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GAPDH, SO3 (Glyceraldehyde-3-phosphate Dehydrogenase, Peptidyl-cysteine S-nitrosylase GAPDH, GAPD, CDABP0047, OK/SW-cl.12)

Cat no: G8140-02M


Supplier: United States Biological
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Glyceraldehyde-3-phosphate dehydrogenase(GAPDH) is a catalytic enzyme commonly known to be involved in glycolysis. The enzyme exists as a tetramer of identical 37kDa 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. Applications: Suitable for use in Western Blot. Other applications not tested. Recommended Dilutions: Western Blot: 1:2000 Optimal dilutions to be determined by the researcher. Positive Control: HeLa cell treated with H2O2 Storage and Stability: May be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Catalogue number: G8140-02M
Reactivities: Human
Hosts: Rabbit
Applications: Western Blot
Size: 100ul
Form: Supplied as a liquid in HEPES, 0.15M sodium chloride, 0.01% BSA, 0.03% sodium azide, 50% glycerol.
P type: Pab
Isotype: IgG
Purity: Serum
References: 1. Baxi, M. D. et.al.(1995)Biochemistry.34:9700-9707. 2. Singh, R. et.al.(1993)Science. 259:365-368. 3. Han, X. et. al. (1998)Biochem. Biophys. Acta. 1414:95-107. 4. Kragten, E. et.al. (1998) J. Biol. Chem. 273:5821-5828. 5. Baty,J.W.et.al.(2005)Biochem J. Mar 31, published.
Additional info: Recognizes human GAPDH, SO3.

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