Annexin V Antibody #8555
- WB
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 30 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
Annexin V Antibody recognizes endogenous levels of total annexin V protein. This antibody is not predicted to cross-react with other annexin family members.
Species Reactivity:
Human, Mouse, Rat, Monkey
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human annexin V protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Annexin V, also known as PAP-1 or Lipocortin V, is an ~30 kDa protein that binds to phospholipids in a calcium-dependent manner (1). All annexins contain a putative PKC binding site, but only annexin V has been identified as an inhibitor of this pathway (2). Via direct interaction with VEGFR-2 receptor, annexin V may also signal to regulate vascular endothelial cell proliferation (3). Annexin V preferentially binds phosphatidylserine in competition with prothrombin, leading to inhibition of blood coagulation at sites of injury preceding contact between lipid components and coagulation factors that initiate thrombosis (4-6). The ability of annexin V to bind specifically and robustly to phosphatidylserine makes it an attractive reagent in detecting apoptotic cells (7). Annexin V is inducible by glucocorticoids and can be phosphorylated by tyrosine and serine/threonine kinases (8). It is thought to block the production of inflammation mediators, such as prostaglandins and leukotrienes by inhibiting the release of arachidonic acid from membranes by phospholipase A2 (8).
- Huber, R. et al. (1990) EMBO J 9, 3867-74.
- Cardó-Vila, M. et al. (2003) Mol Cell 11, 1151-62.
- Wen, Y. et al. (1999) Biochem Biophys Res Commun 258, 713-21.
- Koopman, G. et al. (1994) Blood 84, 1415-20.
- London, F. et al. (1996) Biochemistry 35, 16886-97.
- Thiagarajan, P. and Benedict, C.R. (1997) Circulation 96, 2339-47.
- Vermes, I. et al. (1995) J Immunol Methods 184, 39-51.
- Grundmann, U. et al. (1988) Proc Natl Acad Sci USA 85, 3708-12.
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