Technical Data
Spectrin, alpha, Cleavage Site (Asp1185) (Spectrin Non-erythroid alpha Chain, Alpha Fodrin, Alpha II Spectrin, FLJ44613, Spectrin alpha Non-erythrocytic 1, SPTAN1, SPTA2)
Spectrin is a universally expressed membrane-associated cytoskeletal protein consisting of alpha-and beta-subunits. This protein is important for maintaining normal membrane structure and supporting cell surface protein function. Alpha-spectrin is one of the primary targets cleaved by caspases during apoptosis. The full length 240kD protein can be cleaved at several sites within its sequence by activated caspases, to yield Nterminal 150kD, C-terminal 120kD and 35kD major products. Cleavage of alpha-fodrin leads to membrane malfunction and cell shrinkage.

Suitable for use in ELISA and Western Blot. Other applications not tested.

Recommended Dilutions:
Western Blot: 1:1000
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
PabIgGAffinity Purified
100ul-20CBlue IceHumanRabbit
Not Determined
Synthetic peptide corresponding to amino-terminal residues surronding Asp1185 from human Spectrin, alpha conjugated to KLH.
Purified by Protein A and peptide affinity chromatography.
Supplied as liquid in 10mM sodium HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, 50% glycerol.
Recognizes endogenous levels of the large fragment of human Spectrin, alpha resulting from cleavage at aspartic acid 1185. Does not recognize full length Spectrin, alpha.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Bennett, B. and Gilligan, D.M. (1993) Annu. Rev. Cell Biol. 9, 27-66. 2. Vanags, D.M. et al. (1996) J. Biol. Chem. 271, 31075-31085. 3. Cryns, V.L. et al. (1996) J. Biol. Chem. 271, 1277-31282. 4. Wang, K.K. et al. (1998) J. Biol. Chem. 273, 22490-22497. 5. Janicke, R.U. et al. (1998) J. Biol. Chem. 273, 15540-15545.