Anti-N-WASP Antibody, phospho-specific [Tyr256]

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. WASP is expressed primarily in hematopoietic cells, while its homolog N-WASP is widely expressed. These proteins have 48% identity in human with higher homology in the functional regions of these proteins. Phosphorylation at serine and tyrosine residues regulates the activity of both proteins. WASP is tyrosine phosphorylated at tyrosine 291 after antigen receptor activation in B-cells and collagen stimulation of platelets. Phosphorylation of the analogous site in N-WASP (Tyr256) stimulates its activity, reduces nuclear N-WASP, and is required for neurite extension.

Epitope: phosphotyrosine 256

Phospho-N-WASP (Tyr256) synthetic peptide (coupled to BSA) corresponding to amino acid residues around tyrosine 256 of human N-WASP. The human WASP sequence has a two amino acid difference in the same region surrounding tyrosine 291.

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Domaine de recherche
Signalisation

Sous-domaine de recherche
Signalisation du cytosquelette

Western blotting : 1:10,000 ELISA: 1:20,000

The antibody detects a 65 kDa protein corresponding to the molecular weight of phosphorylated N-WASP on SDS-PAGE Western blots of A431 cells treated with pervanadate. A similar band is observed in pervanadate treated HeLa and endothelial cells. Weak bands are also observed at higher molecular weights after pervanadate treatment. These bands may be due to low cross-reactivity with phosphotyrosine.

This antibody was cross-adsorbed to phosphotyrosine then affinity purified using phospho-N-WASP (Tyr256) peptide (without carrier). μ

° Do not aliquot.

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