bs-70693R

DATASHEET

Host: Rabbit

Target Protein: Talin (Ser-425)

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 treated with Calyculin A, but is not observed after lambda phosphatase treatment. This sequence is conserved in rat, mouse, and chicken Talin 1, as well as in Talin 2 (Ser-428).

Modification Site: Ser-425

Clonality: Polyclonal

Isotype: IgG

Swiss Prot: Q9Y490

Source: Phospho-Talin (Ser-425) synthetic peptide (coupled to carrier protein) corresponding to amino acids surrounding Ser-425 in human Talin 1.

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:

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