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G6751

Sigma-Aldrich

α-Glycerophosphate Dehydrogenase from rabbit muscle

Type I, ammonium sulfate suspension, 100-300 units/mg protein

Synonym(s):

sn-Glycerol-3-phosphate Dehydrogenase from rabbit muscle, sn-Glycerol-3-phosphate:NAD+ 2-oxidoreductase

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$76.30
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$147.00
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$817.00

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About This Item

CAS Number:
9075-65-4
EC Number:
1.1.1.8 (BRENDA, IUBMB)
EC Number:
232-982-3
MDL number:
MFCD00040474
UNSPSC Code:
12352204
NACRES:
NA.54

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biological source

rabbit muscle

Quality Level

200

type

Type I

form

ammonium sulfate suspension

specific activity

100-300 units/mg protein

storage condition

(Tightly closed)

technique(s)

activity assay: suitable

color

white

foreign activity

Lactic dehydrogenase, pyruvate kinase, aldolase, and glyceraldehyde-3-phosphate dehydrogenase ≤0.01%
Triosephosphate isomerase ≤0.02%

storage temp.

2-8°C

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P3397G6880G1881
α-Glycerophosphate Dehydrogenase from rabbit muscle Type I, ammonium sulfate suspension, 100-300 units/mg protein

Sigma-Aldrich

G6751

α-Glycerophosphate Dehydrogenase from rabbit muscle

Phosphoglucomutase from rabbit muscle ammonium sulfate suspension, ≥100 units/mg protein

Sigma-Aldrich

P3397

Phosphoglucomutase from rabbit muscle

α-Glycerophosphate Dehydrogenase from rabbit muscle Type X, lyophilized powder, ≥100 units/mg protein

Sigma-Aldrich

G6880

α-Glycerophosphate Dehydrogenase from rabbit muscle

α-Glycerophosphate Dehydrogenase-Triosephosphate Isomerase from rabbit muscle Type III, ammonium sulfate suspension

Sigma-Aldrich

G1881

α-Glycerophosphate Dehydrogenase-Triosephosphate Isomerase from rabbit muscle

biological source

rabbit muscle

biological source

rabbit muscle

biological source

-

biological source

rabbit muscle

specific activity

100-300 units/mg protein

specific activity

≥100 units/mg protein

specific activity

≥100 units/mg protein

specific activity

-

technique(s)

activity assay: suitable

technique(s)

activity assay: suitable

technique(s)

-

technique(s)

-

form

ammonium sulfate suspension

form

ammonium sulfate suspension

form

lyophilized powder

form

ammonium sulfate suspension

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

2-8°C

storage condition

(Tightly closed)

storage condition

(Tightly closed)

storage condition

-

storage condition

-

General description

α-Glycerophosphate dehydrogenase is a membrane protein and a flavin-linked primary dehydrogenase.[1]

Research area: Cell Signaling[1]

Application

α-Glycerophosphate Dehydrogenase from rabbit muscle has been used:
  • in the reaction mixture to measure the glycerol kinase activity[2]
  • to demonstrate compartmentalized enzymatic reactions where NADH is involved[3]
  • in the reaction mixture assay for L-fuculose-1-phosphate aldolase[4]

Biochem/physiol Actions

α-Glycerophosphate dehydrogenase catalyzes the oxidation of L-α-glycerophosphate (Glp) to form dihydroxyacetone phosphate (DHAP) and hydrogen peroxide (H2O2).[5] This enzyme is associated with respiratory electron transport chain, glycolysis, and phospholipid metabolism.[1]

Physical form

Crystalline suspension in 3.2 M (NH4)2SO4 and 0.1 g/L EDTA solution, pH 6.0

Preparation Note

Prepared by modification of the method of Fondy.

Analysis Note

Protein determined by biuret.

Other Notes

One unit will convert 1.0 μmole of dihydroxyacetone phosphate to α-glycerophosphate per min at pH 7.4 at 25 °C.

related product

Product No.
Description
Pricing

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
0000489805
0000489805
0000446288
0000446287
0000446287

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Somchart Maenpuen et al.
The FEBS journal, 282(16), 3043-3059 (2015-02-26)
L-α-glycerophosphate oxidase is an FAD-dependent enzyme that catalyzes the oxidation of L-α-glycerophosphate (Glp) by molecular oxygen to generate dihydroxyacetone phosphate (DHAP) and hydrogen peroxide (H2O2). The catalytic properties of recombinant His6-GlpO from Mycoplasma pneumoniae (His6-MpGlpO) were investigated through transient and
Joanne I Yeh et al.
Proceedings of the National Academy of Sciences of the United States of America, 105(9), 3280-3285 (2008-02-26)
Sn-glycerol-3-phosphate dehydrogenase (GlpD) is an essential membrane enzyme, functioning at the central junction of respiration, glycolysis, and phospholipid biosynthesis. Its critical role is indicated by the multitiered regulatory mechanisms that stringently controls its expression and function. Once expressed, GlpD activity
Structural studies on nicotinamide adenine dinucleotide-linked L-glycerol 3-phosphate dehydrogenase crystallized from rat skeletal muscle.
T P Fondy et al.
The Journal of biological chemistry, 243(11), 3148-3160 (1968-06-10)
Optimal conditions for biomass and recombinant glycerol kinase production using the yeast Pichia pastoris
Aizemberg R, et al.
Food Technology and Biotechnology, 49(3), 329-329 (2011)
Susan K Boehlein et al.
The Plant journal : for cell and molecular biology, 99(1), 23-40 (2019-02-13)
Cereal yields decrease when grain fill proceeds under conditions of prolonged, moderately elevated temperatures. Endosperm-endogenous processes alter both rate and duration of dry weight gain, but underlying mechanisms remain unclear. Heat effects could be mediated by either abnormal, premature cessation
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