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| Product | Description | |
|---|---|---|
| phosphoglycerate phosphatase | This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. Group: Enzymes. Synonyms: D-2-phosphoglycerate phosphatase; glycerophosphate phosphatase. Enzyme Commission Number: EC 3.1.3.20. CAS No. 9055-30-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3623; phosphoglycerate phosphatase; EC 3.1.3.20; 9055-30-5; D-2-phosphoglycerate phosphatase; glycerophosphate phosphatase. Cat No: EXWM-3623. |  |
| 3-phosphoglycerate phosphatase | Wide specificity, but 3-phosphoglycerate is the best substrate. Group: Enzymes. Synonyms: D-3-Phosphoglycerate phosphatase; 3-PGA phosphatase. Enzyme Commission Number: EC 3.1.3.38. CAS No. 62213-13-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3641; 3-phosphoglycerate phosphatase; EC 3.1.3.38; 62213-13-2; D-3-Phosphoglycerate phosphatase; 3-PGA phosphatase. Cat No: EXWM-3641. | |
| ADP-phosphoglycerate phosphatase | Also acts on 2,3-bisphosphoglycerate. Group: Enzymes. Synonyms: adenosine diphosphate phosphoglycerate phosphatase. Enzyme Commission Number: EC 3.1.3.28. CAS No. 37288-12-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3631; ADP-phosphoglycerate phosphatase; EC 3.1.3.28; 37288-12-3; adenosine diphosphate phosphoglycerate phosphatase. Cat No: EXWM-3631. | |
| glucosyl-3-phosphoglycerate phosphatase | The enzyme is involved in biosynthesis of 2-O-(α-D-glucopyranosyl)-D-glycerate via the two-step pathway in which EC 2.4.1.266 (glucosyl-3-phosphoglycerate synthase) catalyses the conversion of GDP-glucose and 3-phospho-D-glycerate into 2-O-(α-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(α-D-glucopyranosyl)-D-glycerate by glucosyl-3-phosphoglycerate phosphatase. In vivo the enzyme catalyses the dephosphorylation of 2-O-(α-D-mannopyranosyl)-3-phospho-D-glycerate with lower efficiency. Divalent metal ions (Mg2+, Mn2+ or Co2+) stimulate activity. Group: Enzymes. Synonyms: GpgP protein. Enzyme Commission Number: EC 3.1.3.85. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3691; glucosyl-3-phosphoglycerate phosphatase; EC 3.1.3.85; GpgP protein. Cat No: EXWM-3691. | |
| mannosyl-3-phosphoglycerate phosphatase | Requires Mg2+. The enzyme from Pyrococcus horikoshii is specific for α-D-mannosyl-3-phosphoglycerate and forms part of the pathway for the synthesis of mannosylglycerate. Group: Enzymes. Enzyme Commission Number: EC 3.1.3.70. CAS No. 393512-74-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3675; mannosyl-3-phosphoglycerate phosphatase; EC 3.1.3.70; 393512-74-8. Cat No: EXWM-3675. | |
| bisphosphoglycerate mutase | In the direction shown, this enzyme is phosphorylated by 3-phosphoglyceroyl phosphate, to give phosphoenzyme and 3-phosphoglycerate. The latter is rephosphorylated by the enzyme to yield 2,3-bisphosphoglycerate, but this reaction is slowed by dissociation of 3-phosphoglycerate from the enzyme, which is therefore more active in the presence of added 3-phosphoglycerate. This enzyme also catalyses, slowly, the reactions of EC 3.1.3.13 (bisphosphoglycerate phosphatase), EC 5.4.2.11 [phosphoglycerate mutase (2,3-diphosphoglycerate-dependent)] and EC 5.4.2.12 [phosphoglycerate mutase (2,3-diphosphoglycerate-independent)]. Group: Enzymes. Synonyms: diphosphoglycerate mutase; glycerate phosphomutase; bisphosphoglycerate synthase; bisphosphoglyceromutase; bip. Enzyme Commission Number: EC 5.4.2.4. CAS No. 37211-69-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5526; bisphosphoglycerate mutase; EC 5.4.2.4; 37211-69-1; diphosphoglycerate mutase; glycerate phosphomutase; bisphosphoglycerate synthase; bisphosphoglyceromutase; biphosphoglycerate synthase; diphosphoglyceric mutase; 2,3-diphosphoglycerate mutase; phosphoglyceromutase; 2,3-diphosphoglycerate synthase; DPGM; 2,3-bisphosphoglycerate mutase; BPGM; diphosphoglyceromutase; 2,3-diphosphoglyceromutase. Cat No: EXWM-5526. | |
