bsm-70692M

DATASHEET

Host: Mouse

Target Protein: Talin (Rod domain)

Specificity: The antibody detects a 240 kDa* protein corresponding to the molecular mass of Talin on SDS-PAGE immunoblots of human A431, rat PC12, and rabbit fibroblast cells.

Clonality: Monoclonal

Isotype: IgG1

Swiss Prot: P54939

Source: Clone 8D4 was generated from purified chicken gizzard talin. The antibody recognizes an epitope within the rod domain of talin from many species, including human, rat, mouse, chicken, and frog.

Purification: Purified by Protein A.

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:

Talin is an important cytoskeletal component of integrin adhesion sites. Calpins cleave talin precursor (240 kDa) into an amino-terminal globular head domain of 47 kDa and a carboxyl-terminal 190 kDa rod domain. The talin head domain contains a FERM domain that binds integrins, PIP kinase (Type I), and FAK. The rod domain has several vinculin-binding sites, a second integrin-binding site, and two actin-binding sites. These talin protein-protein interactions are critical for integrin activation, focal adhesion formation, and cell migration. Talin regulation may occur through phosphorylation and regulated degradation. The talin head domain binds Smurf1, an E3 ubiquitin ligase, and this interaction leads to talin head ubiquitylation and degradation. Cdk5 can phosphorylate Ser-425 in the head domain, and this inhibits both binding to Smurf1 and subsequent degradation. The S425A talin mutant resists Cdk5 phosphorylation, increases susceptibility to Smurf1-mediated ubiquitylation, and inhibits cell migration. Thus, talin head phosphorylation may be important for regulating adhesion stability and cell migration