PHGDH Protein, Human, Recombinant (His)

Catalog No. TMPY-02801

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.

PHGDH Protein, Human, Recombinant (His)

Catalog No. TMPY-02801

Pack Size	Price	Availability
5 μg	$52	In Stock
10 μg	$82	In Stock
20 μg	$132	In Stock
50 μg	$256	7-10 days
100 μg	$428	In Stock
200 μg	$731	7-10 days
500 μg	$1,480	7-10 days

Bulk & Custom

Add to Cart

All TargetMol products are for research purposes only and cannot be used for human consumption. We do not provide products or services to individuals. Please comply with the intended use and do not use TargetMol products for any other purpose.

Questions

Select Batch

Resource Download

COA User Guide of Recombinant Proteins

Product Information

Biological Activity	Activity testing is in progress. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.
Description	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.
Species	Human
Expression System	E. coli
Tag	C-His
Accession Number	O43175
Synonyms	SERA,phosphoglycerate dehydrogenase,PHGDHD,PGDH,PGD,PGAD,PDG,NLS1,NLS,HEL-S-113,3-PGDH,3PGDH
Construction	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. Predicted N terminal: Met
Protein Purity	> 90 % as determined by SDS-PAGE
Molecular Weight	58kDa (predicted); 55 kDa (reducing conditions)
Endotoxin	Please contact us for more information.
Formulation	Supplied as sterile PBS, 100 mM Arg, 0.1% Tween20, 20% glycerol, pH 8.0.
Reconstitution	A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.
Stability & Storage	It is recommended to store the product under sterile conditions at -20°C to -80°C. Samples are stable for up to 12 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
Shipping	Shipping with blue ice.
Research Background	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.