Non-erythroid Spectrin, also known as Fodrin, plays a role in stabilizing membrane structures, maintaining cell shape and linking the cytoskeleton to plasma membranes or intracellular vesicles. As one of the primary targets cleaved by activated caspases during apoptosis, the full-length ~240 kDa protein can be cleaved to yield an N-terminal product of ~150 kDa, and C-terminal products of ~120 and ~35 kDa.
Specific for the 240, 150, and 120 kDa forms of alpha-spectrin/alpha-fodrin molecule of all mammalian nonerythroid cells and chicken alpha-spectrin.
Wide-mammalian reactivity is expected.
Chicken red blood cell membranes purified by hypotonic lysis and mechanical enucleation.
A 1:200-1:400 dilution of a previous lot was used in immunohistochemistry.
Does not work on paraffin sections.
Optimal working dilutions must be determined by end user.
A previous lot of this antibody was used to immunoprecipitate Spectrin Alpha from chromatin-associated protein extracts derived from normal human, HeLa, FA-A, and transduced FA-A cells (McMahon, L.W., et al. (1999). J. Biological Chem. 274:32904-32908).
Anti-Spectrin alpha chain (nonerythroid) Antibody, clone AA6 is an antibody against Spectrin alpha chain (nonerythroid) for use in IH, IP, WB, ChIP.
Research Sub Category
Evaluated by Western Blot on staurosporine-treated HeLa lysates.
Western Blot Analysis:
1:500 dilution of this antibody detected N-, C- terminal Spectrin alpha/Fodrin alpha on 10 μg of staurosporine treated HeLa lysates.
~240 kDa full length product, ~150 kDa N-terminal cleaved product and ~120 kDa C-terminal product may be seen in varing amounts in lysates, depending on condition. The smaller sizes represent break down products seen during apoptosis.
Purified mouse monoclonal IgG1 in buffer containing PBS with 1% BSA and 0.09% sodium azide.
Protein A purified
Storage and Stability
Stable for 12 months at 2-8°C from date of receipt.
HeLa cells treated with staurosporine
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
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