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Phosphoglycerate mutase 1 from Human, Recombinant

Cat No.
NATE-1647
Description
Phosphoglycerate mutase (PGM) is an enzyme that catalyzes step 8 of glycolysis. It catalyzes the internal transfer of a phosphate group from C-3 to C-2 which results in the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG) through a 2,3-bisphosphoglycerate intermediate. These enzymes are categorized into the two distinct classes of either cofactor-dependent (dPGM) or cofactor-independent (iPGM). The dPGM enzyme (EC 5.4.2.11) is composed of approximately 250 amino acids and is found in all vertebrates as well as in some invertebrates, fungi, and bacteria. The iPGM (EC 5.4.2.12) class is found in all plants and algae as well as in some invertebrate, fungi, and Gram-positive bacteria. This class of PGM enzyme shares the same superfamily as alkaline phosphatase.
Abbr
PGAM1, Recombinant (Human)
Source
E. coli and fused to His-tag at N-terminus
Species
Human
Form
Liquid
Enzyme Commission Number
EC 5.4.2.1
Activity
>300 units/mg
Molecular Weight
30.9 kDa
Purity
> 90% by SDS-PAGE
Concentration
1 mg/ml
Unit Definition
One unit will convert 1.0 umole of 3-phosphoglycerate to 2-phosphoglcerate per minute at pH 7.6 at 37°C.
Storage
Store at +4°C for short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freeze/thaw cycles.
Synonyms
Pgam-1; PGAM1
Formulation
0.5 mg/ml in 50 mM Tris, 100 mM NaCl, pH 8.0 and 20% glycerol
Catalog Product Name EC No. CAS No. Source Price
NATE-1643 Phosphoglycerate mutase 2 from Human, Recombinant EC 5.4.2.11 E. coli and fused to His-tag at N-terminus Inquiry
NATE-1646 Phosphoglycerate mutase 1 from Mouse, Recombinant EC 5.4.2.1 E. coli and fused to His-tag at N-terminus Inquiry
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