bs-70719R

DATASHEET

Host: Rabbit

Target Protein: Vav3

Specificity: The antibody detects a 98 kDa* protein corresponding to the molecular mass of Vav3 on SDS-PAGE immunoblots of human Jurkat cells. The antibody also strongly detects an unidentified protein at 120 kDa in Jurkat and K562. This sequence has high homology with similar regions in rat and mouse Vav3, and has low homology to other Vav family members.

Clonality: Polyclonal

Isotype: IgG

Swiss Prot: Q9UKW4

Source: A synthetic peptide (coupled to KLH) corresponding to amino acid residues in the Dbl homology domain of human Vav3.

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:

The Vav family of Rho-guanine nucleotide exchange factors, Vav1, Vav2, and Vav3, have central roles in transducing signals from cell surface receptors, such as integrin, growth factor and immune cell receptors to the cytoskeleton. This role includes receptor-mediated changes in the actin cytoskeleton and cell motility. Vav1 expression is normally restricted to hematopoietic cells, while Vav2 and Vav3 are more widely expressed. All three Vav isoforms have been shown to be abnormally expressed in several types of cancer. Vavs are composed of multiple domains, including a Dbl homology domain, a calponin homology domain, an acidic amino acid region, a pleckstrin homology domain, a cysteine-rich domain, and SH3 and SH2 domains. Vav activity is regulated by the phosphorylation status of several conserved tyrosine residues in the acidic region (In Vav2: Tyr-142, Tyr-159, and Tyr-172). These tyrosine residues are able to participate in autoinhibitory interactions with the Dbl homology domain and this interaction is prevented after phosphorylation of these sites leading to activation of Vav GEF activity.