Clone REA537 recognizes the human Wiskott-Aldrich syndrome protein-interacting protein (WIP) antigen phosphorylated at serine 488 (pS488). WIP is a multifunctional adaptor implicated in a wide range of cellular functions, including cell adhesion, migration and chemotaxis, T cell activation and proliferation, and intracellular pathogen motility. WIP functions through binding to both globular and filamentous actin and several regulators of actin dynamics. WIP can also bind to and regulate the function of the actin-nucleation-promoting factor cortactin. In cells of haematopoietic origin, WIP is an important regulator of Wiskott-Aldrich syndrome protein (WASP), the expression of which is restricted to cells of this lineage. WASP is indispensable for normal leukocyte function and its importance is highlighted in the congenital disorder Wiskott–Aldrich syndrome in which missense mutations in the WAS gene result in severe immunodeficiency. Phosphorylation represents a strong candidate for regulation of WIP function, as studies have reported serine/threonine phosphorylation of WIP on a number of residues. S488 has been reported to be phosphorylated in a PKCθ-dependent manner in response to T cell receptor activation.

Additional information: Clone REA537 displays negligible binding to Fc receptors.

Alternative names

WIPF1, PRPL-2, WAS2, WASPIP, WIP

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