Anti-N-WASP (Ser-484/Ser-485), Phosphospecific Antibody

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

Our N-WASP (Ser-484/Ser-485) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat N-WASP (Ser-484/Ser-485) and is antigen affinity purified. It is great for use in WB, ICC.

Phospho-N-WASP (S484/S485) synthetic peptide (coupled to KLH) corresponding to amino acid residues around serine 484 and 485 of human N-WASP. The human WASP sequence has a similar peptide sequence surrounding serine 483 and 484.

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.

This antibody was cross-adsorbed to unphosphorylated-N-WASP (S484/S485) peptide then affinity purified 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. In rat brain, A431, human endothelial and SKN-SH cells, this antibody detects a 65 kDa* protein corresponding to phosphorylated N-WASP.