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Caveolin-2 Antibody Phospho (pY27)Rabbit Monoclonal Antibody
| Country | United States
Ordering Information
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| Catalog # | Size | Availability | Price | |
| AJ1141b | 100ul 400 ul | 2-3 days | $ 355.00 | DISCONTINED INQUIRE CLICK INQUIRE Add to cart |
- Specification
- Citiations : 0
- Reviews
- Protocols
- Backgrounds
Caveolin-2 Antibody Phospho (pY27) - Product info | |
| Application | WB
|
| Primary Accession | P51636 |
| Reactivity | Human |
| Clone Names | EP2221Y |
| Calculated MW | 18291 Da |
| Gene ID 858 | |
| Other Names CAV2, Caveolin-2 | |
| Target/Specificity A phospho specific peptide corresponding to residues surrounding tyrosine 27 of human Caveolin2. This antibody detects Caveloin2 phosphorylated at tyrosine 27. | |
| Dilution WB~~1:1000 | |
| Format 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA. | |
| Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. | |
| Precautions Caveolin-2 Antibody Phospho (pY27) is for research use only and not for use in diagnostic or therapeutic procedures. | |
Caveolin-2 Antibody Phospho (pY27) - Protein Information | |
| Name CAV2 | |
| Function May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity) | |
| Cellular Location Nucleus. Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at sites of cell-cell contact and is translocated to the nucleus in complex with MAPK1 in response to insulin (By similarity). Tyr-27- phosphorylated form is located both in the cytoplasm and plasma membrane. CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. Ser-36-phosphorylated form resides in intracellular compartments | |
| Tissue Location Expressed in endothelial cells, smooth muscle cells, skeletal myoblasts and fibroblasts | |
Caveolin-2 Antibody Phospho (pY27) - Related products
AP8645a: CAV2 Antibody (N-term)
AP8645c: CAV2 Antibody (Center)
LY11277a: CAV2 Over-expression Lysate
BP8645a: CAV2 Antibody (N-term) Blocking Peptide
Caveolin-2 Antibody Phospho (pY27) - Application data
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A. Western blot analysis on HeLa cell lysates using anti-Phospho-Caveolin2 (pY27) RabMAb (Cat. #AJ1141b), 1:2000 dilution. Cells were either (A) untreated (B) treated with pervanadate.
Caveolin-2 Antibody Phospho (pY27) - Research Areas
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BACKGROUND
Caveolae are cholesterol/sphingolipid-rich microdomains of the plasma membrane that have been implicated in signal transduction and vesicular trafficking. Caveolins are a family of caveolae-associated integral membrane proteins (1). Caveolin, a 21- to 24-kDa integral membrane protein, is a principal component of caveolae membranes. Caveolin interacts directly with heterotrimeric guanine nucleotide binding proteins (G proteins) and can functionally regulate their activity. Caveolins 1 and 2 are similar in most respects, however, caveolin-1 and caveolin-2 differ in their functional interactions with heterotrimeric G proteins, possibly explaining why caveolin-1 and -2 are coexpressed within a single cell (2). Caveolin-2 is up-regulated in response to the mechanical injury of differentiated PC12 cells; up-regulation of caveolin-2 under these conditions is strictly dependent on continued treatment with NGF. Robust expression of caveolin-1 and -2 is also observed along the entire cell surface of DRG neurons, including high levels on growth cones. These findings demonstrate that neuronal cells express caveolins (1).
REFERENCES
1. Galbiati F, et al. Proc Natl Acad Sci USA 95(17):10257-62, 1998.
2. Scherer PE, et al. Proc Natl Acad Sci 93(1): 131-5, 1996
