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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

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, 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.\n\nSource:\nRecombinant corresponding to aa1-253 from human PGAM2, fused to His-tag at N-terminus, expressed in E.coli.\n\nMolecular Weight:\n~30.9kD (273aa) confirmed by MALDI-TOF\n\nAA Sequence:\nMGSSHHHHHH 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\n\nStorage and Stability:\nMay 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.

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SPECIFICATIONS

Catalog 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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