G5262
GAPDH
standard for protein electrophoresis
Synonym(s):
Glyceraldehyde-3-phosphate Dehydrogenase from rabbit muscle, D-Glyceraldehyde 3-phosphate:NAD+ oxidoreductase (phosphorylating), GAPDH
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About This Item
Recommended Products
grade
for molecular biology
Quality Level
form
powder
mol wt
~36 kDa
packaging
vial of 5 mg
technique(s)
electrophoresis: suitable
storage temp.
2-8°C
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General description
GAPDH (Glyceraldehyde-3-phosphate dehydrogenase) catalyzes the conversion of glyceraldehyde-3-phosphate into D-glycerate-1,3-bisphosphate as part of the glycolysis pathway. GAPDH has also been found to function in additional cellular process, such as transcription, apoptosis, oxidative stress and ER to Golgi transport.
Application
GAPDH protein is suitable for use as a molecular weight marker and protein standard for molecular biology applications, including western blotting and mass spectometry.
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.
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Product No.
Description
Pricing
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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The initial 7 steps of the glycolytic pathway from glucose to 3-phosphoglycerate are localized in the glycosomes in Leishmania, including step 6, catalyzed by the enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). In L. donovani and L. mexicana, there exists a second GAPDH
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Acta crystallographica. Section D, Biological crystallography, 61(Pt 11), 1508-1513 (2005-10-22)
The crystal structure of human liver glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has been determined. This structure represents the first moderate-resolution (2.5 A) and crystallographically refined (Rfree = 22.9%) human GAPDH structure. The liver GAPDH structure consists of a homotetramer, each subunit of
J E Welch et al.
Journal of andrology, 21(2), 328-338 (2000-03-14)
Although the process of glycolysis is highly conserved in eukaryotes, several glycolytic enzymes have unique structural or functional features in spermatogenic cells. We previously identified and characterized the mouse complementary DNA (cDNA) and a gene for 1 of these enzymes
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