Product Pathways - Apoptosis
Cleaved α-Fodrin (Asp1185) Antibody #2121
Reactivity Key: H=Human
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
Cleaved alpha-Fodrin (Asp1185) Antibody detects endogenous levels of the large fragment of alpha-fodrin resulting from cleavage at aspartic acid 1185. The antibody does not recognize full length alpha-fodrin.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to amino-terminal residues surrounding Asp1185 in human alpha-fodrin. Antibodies are purified by protein A and peptide affinity chromatography.
Fodrin (also named nonerythroid spectrin) is a universally expressed membrane-associated cytoskeletal protein consisting of alpha- and beta-subunits (1). This protein is important for maintaining normal membrane structure and supporting cell surface protein function (1). Alpha-fodrin is one of the primary targets cleaved by caspases during apoptosis. The full length 240 kDa protein can be cleaved at several sites within its sequence by activated caspases to yield amino-terminal 150 kDa, carboxy-terminal 120 kDa and 35 kDa major products (2-5). Cleavage of alpha-fodrin leads to membrane malfunction and cell shrinkage.
- Bennett, V. and Gilligan, D.M. (1993) Annu. Rev. Cell Biol. 9, 27-66.
- Vanags, D. M. et al. (1996) J. Biol. Chem. 271, 31075-31085.
- Cryns, V. L. et al. (1996) J. Biol. Chem. 271, 31277-31282.
- Wang, K. K. et al. (1998) J. Biol. Chem. 273, 22490-22497.
- Janicke, R. U. et al. (1998) J. Biol. Chem. 273, 15540-15545.
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For Research Use Only. Not For Use In Diagnostic Procedures.