αII-Spectrin , cleavage-specific Antibody

Applications

Reactivity

Human
Mouse
Rat

Overview
Catalog #	bs-70673r-100ul
Product Name	αII-Spectrin , cleavage-specific Antibody
Applications	WB
Specificity	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. This sequence has high homology with similar regions in rat and mouse αII-spectrin, but is not found in other spectrin family members.
Reactivity	Human, Mouse, Rat
Specifications
Conjugation	Unconjugated
Host	Rabbit
Source	A synthetic peptide (coupled to KLH) corresponding to amino acid residues around the calpain cleavage site, tyrosine 1176 in human αII-spectrin.
Clonality	Polyclonal
Isotype	IgG
Purification	Antigen Affinity purification
Storage Buffer	PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol
Storage Condition	Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
Target
Swiss Prot	Q13813
Synonyms	Alpha-II spectrin, Fodrin alpha chain, Spectrin, non-erythroid alpha subunit, SPTAN1, NEAS, SPTA2
Background	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.
Application Dilution
WB	1:300-5000