bs-70727R

DATASHEET

Host: Rabbit

Target Protein: N-WASP (Ser-484/Ser-485)

Specificity: This antibody was cross-adsorbed to unphosphorylated-N-WASP (S484/S485) peptide then Affinity purification using phospho-N-WASP (S484/S485) peptide. The antibody detects a 63 kDa* protein corresponding to the molecular mass of phosphorylated WASP on SDS-PAGE immunoblots of Jurkat cell lysate.

Modification Site: Ser-484/Ser-485

Clonality: Polyclonal

Isotype: IgG

Swiss Prot: O00401

Source: Phospho-N-WASP (S484/S485) synthetic peptide (coupled to KLH) corresponding to amino acid residues around serine 484 and 485 of human N-WASP.

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:

Members of the Wiskott-Aldrich sydrome protein (WASP) family regulate the formation of actin-based cell structures in many cell types. These proteins contain C-terminal actin-binding domains that can stimulate actin polymerization. In addition, these proteins bind the ARP2/3 complex, which can nucleate actin polymerization at sites that lead to branched actin structures. WASP is expressed primarily in hematopoietic cells, while its homolog N-WASP is widely expressed. These proteins have 48% identity in human with the highest homology in the functional regions of these proteins. Phosphorylation regulates the activity of both proteins. Dual phosphorylation of WASP on serine 483 and 484 by casein kinases increase the affinity for the ARP2/3 complex. Thus, dual serine phosphorylation may be important for formation of actin-based structures in various cell types