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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-609-4
MDL number:
Specific activity:
≥75 units/mg protein
Biological source:
rabbit muscle
biological source
rabbit muscle
form
lyophilized powder
specific activity
≥75 units/mg protein
composition
Protein, ≥80% biuret
foreign activity
3-Phosphoglyceric phosphokinase ≤0.05%, lactic dehydrogenase, myokinase, and pyruvate kinase ≤0.01%, triosephosphate isomerase ≤0.1%
shipped in
wet ice
storage temp.
−20°C
Quality Level
Related Categories
General description
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a multifunctional protein. It is basically called as a glycolytic enzyme.
Application
Glyceraldehyde-3-phosphate Dehydrogenase from rabbit muscle has been used:
- for measurements of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) activity assay
- to generate a linear standard curve to analyse GAPDH activity in the experimental samples collected from mice
- in anti-aggregation assays
- in purified GAPDH studies
Biochem/physiol Actions
Glyceraldehyde-3-phosphate dehydrogenase catalyzes the conversion of glyceraldehyde-3-phosphate into D-glycerate-1,3-bisphosphate as part of the glycolysis pathway.
Glyceraldehyde-3-phosphate dehydrogenase catalyzes the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate as part of glycolysis. It has also been shown to have roles in initiation of apoptosis, transcription activation and the shuttling of ER to Golgi vesicles<<<18,New>>>.
Physical form
Lyophilized powder containing citrate buffer salts
Other Notes
One unit will reduce 1.0 μmole of 3-phosphoglycerate to D-glyceraldehyde 3-phosphate per min in a coupled system with 3-phosphoglyceric phosphokinase at pH 7.6 at 25 °C.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Role of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in DNA repair
Kosova A A, et al.
The Journal of Biological Chemistry, 82(6), 643-654 (2017)
Paradoxical inhibition of glycolysis by pioglitazone opposes the mitochondriopathy caused by AIF deficiency
Benit P, et al.
EBioMedicine, 17, 75-87 (2017)
Poly ADP-Ribose Polymerase Inhibition Ameliorates Hind Limb Ischemia Reperfusion Injury in a Murine Model of Type 2 Diabetes
Long C A, et al.
Annals of Surgery, 258(6) (2013)
The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity
Merz F, et al.
The Journal of Biological Chemistry, 281(42), 31963-31971 (2006)
Oligomerization of a molecular chaperone modulates its activity
Saio T, et al.
eLife, 7(6), e35731-e35731 (2018)
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