Catalog # SP5601


αII-Spectrin (a.a. 1171-1176), cleavage-specific

Rabbit Polyclonal

Application Dilution
ELISA1:1000
WB1:1000

Size 100 μl

Species Reactivity Hu, Rt, Ms

MW 136 kDa

$295

Spectrins are central components of the cytoskeleton that form a scaffold below the plasma membrane. Spectrins contain two subunits, α and β, which intertwine to form heterodimers that can self associate into elongated tetramers. α-spectrin I and β-spectrin I form heterodimers in red blood cells, while nonerythroid mammalian cells contain heterodimers of α-spectrin I and II with β-spectrin I to V. The structure of spectrins includes a succession of triple-helical repeats along with various domains, such as SH3 domain, EF hands, PH domains, and binding domains for ankyrin, actin, band 4.1, and calmodulin. α-spectrin II is a widely expressed non-erythroid spectrin that contains an SH3 domain, a calmodulin binding site, and two cleavage sites, one at Tyr-1176 for calpains and one at Asp-1185 for caspase-3. α-spectrin II and β-spectrin II, like many other spectrins, can form heterodimers that can self associate into tetramers, as well as interact with Band 4.1, F-actin, and other proteins near the plasma membrane.

 

References

Higuchi, M. et al. (2005) J Biol Chem. 280:15229.
Manya, H. et al. (2002) J Biol Chem. 277(38):35503.
Robert-Lewis, J.M. et al. (1994) J Neurosci. 14(6):3934.

A synthetic peptide (coupled to KLH) corresponding to amino acid residues 1171 to 1176 in human αII-spectrin. This sequence has high homology with similar regions in rat and mouse αII-spectrin, but is not found in other spectrin family members.

*For more information, see UniProt Accession Q13813
Rabbit polyclonal, affinity-purified antibody is supplied in 100μl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.

The products are are safely shipped at ambient temperature for both domestic and international shipments. Each product is guaranteed to match the specifications as indicated on the corresponding technical data sheet. Please store at -20C upon arrival for long term storage.

This antibody was affinity purified using αII-spectrin (a.a. 1171-1176) peptide (without carrier). The antibody detects a 136 kDa* cleaved fragment corresponding to αII-Spectrin on SDS-PAGE immunoblots of mouse diaphram treated with thapsigargin. The antibody only detects cleaved αII-Spectrin and does not detect full length αII-Spectrin.

*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.

Western blot analysis of adult mouse diaphram treated with thapsigargin for 0, 6, 12, or 24 hours to induce cleavage of αII-spectrin from 250 kDa to 136 kDa. The blot was probed with rabbit polyclonal αII-spectrin (a.a. 1171-1176) cleavage-specific antibody at a dilution of 1:1,000 (Image provided by Dr. Leigh Ann Callahan, Department of Internal Medicine, University of Kentucky.)



This kit contains:

KIT SUMMARY