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

Glyceraldehyde 3-Phosphate Dehydrogenase (GAPDH) is a metabolic enzyme responsible for catalyzing one step in the glycolytic pathway, the reversible oxidative phosphorylation of glyceraldehyde 3-phosphate. Because GAPDH as a protein expressed in large amounts and which is required at all times for an important "house keeping" functions, levels of GAPDH mRNA are often measured and used as standards in studies of mRNA expression. Increasingly, scientists are making use of specific antibodies to GAPDH in comparable studies of levels of protein expression. This antibody can be used as a loading control for western blotting experiments, allowing comparison between the level of this protein and others in a cell or tissue. Apart from a role in glycolysis, GAPDH may have other roles such as in the activation of transcription (1). GAPDH is reported to bind to a variety of other proteins, including the amyloid precursor protein, mutations in which cause some forms of Alzheimer's disease, and the polyglutamine tracts of Huntingtin, the protein product aberrant forms of which are causative of Huntington's disease (2,3). Associations with actin and tubulin have also been reported. The protein may also have a role in the regulation of apoptosis, and interestingly migrates from the cytoplasm into the nucleus when cells become apoptotic (4). The HGNC name for this protein is GAPDH.\n\nApplications:\nSuitable for use in Immunofluorescence and Western Blot. On blots, reveals a prominent ~38kD band, and on cells in tissue culture the antibody stains in a punctate cytoplasmic fashion. Other applications not tested.\n\nRecommended Dilution:\nImmunofluorescence: 1:100\nWestern Blot: 1:1000\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nMay 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.

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SPECIFICATIONS

Catalog Number

031365

Size

500ul

Applications

IF, WB

Hosts

Mouse

Reactivities

Hum, Mouse, Rat, Bov, Prc

Form

Supplied as a liquid in 10mM sodium azide.

