Recombinant Human PSAT1 His-tag Protein, CF

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Phosphoserine aminotransferase (PSAT1), a pyridoxal-phosphate (PLP)-dependent cytosolic protein catalyzes the conversion of 3-phosphohydroxypyruvate into phosphoserine; the reversible second step in the de novo serine synthesis pathway. PSAT1 forms an active a/b domain structure homodimer where each monomer is 40 kDa and 370 amino acids (1). PSAT1 contains a catalytic lysine and bound PLP in the active site. Although serine is considered a nonessential amino acid, de novo synthesis is essential in the brain due to insufficient delivery through the blood brain barrier. PSAT1 expression is concentrated in brain, liver, kidney, and pancreas suggesting these tissues are primary sites for de novo serine synthesis (2). Mutations in PSAT1 can cause Neu-Laxova syndrome, a serine-deficiency disorder (3). PSAT1 has been reported to signal through the GSK3beta/beta-catenin pathway (4, 5), regulate alpha keto-glutarate in a role essential for embryonic stem cell self-renewal and pluripotency (6) and promote migratory metastasis and proliferation in roles independent of serine synthesis (7,8). PSAT1 is up-regulated and associated with poor prognosis in several cancers including nasopharyngeal (9), breast (10), and esophageal squamous carcinoma (11). PSAT1 has been proposed as a promising target for tumor suppression in colorectal, esophageal, and breast cancers (8, 12, 13). It has been proposed as a target in brain tumors through a novel stabilization mechanism (14) and for inhibition of the serine production pathway in tuberculosis (15).

Array 10342-PS

• PSAT1 Antibodies
• PSAT1 Lysate
• PSAT1 Proteins
• PSAT1 Proteins and Enzyme