anti-GAPDH-SO3, pAb

CHF 322.00
In stock
YIF-LF-PA0006100 µlCHF 322.00
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Product Details
Synonyms GAPD; GAPDH; CDABP0047; EC=1.2.1.12; EC=2.6.99.-; Peptidyl-Cysteine S-Nitrosylase GAPDH; Glyceraldehyde-3-Phosphate Dehydrogenase; Sulfonylated
Product Type Polyclonal Antibody
Properties
Immunogen/Antigen Sulfonylated peptide (KLH coupled) corresponding to the oxidation sensitive site sequence to human GADPH.
Application

Western Blot (1:2,000)

Crossreactivity Human
Formulation Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol.
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.
Documents
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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-bisphosphoglycerate 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, DNA repair, nuclear RNA export, membrane fusion 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. On recent study, GAPDH has identified of the most oxidant sensitive cell proteins. Independent of its glycolytic activity it is also involved in membrane trafficking in the early secretory pathway.

Product References

1) Baxi, M. D. et.al. (1995) Biochemistry.34:9700-9707. (General)
2) Singh, R. et.al. (1993) Science. 259:365-368. (General)
3) Han, X. et. al. (1998) Biochem. Biophys. Acta. 1414:95-107. (General)
4) Kragten, E. et.al. (1998) J. Biol. Chem. 273:5821-5828. (General)
5) Baty, J.W. et.al. (2005) Biochem J. (General)

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