Cleaved-Spectrin α II (D1185) polyclonal antibody

Fodrin (also named nonerythroid 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-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. Cleavage of alpha-fodrin leads to membrane malfunction and cell shrinkage.

Rho GTPase-activating protein 17; Rho-type GTPase-activating protein 17; RhoGAP interacting with CIP4 homologs protein 1; RICH-1; ARHGAP17; RICH1; MSTP066; MSTP110

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Western blot (WB) analysis of Cleaved-Spectrin α II (D1185) pAb at 1:500 dilution Lane1:Hela whole cell lysate (40ug) Lane2:A549 whole cell lysate (40ug) Lane3:Panc1 whole cell lysate (40ug) Lane4:PC12 whole cell lysate (40ug) Lane5:CT26 whole cell lysate (40ug)