P1103-Phosphoglycerate Mutase 2 Human

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BioVision 10/16 For research use only Phosphoglycerate mutase 2, human recombinant CATALOG NO: P1103-10 10 µg P1103-50 50 µg ALTERNATE NAMES: GSD10, PGAM-M, PGAMM, PGAM2 CONCENTRATION: 1 mg/ml (determined by Bradford assay) SOURCE: Phosphoglycerate mutase 2 recombinant protein was expressed in E.coli and fused to His-tag at N-terminus (1-253aa). PURITY: > 95% by SDS-PAGE MOL. WEIGHT: This protein is fused with 6x His tag at C terminus and the protein has a calculated MW of 30.9 kDa (253aa) FORM: Liquid 20mM Tris-HCl buffer (pH8.0) containing 20% glycerol, 0.1M NaCl, FORMULATION: Human recombinant PGAM2 1mM DTT STORAGE CONDITIONS: 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. 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 RELATED PRODUCT: DESCRIPTION: PGAM2, also known as phosphoglycerate mutase 2, belongs to the phosphoglycerate mutase family. Phosphoglycerate mutase 6-Phosphogluconic Acid (6-PGA) Assay Kit (Colorimetric) (Cat. No. K217-100) (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 FOR RESEARCH USE ONLY! Not to be used on humans. 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 efficiency, also known as glycogen storage disease X. Recombinant human PGAM2 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography. BIOLOGICAL ACTIVITY: Specific activity is >100 units/mg, in which One unit will convert 1.0 umole of 3-phosphoglycerate to 2-phosphoglcerate per minute at pH 7.6 at 37C. BioVision Incorporated Tel: 408-493-1800 | Fax: 408-493-1801 155 S. Milpitas Boulevard, Milpitas, CA 95035 USA www.biovision.com | [email protected] .

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Oxidative Stress Activates SIRT2 to Deacetylate and Stimulate Phosphoglycerate Mutase
Published OnlineFirst May 1, 2014; DOI: 10.1158/0008-5472.CAN-13-3615 Cancer Tumor and Stem Cell Biology Research Oxidative Stress Activates SIRT2 to Deacetylate and Stimulate Phosphoglycerate Mutase Yanping Xu2,3, Fulong Li2,3, Lei Lv1,2, Tingting Li2,3, Xin Zhou2,3, Chu-Xia Deng4, Kun-Liang Guan1,2,5, Qun-Ying Lei1,2, and Yue Xiong1,2,6 Abstract Glycolytic enzyme phosphoglycerate mutase (PGAM) plays an important role in coordinating energy production with generation of reducing power and the biosynthesis of nucleotide precursors and amino acids. Inhibition of PGAM by small RNAi or small molecule attenuates cell proliferation and tumor growth. PGAM activity is commonly upregulated in tumor cells, but how PGAM activity is regulated in vivo remains poorly understood. Here we report that PGAM is acetylated at lysine 100 (K100), an active site residue that is invariably conserved from bacteria, to yeast, plant, and mammals. K100 acetylation is detected in ﬂy, mouse, and human cells and in multiple tissues and decreases PGAM2 activity. The cytosolic protein deacetylase sirtuin 2 (SIRT2) deacetylates and activates PGAM2. Increased levels of reactive oxygen species stimulate PGAM2 deacetylation and activity by promoting its interaction with SIRT2. Substitution of endogenous PGAM2 with an acetylation mimetic mutant K100Q reduces cellular NADPH production and inhibits cell proliferation and tumor growth. These results reveal a mechanism of PGAM2 regulation and NADPH homeostasis in response to oxidative stress that impacts cell proliferation and tumor growth. Cancer Res; 74(13); 1–13. Ó2014 AACR. Introduction contains two PGAM genes, PGAM1 (also known as PGAM-B), Enhanced glycolysis, commonly referred to as the "Warburg which is expressed in brain and most other tissues, and PGAM2 effect" (1), is a distinctive and prominent feature of cancer cells.
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Phosphoglycerate Mutase Deficiency
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