P Type

Mab

Purity

Concentrated tissue culture supernatant

Isotype

IgM,k

References

1. Morgenegg G, Winkler GC, Hubscher U, Heizmann CW, Mous J, Kuenzle CC. Glyceraldehyde-3-phosphate dehydrogenase is a nonhistone protein and a possible activator of transcription in neurons. J Neurochem. 47:54-62 1986\n\n2. Schulze H, Schuler A, Stuber D, Dobeli H, Langern H & Huber G. Rat brain glyceraldehyde-3-phosphate dehydrogenase interacts with the recombinant cytoplasmic domain of Alzheimer's beta-amyloid precursor protein. J Neurochem. 60:1915-22 1993\n\n3. Burke JR, Enghild JJ, Martin ME, Jou Y-S, Myers RM, Roses AD, Vance JM & Strittmatter WJ. Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH. Nature Med. 2: 347-350, 1996. \n\n4. Dastoor Z. & Dreyer, J-L. Potential role of nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase in apoptosis and oxidative stress. J. Cell Sci. 114:1643-1653 2001.\n\n5. Fortun J, Dunn WA, Joy S, Li J. & Notterpek, L. Emerging Role for Autophagy in the Removal of Aggresomes in Schwann Cells. J. Neurosci. 23:10672-10680 2003.\n\n6. Ellis RC, Earnhardt JN, Hayes RL, Wang KK & Anderson DK. Cathepsin B mRNA and protein expression following contusion spinal cord injury in rats. J Neurochem. 88:689-97 2004.\n\n7. Fortun J, Li J, Go J, Fenstermaker A, Fletcher BS & Notterpek L. Impaired proteasome activity and accumulation of ubiquitinated substrates in a hereditary neuropathy model. J Neurochem. 92:1531-41 2005\n\n8. Fortun J, Li J, Go J, Fenstermaker A, Fletcher BS & Notterpek L. Impaired proteasome activity and accumulation of ubiquitinated substrates in a hereditary neuropathy model. J Neurochem. 93:766-8 2005\n\n9. Iskandar M, Swist E, Trick KD, Wang B, L'Abbe MR, Bertinato J. Copper chaperone for Cu/Zn superoxide dismutase is a sensitive biomarker of mild copper deficiency induced by moderately high intakes of zinc. Nutr J. 4:35 2005\n\n10. Fortun J, Go JC, Li J, Amici SA, Dunn WA Jr, Notterpek L. Alterations in degradative pathways and protein aggregation in a neuropathy model based on PMP22 overexpression. Neurobiol Dis. 22:153-164 2006\n\n11. Amici SA, Dunn WA, Murphy AJ, Adams NC, Gale NW, Valenzuela DM, Yancopoulos GD & Notterpek L.Peripheral Myelin Protein 22 Is in Complex with {alpha}6beta4 Integrin, and Its Absence Alters the Schwann Cell Basal Lamina. J. Neurosci. 26:1179-89 2006\n\n12. Amici SA, Dunn WA & Notterpek, L. Developmental abnormalities in the nerves of peripheral myelin protein 22-deficient mice. J. Neurosci. Res. 85:238-249 2006\n\n13. Felitsyn N, Stacpoole, PW & Nottepek L. Dichloroacetate causes reversible demyelination in vitro: potential mechanism for its neuropathic effect. J. Neurochem 100:429-36 2007\n\n14. Rangaraju S, Madorsky I, Pileggi JG, Kamal A, Notterpek L. Pharmacological induction of the heat shock response improves myelination in a neuropathic model. Neurobiol Dis. 32:105-15 2008\n\n15. Felitsyn N, McLeod C, Shroads AL, Stacpoole PW, Notterpek L. The heme precursor delta-aminolevulinate blocks peripheral myelin formation. J Neurochem. 106:2068-79 2008\n\n16. Lau P, Verrier JD, Nielsen JA, Johnson KR, Notterpek L, Hudson LD. Identification of dynamically regulated microRNA and mRNA networks in developing oligodendrocytes. J Neurosci. 28:11720-30 2008\n\n17. Verrier JD, Lau P, Hudson L, Murashov AK, Renne R, Notterpek L. Peripheral myelin protein 22 is regulated post-transcriptionally by miRNA-29a. Glia 57:1265-79 2009\n\n18. Rangaraju S, Hankins D, Madorsky I, Madorsky E, Lee WH, Carter CS, Leeuwenburgh C, Notterpek L.Molecular architecture of myelinated peripheral nerves is supported by calorie restriction with aging. Aging Cell. 8:178-91 2009\n\n19. Madorsky I, Opalach K, Waber A, Verrier JD, Solmo C, Foster T, Dunn WA Jr, Notterpek L. Intermittent fasting alleviates the neuropathic phenotype in a mouse model of Charcot-Marie-Tooth disease. Neurobiol Dis. 34:146-54 2009\n\n20. Opalach K, Rangaraju S, Madorsky I, Leeuwenburgh C, Notterpek L. Lifelong calorie restriction alleviates age-related oxidative damage in peripheral nerves. Rejuvenation Res. 13:65-74 2010.\n\n21. Verrier JD, Semple-Rowland S, Madorsky I, Papin JE, Notterpek L. Reduction of Dicer impairs Schwann cell differentiation and myelination. J. Neurosci Res. 88:2558-68 2010.\n\n22. Zeier Z, Madorsky I, Xu Y, Ogle WO, Notterpek L, Foster TC. Gene Expression in the Hippocampus: Regionally Specific Effects of Aging and Caloric Restriction. Mech Ageing Dev. 132:8-19 2011\n\n23. Verrier JD, Madorsky I, Coggin WE, Geesey M, Hochman M, Walling E, Daroszewski D, Eccles KS, Ludlow R, Semple-Rowland SL. Bicistronic lentiviruses containing a viral 2A cleavage sequence reliably co-express two proteins and restore vision to an animal model of LCA1. PLoS One. 6:e20553 2011\n\n24. Lee WH, Kumar A, Rani A, Herrera J, Xu J, Someya S, Foster TC. Influence of viral vector-mediated delivery of superoxide dismutase and catalase to the hippocampus on spatial learning and memory during aging. Antioxid Redox Signal. 16:339-50 2012\n\n25. Kumar A, Rani A, Tchigranova O, Lee WH, Foster TC. Influence of late-life exposure to environmental enrichment or exercise on hippocampal function and CA1 senescent physiology. Neurobiol Aging. 2011 Aug 3. [Epub ahead of print]

Additional Info

Recognizes GAPDH from human, bovine, porcine, mouse, rat and other mammals, and also recognizes avian GAPDH. Since GAPDH is one of the most conserved proteins known, it is likely that the antibody is effective on other species also.