Human PGDH/PHGDH (His Tag) recombinant protein

Human PGDH/PHGDH (His Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

PHGDH is a member of the D-isomer specific 2-hydroxyacid dehydrogenase family. This new family consists of D-isomer-stereospecific enzymes. The conserved residues in this family appear to be the residues involved in the substrate binding and the catalytic reaction, and thus to be targets for site-directed mutagenesis. A number of NAD-dependent 2-hydroxyacid dehydrogenases which seem to be specific for the D-isomer of their substrate have been shown to be functionally and structurally related. PHGDH catalyzes the transition of 3-phosphoglycerate into 3-phosphohydroxypyruvate, which is the first and rate-limiting step in the phosphorylated pathway of serine biosynthesis, using NAD+/NADH as a cofactor. Overexpression of PHGDH may cause certain breast cancers. Defects in PHGDH are the cause of phosphoglycerate dehydrogenase deficiency which is characterized by congenital microcephaly, psychomotor retardation, and seizures.

D-3-phosphoglycerate dehydrogenase

RP4-683H9.1; NLS; PDG; HEL-S-113; 3-PHOSPHOGLYCERATE DEHYROGENASE; A10; SERA; NLS1; 4930479N23; PGAD; 3PGDH; 3-PHOSPHOGLYCERATE DEHYDROGENASE; 3-PGDH; PGDH; PGD; D-3-PHOSPHOGLYCERATE DEHYDROGENASE; PHGDHD

O43175

PHGDH; PGDH3

E. coli

A DNA sequence encoding the mature form of human PHGDH (O43175) (Met 1-Phe 533) was fused with a polyhistidine tag at the C-terminus and an initial Met at the N-terminus.

Human

The recombinant human PHGDH comprises 543 amino acids and has a calculated molecular mass of 58KDa. It migrates as an approximately 55 kDa band in SDS-PAGE under reducing conditions.

> 90 % as determined by SDS-PAGE