GAPDH (human) (rec.)

CHF 219.00
In stock
YIF-LF-P00080.5 mgCHF 219.00
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Product Details
Synonyms GAPD; GAPDH; EC=2.6.99.-; EC=1.2.1.12; Peptidyl-Cysteine S-Nitrosylase GAPDH; Glyceraldehyde-3-Phosphate Dehydrogenase
Product Type Protein
Properties
Source/Host E. coli
Crossreactivity Human
Biological Activity

43.96U/mg (One unit of activity of GAPDHis defined as the amount of enzyme required to convert 1 μmole of NAD to NADH per minunder standard assay conditions)

Formulation Lyophilized in 20mM HEPES, pH 7.4.
Other Product Data

Click here for Original Manufacturer Product Datasheet
Our product description may differ slightly from the original manufacturers product datasheet.

Declaration Manufactured by AbFrontier
Shipping and Handling
Shipping BLUE ICE
Short Term Storage +4°C
Long Term Storage -20°C
Handling Advice Avoid freeze/thaw cycles.
Use/Stability After reconstitution, store at -80°C.
Documents
MSDS Inquire
Product Specification Sheet
Datasheet Download PDF

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a catalytic enzyme commonly known to be involved in glycolysis. The enzyme exists as a tetramer of identical 37-kDa subunits. GAPDH catalyzes the reversible reduction of 1,3-bisphosphoglycerate to glyceraldehydes 3-phosphophate in the presence of NADPH. Apart from playing a key role in glycolysis, this ubiquitously expressed enzyme also displays other activities unrelated to its glycolytic function. GAPDH is reported to be involved in the processes of DNA replication, DNA repair, nuclear RNA export, membrane fusion and microtubule bundling (1-5). Other studies also provide evidence of GAPDH playing an essential part of the program of gene expression observed in apoptosis and as part of the cellular phenotype of age-related neuro-degenerative diseases (6-7).

Product References

1) Baxi, M. D. and Vishwanatha, J. K. (1995) Biochemistry. 34, 9700-9707. (General)
2) McNulty, S. E. and Toscano, W. A. Jr. (1995) Biochem. Biophys. Res. Commun. 34, 165-171. (General)
3) Singh, R. and Green, M. R. (1993) Science. 259, 365-368. (General)
4) Zang, W. Q. et al. (1998) Virology. 28, 46-52. (General)
5) Han, X. et al. (1998) Biochem. Biophys. Acta. 1414, 95-107. (General)
6) Kragten, E. et al. (1998) J. Biol. Chem. 273, 5821-5828. (General)
7) Koshy, B. (1996) Hum. Mol. Genet. 5, 1311-1318. (General)
8) Bagui, S. et al. (1999) Eur. J. Biochem. 262(2), 386-395. (General)

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