caveolin-1 (phospho Y14) Western blot staining using rabbit Anti-Caveolin-1 (phospho Y14) antibody
Lanes 1 - 2: Caveolin-1 Antibody
Lanes 3 - 4: Western blot - Anti-Caveolin-1 (phospho Y14) antibody - Caveolae Marker (ab38468) at 1/500 dilution
Lane 1: NIH 3T3 cell extract
Lane 2: NIH 3T3 cell extract. Pre-incubated with synthesized peptide
Lane 3: NIH 3T3 cell extract.
Lane 4: NIH 3T3 cell extract. Treated with H2O2.
Predicted band size: 20 kDa
Observed band size: 20 kDa
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