| glucosyl-3-phosphoglycerate synthase | The enzyme is involved in biosynthesis of 2-O-(α-D-glucopyranosyl)-D-glycerate via the two-step pathway in which glucosyl-3-phosphoglycerate synthase catalyses the conversion of GDP-glucose and 3-phospho-D-glycerate into 2-O-(α-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(α-D-glucopyranosyl)-D-glycerate by EC 3.1.3.85 glucosyl-3-phosphoglycerate phosphatase. The activity is dependent on divalent cations (Mn2+, Co2+, or Mg2+). The enzyme from Persephonella marina shows moderate flexibility on the sugar donor concerning the nucleotide moiety (UDP-glucose, ADP-glucose, GDP-glucose) but is strictly specific for glucose. The enzyme is also strictly specific for 3-phospho-D-glycerate as acceptor. The enzyme from Methanococcoides burtonii is strictly specific for GDP-glucose and 3-phospho-D-glycerate. This enzyme catalyses the first glucosylation step in methylglucose lipopolysaccharide biosynthesis in mycobacteria. Group: Enzymes. Synonyms: GpgS protein; GPG synthase; glucosylphosphoglycerate s. Enzyme Commission Number: EC 2.4.1.266. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2497; glucosyl-3-phosphoglycerate synthase; EC 2.4.1.266; GpgS protein; GPG synthase; glucosylphosphoglycerate synthase. Cat No: EXWM-2497. | |
| glucosylglycerate synthase | Persephonella marina possesses two enzymic systems for the synthesis of glucosylglycerate. The first one is a single-step pathway in which glucosylglycerate synthase catalyses the synthesis of 2-O-(α-D-glucopyranosyl)-D-glycerate in one-step from ADP-glucose and D-glycerate. The second system is a two-step pathway in which EC 2.4.1.266 (glucosyl-3-phosphoglycerate synthase) catalyses the conversion of NDP-glucose and 3-phospho-D-glycerate into 2-O-(α-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(α-D-glucopyranosyl)-D-glycerate by EC 3.1.3.85 (glucosyl-3-phosphoglycerate phosphatase). Group: Enzymes. Synonyms: Ggs (gene name). Enzyme Commission Number: EC 2.4.1.268. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2499; glucosylglycerate synthase; EC 2.4.1.268; Ggs (gene name). Cat No: EXWM-2499. | |
| mannosyl-3-phosphoglycerate synthase | Requires Mg2+. The enzyme is absolutely specific for GDPmannose and 3-phosphoglycerate, and transfers the mannosyl group with retention of configuration. In the hyperthermophilic archaeon Pyrococcus horikoshii, the mannosyl-3-phosphoglycerate formed is subsequently dephosphorylated by a specific phosphatase, EC 3.1.3.70 (mannosyl-3-phosphoglycerate phosphatase), producing mannosylglycerate. Group: Enzymes. Synonyms: MPG synthase; GDP-mannose:3-phosphoglycerate 3-α-D-mannosyltransferase. Enzyme Commission Number: EC 2.4.1.217. CAS No. 393512-63-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2445; mannosyl-3-phosphoglycerate synthase; EC 2.4.1.217; 393512-63-5; MPG synthase; GDP-mannose:3-phosphoglycerate 3-α-D-mannosyltransferase. Cat No: EXWM-2445. | |
| mannosylglycerate synthase | Rhodothermus marinus can also form mannosylglycerate via a two-step pathway catalysed by EC 2.4.1.217 (mannosyl-3-phosphoglycerate synthase) and EC 3.1.3.70 (mannosyl-3-phosphoglycerate phosphatase). Depending on experimental conditions mannosylglycerate synthase is more or less specific for the GDP-mannose and D-glycerate. Group: Enzymes. Enzyme Commission Number: EC 2.4.1.269. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2500; mannosylglycerate synthase; EC 2.4.1.269. Cat No: EXWM-2500. | |
| Phosphoglycerate mutase 1 from Human, Recombinant | 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. Group: Enzymes. Synonyms: Pgam-1; PGAM1. Enzyme Commission Number: EC 5.4.2.1. Purity: > 90% by SDS-PAGE. Mole weight: 30.9 kDa. Activity: >300 units/mg. 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. Form: Liquid. Source: E. coli and fused to His-tag at N-terminus. Species: Human. Pgam-1; PGAM1; Phosphoglycerate mutase 1; Phosphoglycerate mutase. Cat No: NATE-1647. | |
| Phosphoglycerate mutase 1 from Mouse, Recombinant | 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. Group: Enzymes. Synonyms: Pgam-1; PGAM1. Enzyme Commission Number: EC 5.4.2.1. Purity: > 95% by SDS-PAGE. Mole weight: 31.4 kDa. Activity: >150 units/mg. 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. Form: Liquid. Source: E. coli and fused to His-tag at N-terminus. Species: Mouse. Pgam-1; PGAM1; Phosphoglycerate mutase 1; Phosphoglycerate mutase. Cat No: NATE-1646. | |
| Phosphoglycerate mutase 2 from Human, Recombinant | 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. Group: Enzymes. Synonyms: GSD10; PGAM-M; PGAMM; PGAM2. Enzyme Commission Number: EC 5.4.2.11. Purity: > 95% by SDS-PAGE. Mole weight: 30.9 kDa. Activity: >100 units/mg. 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. Form: Liquid. Source: E. coli and fused to His-tag at N-terminus. Species: Human. GSD10; PGAM-M; PGAMM; PGAM2; Phosphoglycerate mutase 2; Phosphoglycerate mutase. Cat No: NATE-1643. | |
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