The Annexin family of calcium-binding proteins is composed of al least thirteen mammalian genes (Annexin A1-13). These proteins are characterized by a conserved core domain which binds to phospholipids in a Ca2+-dependent manner and a unique amino terminal region which may confer binding specificity. The Annexin family has been implicated as regulators of such diverse processes as ion-flux, endocytosis and exocytosis, and cellular adhesion. Annexin A2 (calpactin I, chromobindin 8, p36, Lipocortin II, PAP-IV, or Protein I) is a cytoskeletal calcium-dependent phospholipid binding protein, which has been shown to be a mediator of cortocosteroid activity, a substrate for serine/threonine kinases and growth regulated tyrosine kinases, and may play a role in secretion. Annexin A6 reverses transformation of A431 cells after overexpression, and this effect may involve annexin A6 targeting of p120 RasGAP to the plasma membrane to inactivate Ras.
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blotmobilities of known proteins with similar MW.
Product References:
Moylan, J. et al. (2014) Redox biology 2:910. (WB: C2C12 myoblast)Gilliam, L.A. et al. (2011) AJP Lung Cell Mol Physiol. 300:L225. (IHC: mouse diaphragm)This kit contains:
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