Anti-N-WASP 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. Serine and tyrosine phosphorylation regulates the activity of both proteins. WASP is observed as a 63 kDa protein in hematopoietic cells, while N-WASP is observed as a 65 kDa in many tissues, especially brain.

Our N-WASP rabbit polyclonal primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat N-WASP and is antigen affinity purified. It is great for use in WB.

N-WASP synthetic peptide (coupled to KLH) corresponding to amino acid residues in the N-terminal region of human N-WASP. This N-WASP peptide sequence is 100% homologous to rat and mouse N-WASP, and has low homology to the corresponding region in the human WASP.

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 detects a 65 kDa* protein corresponding to the molecular mass of N-WASP on SDS-PAGE immunoblots of neonatal rat brain lysate. It is also detects 65 kDa* proteins in A431, human endothelial, and SKN-SH cells. It does not recognize the 63 kDa* WASP protein in Jurkat cell lysate.