anti-GAPDH, mAb (7B)

CHF 315.00
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YIF-LF-MA0038100 µlCHF 315.00
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Product Details
Synonyms GAPD; GAPDH; CDABP0047; EC=2.6.99.-; EC=; Peptidyl-Cysteine S-Nitrosylase GAPDH; Glyceraldehyde-3-Phosphate Dehydrogenase
Product Type Monoclonal Antibody
Clone 7B
Isotype Mouse IgG1 κ
Immunogen/Antigen Recombinant human protein purified from E. coli.

Western Blot (1:10,000)
Immunoprecipitation (1~2 μl)

Crossreactivity Human
Purity Detail Ammonium sulfate precipitation.
Formulation Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol.
Isotype Negative Control

Mouse IgG1 Isotype Control

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
Use/Stability Stable for at least 1 year after receipt when stored at -20°C.
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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-bisphos-phoglycerate to glyceraldehyde 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 (1), DNA repair (2), nuclear RNA export (3-4), membrane fusion (5) and microtubule bundling. 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 neurodegenerative diseases (6-7). Independent of its glycolytic activity it is also involved in membrane trafficking in the early secretory pathway.

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)

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