bsm-70321M

DATASHEET

Host: Mouse

Target Protein: β-Actin

Specificity: Clone M008 detects a 42 kDa* protein corresponding to the molecular mass of β-actin on SDS-PAGE immunoblots of human cancer cell lines, as well as human recombinant β-actin. This actin antibody preferentially detects human β-actin with only weak reactivity toward actins in rat, mouse, or rabbit.

Clonality: Monoclonal

Isotype: IgG2b

Swiss Prot: P60709

Source: Clone M008 was generated from a proprietary antigen related to human β-actin in MDA-MB-231 breast cancer cell line.

Purification: Purified by Protein G.

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