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.
Feinberg, J.M. et al. (1991) J Histochem. & Cytochem. 39:955.
Zokas, L. & Glenney, J.R. (1987) J Cell Biol. 105:2111.
*For more information, see UniProt Accession P48037
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
This kit contains: