Anti-Human WASL Antibody Pair

Product Description: WASP like actin nucleation promoting factor (WASL), also known as Neural Wiskott-Aldrich Syndrome Protein (N-WASP), is a member of the WASP family that regulates actin cytoskeleton dynamics by activating the Arp2/3 complex, facilitating actin polymerization. Structurally, WASL contains a WASP homology 1 (WH1) domain for binding partners, a basic region (BR), a GTPase-binding domain (GBD), a proline-rich region, and a verprolin-cofilin-acidic (VCA) domain critical for Arp2/3 activation. It integrates signals from Cdc42, phosphoinositides, and SH3 domain-containing proteins to coordinate actin remodeling during processes like endocytosis, cell motility, and neuronal development. Dysregulation of WASL is linked to neurodevelopmental disorders and cancer. Mutations in WASL are associated with X-linked intellectual disability (XLID) and developmental delay, attributed to impaired synaptic plasticity and neurite outgrowth. Additionally, WASL overexpression promotes cancer metastasis by enhancing invasive cell migration. Protein Function: Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex (PubMed:16767080, PubMed:19366662, PubMed:19487689, PubMed:22847007, PubMed:22921828, PubMed:9422512). Involved in various processes, such as mitosis and cytokinesis, via its role in the regulation of actin polymerization (PubMed:19366662, PubMed:19487689, PubMed:22847007, PubMed:22921828, PubMed:9422512). Together with CDC42, involved in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia (PubMed:9422512). In addition to its role in the cytoplasm, also plays a role in the nucleus by regulating gene transcription, probably by promoting nuclear actin polymerization (PubMed:16767080). Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression (By similarity). Plays a role in dendrite spine morphogenesis (By similarity). Decreasing levels of DNMBP (using antisense RNA) alters apical junction morphology in cultured enterocytes, junctions curve instead of being nearly linear (PubMed:19767742) [The Uniprot Consortium]