bs-70320R

DATASHEET

Host: Rabbit

Target Protein: Actin (Tyr-53)

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.

Modification Site: Tyr-53

Clonality: Polyclonal

Isotype: IgG

Swiss Prot: P60709

Source: Phospho-Actin (Tyr-53) synthetic peptide (coupled to KLH) corresponding to amino acid residues around tyrosine 53 of human β actin.

Purification: Antigen Affinity purification

Storage Buffer: PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol

Storage: 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.

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.