Home  >  Products  >  PGAM2, Recombinant, Human, aa1-253, His-Tag (Phosphoglycerate Mutase 2, BPG-dependent PGAM 2, PGAM-M, Muscle-specific Phosphoglycerate Mutase, Phosphoglycerate Mutase Isozyme M, PGAMM)

PGAM2, Recombinant, Human, aa1-253, His-Tag (Phosphoglycerate Mutase 2, BPG-dependent PGAM 2, PGAM-M, Muscle-specific Phosphoglycerate Mutase, Phosphoglycerate Mutase Isozyme M, PGAMM)

Cat no: 045451


Supplier: United States Biological
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PGAM2, also known as phosphoglycerate mutase 2, belongs to the phosphoglycerate mutase family. Phosphoglycerate mutase (PGAM) catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. The PGAM is a dimeric enzyme containing, in different tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). This gene encodes muscle-specific PGAM subunit. Mutations in this gene cause muscle phosphoglycerate mutase eficiency, also known as glycogen storage disease X. Source: Recombinant corresponding to aa1-253 from human PGAM2, fused to His-tag at N-terminus, expressed in E.coli. Molecular Weight: ~30.9kD (273aa) confirmed by MALDI-TOF AA Sequence: MGSSHHHHHH SSGLVPRGSH MATHRLVMVR HGESTWNQEN RFCGWFDAEL SEKGTEEAKR GAKAIKDAKM EFDICYTSVL KRAIRTLWAI LDGTDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD IPPPPMDEKH PYYNSISKER RYAGLKPGEL PTCESLKDTI ARALPFWNEE IVPQIKAGKR VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL NKELKPTKPM QFLGDEETVR KAMEAVAAQG KAK Storage and Stability: May be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Catalogue number: 045451
Size: 100ug
Form: Supplied as a liquid in 20mM Tris-HCl, pH 8.0, 1mM DTT, 0.1M sodium chloride, 20% glycerol.
Purity: ~95% (SDS-PAGE)
References: 1. Tsujino S., et al. (1989) J. Biol. Chem. 264:15334-15337. 2. Hadjigeorgiou G.M., et al. (1999) Neuromuscul. Disord. 9:399-402.

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