Actin (Tyr-53), phospho-specific polyclonal, anti-human, mouse, rat, chicken

Background:
Actin is a major cytoskeletal protein involved in diverse cellular functions including cell motility, adhesion, and morphology. Six different actin isoforms have been identified in vertebrates. There are four α isoforms: skeletal, cardiac, and two smooth muscle (enteric and aortic) actins, along with two cytoplasmic actins (β and γ). Actin exists in two principal forms, globular, monomeric (G) actin, and filamentous polymeric (F) actin. The assembly and disassembly of actin filaments, and also their organization into functional networks, is regulated by a variety of actin-binding proteins (ABPs). Phosphorylation may also be important for regulating actin assembly and interaction with ABPs. In Dictyostelium, phosphorylation of Tyr-53 occurs in response to cell stress and this phosphorylation may alter actin polymerization. In B cells, SHP-1 tyrosine dephosphorylation of actin leads to actin filament depolymerization following BCR stimulation.

Immunogen: Phospho-Actin (Tyr-53) synthetic peptide (coupled to KLH) corresponding to amino acid residues around tyrosine 53 of human β actin. This sequence is identical to similar regions in all four α actins, as well as in γ actin, and is well conserved in actins from most eukaryotic species.

Specificity: This antibody detects a 42 kDa* protein corresponding to the molecular mass of Actin on SDS-PAGE immunoblots of pervanadate treated human C2C12 and SYF cSrc transformed cells, but not in control cells. In addition, this antibody either detects actin cleavage products at 36 and 20 kDa, or cross-reacts with unidentified proteins at these molecular weights in C2C12 cells.

Buffer/Storage:
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.