Phospho-SSH3 (Ser37) Antibody recognizes endogenous levels of SSH3 protein only when phosphorylated at Ser37.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser37 of human SSH3 protein. Antibodies are purified by protein A and peptide affinity chromatography.
原厂资料:
Specificity / Sensitivity
Phospho-SSH3 (Ser37) Antibody recognizes endogenous levels of SSH3 protein only when phosphorylated at Ser37.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser37 of human SSH3 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Slingshot homolog 3 (SSH3) is a protein phosphatase that modifies actin cytoskeleton dynamics via cofilin dephosphorylation. Cofilin is an evolutionarily conserved, actin-binding protein that severs actin filaments during processes that rely on actin filament dynamics, including cytokinesis, cell migration, invasion, and neuronal development. Actin severing and filament depolymerization are regulated through the controlled cycling of cofilin between the phosphorylated and dephosphorylated forms (1). The kinases LIMK and TESK inactivate cofilin by phosphorylating it at Ser3 (2,3). The slingshot homologs (SSH1, SSH2, and, to a lesser extent, SSH3) and chronophin/PDXP phosphatases remove phosphate from cofilin at Ser3, enabling cofilin binding to actin and filament depolymerization (3). SSH3 is widely expressed in epithelial tissues, and has been found to be non-essential for viability and fertility in knockout mice (4). While its biological function remains elusive, phosphorylation at Ser37 of SSH3 has been identified in several phosphoproteomic studies (5-7).