GAPDH Antibody
Purified Mouse Monoclonal Antibody
- 产品详情
- 实验流程
Application
| WB, IHC, ICC, E |
|---|---|
| Primary Accession | P04406 |
| Reactivity | Human |
| Host | Mouse |
| Clonality | Monoclonal |
| Clone Names | 1A10 |
| Isotype | IgG1 |
| Calculated MW | 36053 Da |
| Description | Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is well known as one of the key enzymes involvedin glycolysis. It catalyzes an important energy-yielding step in carbohydrate metabolism, the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate in the presence of inorganic phosphate and nicotinamide adenine dinucleotide (NAD). The enzyme exists as a tetramer of identical chains. Besides its functioning as a glycolytic enzyme in cytoplasm, recent evidence suggest that mammalian GAPDH is also involved in a great number of intracellular proceses such as membrane fusion, microtubule bundling, phosphotransferase activity, nuclear RNA export, DNA replication, and DNA repair. During the last decade a lot of findings appeared concerning the role of GAPDH in different pathologies including prostate cancer progression, programmed neuronal cell death, age-related neuronal diseases, such as Alzheimer’s and Huntington’s disease. |
| Immunogen | Purified recombinant fragment of human GAPDH expressed in E. Coli. |
| Formulation | Ascitic fluid containing 0.03% sodium azide. |
| Gene ID | 2597 |
|---|---|
| Other Names | Glyceraldehyde-3-phosphate dehydrogenase, GAPDH, 1.2.1.12, Peptidyl-cysteine S-nitrosylase GAPDH, 2.6.99.-, GAPDH, GAPD |
| Dilution | WB~~1/500 - 1/2000 IHC~~1/200 - 1/1000 ICC~~N/A E~~N/A |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | GAPDH Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| Name | GAPDH {ECO:0000303|PubMed:2987855, ECO:0000312|HGNC:HGNC:4141} |
|---|---|
| Function | Catalyzes the conversion of D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate in glycolysis and the reverse reaction in gluconeogenesis (PubMed:11724794, PubMed:3170585). Also shows nitrosylase activity, thereby playing a role in nuclear functions (PubMed:11724794, PubMed:3170585). Modulates the organization and assembly of the cytoskeleton (By similarity). Facilitates the CHP1- dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes (PubMed:23071094). Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation (PubMed:23071094). Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively (PubMed:23332158, PubMed:27387501). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis (By similarity). Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity). |
| Cellular Location | Cytoplasm, cytosol. Nucleus {ECO:0000250|UniProtKB:P04797}. Cytoplasm, perinuclear region. Membrane Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P04797} Note=Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal (By similarity). Postnuclear and Perinuclear regions (PubMed:12829261) {ECO:0000250|UniProtKB:P04797, ECO:0000269|PubMed:12829261} |
Research Areas
Application Protocols
Provided below are standard protocols that you may find useful for product applications.
REFERENCES
1. Allen R.W. J. Biol. Chem. 1987.262:649-653. 2. Sumner CJ. Ann Neurol 2003.54:6 47-54.
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