Cell Signaling Technology

Product Pathways - Ca / cAMP / Lipid Signaling

Annexin A1 (D16A10) Rabbit mAb #8691

Applications Reactivity Sensitivity MW (kDa) Isotype
W H M Mk Pg Endogenous 38 Rabbit IgG

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  Mk=Monkey  Pg=Pig
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Annexin A1 (D16A10) Rabbit mAb recognizes endogenous levels of total annexin A1 protein. This antibody does not cross-react with other members of the annexin family.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val236 of human annexin A1 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using Annexin A1 (D16A10) Rabbit mAb.

Background

The annexin superfamily consists of 13 calcium or calcium and phospholipid binding proteins with high biological and structural homology (1). Annexin-1 (ANXA1) is the first characterized member of the annexin family of proteins and is able to bind to cellular membranes in a calcium-dependent manner, promoting membrane fusion and endocytosis (2-4). Annexin A1 has anti-inflammatory properties and inhibits phospholipase A2 activity (5,6). Annexin A1 can accumulate on internalized vesicles after EGF-stimulated endocytosis and may be required for a late stage in inward vesiculation (7). Phosphorylation by PKC, EGFR, and Chak1 results in inhibition of annexin A1 function (8-10). Annexin A1 has also been identified as one of the 'eat-me' signals on apoptotic cells that are to be recognized and ingested by phagocytes (11). Annexin A1, as an endogenous anti-inflammatory mediator, has roles in many diverse cellular functions, such as membrane aggregation, inflammation, phagocytosis, proliferation, apoptosis, and tumorigenesis and cancer development (12-14).

  1. Raynal, P. and Pollard, H.B. (1994) Biochim Biophys Acta 1197, 63-93.
  2. Blackwell, G.J. et al. (1980) Nature 287, 147-9.
  3. Rothhut, B. et al. (1983) Biochem Biophys Res Commun 117, 878-84.
  4. Hirata, F. et al. (1981) Proc Natl Acad Sci USA 78, 3190-4.
  5. Kim, K.M. et al. (1994) FEBS Lett 343, 251-5.
  6. Kim, S.W. et al. (2001) J Biol Chem 276, 15712-9.
  7. White, I.J. et al. (2006) EMBO J 25, 1-12.
  8. Varticovski, L. et al. (1988) Biochemistry 27, 3682-90.
  9. Dorovkov, M.V. and Ryazanov, A.G. (2004) J Biol Chem 279, 50643-6.
  10. Wang, W. and Creutz, C.E. (1994) Biochemistry 33, 275-82.
  11. Arur, S. et al. (2003) Dev Cell 4, 587-98.
  12. Perretti, M. and Gavins, F.N. (2003) News Physiol Sci 18, 60-4.
  13. Parente, L. and Solito, E. (2004) Inflamm Res 53, 125-32.
  14. Lim, L.H. and Pervaiz, S. (2007) FASEB J 21, 968-75.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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