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P3397

Sigma-Aldrich

Phosphoglucomutase from rabbit muscle

ammonium sulfate suspension, ≥100 units/mg protein

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Synonym(s):
PGM, α-D-Glucose-1,6-bisphosphatase, α-D-Glucose-1-phosphate phosphotransferase
CAS Number:
9001-81-4
Enzyme Commission number:
5.4.2.2 (BRENDA, IUBMB)
MDL number:
MFCD00131886
NACRES:
NA.54

biological source

rabbit muscle

Quality Level

300

description

ammonium sulfate suspension, >=100 units/mg protein

form

ammonium sulfate suspension

specific activity

≥100 units/mg protein

storage condition

(Tightly closed)

technique(s)

activity assay: suitable

color

white to light yellow

foreign activity

lactic dehydrogenase ≤0.5%
phosphoglucose isomerase ≤0.01%
pyruvate kinase ≤0.05%

shipped in

wet ice

storage temp.

2-8°C

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General description

Research area: Cell Signaling

Phosphoglucomutase (PGM), a conserved enzyme, is abundantly found in animals, plants, and microorganisms. It is distributed in almost all tissues.

Application

Phosphoglycomutase has been used:

  • to study glycogenesis and phosphoglycomutase deficiency in humans
  • in phosphoglucomutase assays to study metabolic regulation
  • for assay A to assay enzymes closely linked to glycogen metabolism in transformed BL21(DE3)C43 cells
  • in sucrose synthase (SuSy) andADPglucose pyrophosphorylase (AGPase) assays(3)
  • in enzyme activity assay for coupling the reduction of nicotinamide adenine dinucleotide phosphate (NADP+)to determine glucose-1-phosphate from sucrose and inorganic phosphate (Pi)

Biochem/physiol Actions

Phosphoglucomutase(PGM) enzyme plays a vital role in glycolysis and gluconeogenesis. It is involved in glycogen and trehalose metabolism in insects. PGM participates in the development of plants and some microorganisms. It is essential for proteins, lipids, and nucleic acid metabolism and is crucial for the development of plants because glucose-6-phosphate is a crucial central metabolite. PGM catalyzes the interconversion of glucose-6-phosphate (G-6-P)and glucose-1-phosphate (G-1-P).

Unit Definition

One unit will convert 1.0 μmole of α-D-glucose 1-phosphate to α-D-glucose 6-phosphate per min at pH 7.4 at 30 °C.

Physical form

Crystalline suspension in 3.2 M (NH4)2SO4, pH 6.0 containing 0.01% EDTA

Analysis Note

Protein determined by biuret.

antibody

Product No.
Description
Pricing

WH0005238M1

Monoclonal Anti-PGM3 antibody produced in mouse, clone 1E2-1B12, purified immunoglobulin, buffered aqueous solution

WH0055276M5

Monoclonal Anti-PGM2 antibody produced in mouse, clone 1A3, purified immunoglobulin, buffered aqueous solution

HPA024190

Anti-PGM1 antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution, Ab1

HPA024637

Anti-PGM1 antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution, Ab2

HPA029759

Anti-PGM3 antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution, ab1

HPA029760

Anti-PGM3 antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution, ab2

SAB1105944

Anti-PGM2 (596-610) antibody produced in rabbit, IgG fraction of antiserum

MABT1503

Anti-PGM5 (Aciculin) Antibody, clone 14F8, clone 14F8, from mouse

enzyme

Product No.
Description
Pricing

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Nora Alonso-Casajús et al.
Journal of bacteriology, 188(14), 5266-5272 (2006-07-04)
To understand the biological function of bacterial glycogen phosphorylase (GlgP), we have produced and characterized Escherichia coli cells with null or altered glgP expression. glgP deletion mutants (DeltaglgP) totally lacked glycogen phosphorylase activity, indicating that all the enzymatic activity is
Phosphoglucomutase; mechanism of action.
V JAGANNATHAN et al.
The Journal of biological chemistry, 179(2), 569-575 (1949-06-01)
Molecular cloning of a gene encoding the sucrose phosphorylase from Leuconostoc mesenteroides B-1149 and the expression in Escherichia coli
Lee Ha J, et al.
Enzyme and Microbial Technology, 39, 612-620 (2006)
M B Dworkin et al.
The Journal of biological chemistry, 262(35), 17038-17045 (1987-12-15)
When 32P-labeled phosphoenolpyruvate is injected into Xenopus laevis oocytes, a 50-60-kDa protein of subunit size Mr 29,000 is rapidly labeled, followed by a second (monomeric) protein of 66 kDa concomitant with the loss of label from the first protein. We
Bi-Ying Pan et al.
3 Biotech, 10(2), 61-61 (2020-02-08)
Phosphoglucomutase (PGM) is a key enzyme in glycolysis and gluconeogenesis, regulating both glycogen and trehalose metabolism in insects. In this study, we explored the potential function of phosphoglucomutase (PGM) using RNA interference technology in Nilaparvata lugens, the brown planthopper. PGM1
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