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standard for protein electrophoresis

Glyceraldehyde-3-phosphate Dehydrogenase from rabbit muscle, GAPDH, D-Glyceraldehyde 3-phosphate:NAD+ oxidoreductase (phosphorylating)
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:

Quality Level


for molecular biology



mol wt

~36 kDa


vial of 5 mg


electrophoresis: suitable

storage temp.


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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.


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.

Storage Class Code

13 - Non Combustible Solids



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificate of Analysis

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Certificate of Origin

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More Documents

Quotes and Ordering

Ling Ji et al.
Molecular therapy. Nucleic acids, 19, 546-561 (2020-01-14)
Long non-coding RNAs (lncRNAs) are crucial molecules in tumorigenesis and tumor growth in various human cancers, including colorectal cancer (CRC). Studies have revealed that lncRNAs can regulate cellular processes in cancers by interacting with proteins, for example RNA-binding proteins (RBPs).
Wen-Wei Zhang et al.
Eukaryotic cell, 12(1), 70-77 (2012-11-06)
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
Kati Juuti-Uusitalo et al.
Investigative ophthalmology & visual science, 54(5), 3510-3519 (2013-05-21)
Aquaporins (AQPs), a family of transmembrane water channel proteins, are essential for allowing passive water transport through retinal pigmented epithelial (RPE) cells. Even though human native RPE cells and immortalized human RPEs have been shown to express AQPs, the expression
C Dani et al.
European journal of biochemistry, 145(2), 299-304 (1984-12-03)
We have partially purified the messenger RNA coding for glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC from HeLa cells and obtained a cDNA clone containing part of its sequence. Using this clone to probe electrophoregrams of RNA transferred to nitrocellulose, we have
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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