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NB300-221  Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) antibody

see related secondary antibodies
see all 49 Glyceraldehyde-3-Phosphate Dehydrogenase products
0.5 ml / US$ 435 no delivery possible
please contact the manufacturer
Novus Biologicals
Littleton, CO, USA
www.novus-biologicals.com

Quick Overview

Mouse anti Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) -

Synonyms

Loading Control, GAPD, G3P, ,

Product review
Please read our product review about Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH): Antibodies to Loading Controls.

Product Description

Mouse anti Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) -, Presentation: Supernatant. Product is tested for Immunofluorescence ( IF ), Western blot / Immunoblot ( WB )

Properties

ApplicationsImmunofluorescence ( IF ), Western blot / Immunoblot ( WB )
ReactivityMamalia ( Mam ), Avis ( Av )
PresentationSupernatant
HostMouse
IsotypeIgG1
Catalog NumberNB300-221
Swiss Prot. No.P04406
Quantity0.5 ml
PriceUS$ 435 no delivery possible
DeliveryNot USA/Canada
ManufacturerNovus Biologicals Inc.
Datasheetview PDF-Download
NB300-221.pdf

Datasheet Extract

Mouse Monoclonal anti-GAPDH (1D4)
Alternate namesanti-GAPDH antibody, anti-glyceraldehyde-3-phosphate dehydrogenase antibody, anti-HGNC:4141 antibody, anti-G3PD antibody, anti-GAPD antibody, anti-MGC88685 antibody
Concentration1 mg/ml
BackgroundGAPDH is a 146 kDa tetramer composed of four 30-40 kDa subunits. 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 used as standards in studies of mRNA expression. Increasingly, scientists are making use of specific antibodies to GAPDH as loading controls for western blotting experiments. 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 be 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).
ImmunogenThe immunogen used to raise this particular antibody was extensively purified pig GAPDH.

Swiss Num.: P04406
Format
Purification: Tissue culture supernatant
Purity: Tissue culture supernatant
Applicationsimmunofluorescence 1:100, Western Blot 1:1000
Specificity
Species: NB 300-221 reacts with GAPDH from human, cow, pig, mouse, rat and bird. Since GAPDH is one of the most conserved proteins known, it is likely that the antibody
is effective on other species also.
StorageStore at 4C short term. Aliquot and store at -20C long term. Avoid freeze thaw cycles.
References1. 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
2. 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
3. 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.
4. 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.
5. 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. 1. Arthur, D. B., Georgi, S., Akassoglou, K., and Insel, P. A. (2006) Inhibition of Apoptosis by P2Y2 Receptor Activation: Novel Pathways for Neuronal Survival, 26, 3798-3804.
2. Azfer, A., Niu, J., Rogers, L. M., Adamski, F. M., and Kolattukudy, P. E. (2006) Activation of endoplasmic reticulum stress response during the development of ischemic heart disease, 291, H1411-1420.
3. Barry, J. S., Davidsen, M. L., Limesand, S. W., Galan, H. L., Friedman, J. E., Regnault, T. R. H., and Hay, W. W., Jr. (2006) Developmental Changes in Ovine Myocardial Glucose Transporters and Insulin Signaling Following Hyperthermia-Induced Intrauterine Fetal Growth Restriction, 231, 566-575.
4. Block, K., Gorin, Y., Hoover, P., Williams, P., Chelmicki, T., Clark, R. A., Yoneda, T., and Abboud, H. E. (2007) NAD(P)H Oxidases Regulate HIF-2{alpha} Protein Expression, 282, 8019-8026.
5. Dusek, R. L., Getsios, S., Chen, F., Park, J. K., Amargo, E. V., Cryns, V. L., and Green, K. J. (2006) The Differentiation-dependent Desmosomal Cadherin Desmoglein 1 Is a Novel Caspase-3 Target That Regulates Apoptosis in Keratinocytes, 281, 3614-3624.
6. Fatma, S., Yakubov, R., Anwar, K., and Hussain, M. M. (2006) Pluronic L81 enhances triacylglycerol accumulation in the cytosol and inhibits chylomicron secretion, 47, 2422-2432.
7. Jia, Y., and Takimoto, K. (2006) Mitogen-Activated Protein Kinases Control Cardiac KChIP2 Gene Expression, 98, 386-393.
8. Kanadia, R. N., Shin, J., Yuan, Y., Beattie, S. G., Wheeler, T. M., Thornton, C. A., and Swanson, M. S. (2006) Reversal of RNA missplicing and myotonia after muscleblind overexpression in a mouse poly(CUG) model for myotonic dystrophy, 103, 11748-11753.
9. Le Boeuf, F., Houle, F., Sussman, M., and Huot, J. (2006) Phosphorylation of Focal Adhesion Kinase (FAK) on Ser732 Is Induced by Rho-dependent Kinase and Is Essential for Proline-rich Tyrosine Kinase-2-mediated Phosphorylation of FAK on Tyr407 in Response to Vascular Endothelial Growth Factor, 17, 3508-3520.
10. Pisitkun, T., Bieniek, J., Tchapyjnikov, D., Wang, G., Wu, W. W., Shen, R.-F., and Knepper, M. A. (2006) High-throughput identification of IMCD proteins using LC-MS/MS, 25, 263-276.
11. Redman, P. T., He, K., Hartnett, K. A., Jefferson, B. S., Hu, L., Rosenberg, P. A., Levitan, E. S., and Aizenman, E. (2007) Apoptotic surge of potassium currents is mediated by p38 phosphorylation of Kv2.1, 104, 3568-3573.
12. Shibata, Y., Gabbard, J., Yamashita, M., Tsuji, S., Smith, M., Nishiyama, A., Henriksen, R. A., and Myrvik, Q. N. (2006) Heat-killed BCG induces biphasic cyclooxygenase 2+ splenic macrophage formation--role of IL-10 and bone marrow precursors, 80, 590-598.
13. Fatma, S., Yakubov, R., Anwar, K. and Hussain, M.M. (2006) Pluronic L81 enhances triacylglycerol accumulation in the cytosol and inhibits chylomicron secretion, J. Lipid Res., 47, 2422-2432.
14. Porchia, L.M. et al. 2-Amino-N-{4-[5-(2-phenanthrenyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]-phenyl} Acetamide (OSU-03012), a Celecoxib Derivative, Directly Targets p21-Activated Kinase. Mol. Pharmacol. 72:1124-1131, Nov 2007

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