Recombinant human GAPDH protein (Active) is a Human Full Length protein, in the 1 to 335 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, FuncS.
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively (PubMed:11724794, PubMed:3170585). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (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).
GAPD, CDABP0047, OK/SW-cl.12, GAPDH, Glyceraldehyde-3-phosphate dehydrogenase, Peptidyl-cysteine S-nitrosylase GAPDH
Recombinant human GAPDH protein (Active) is a Human Full Length protein, in the 1 to 335 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, FuncS.
1 unit of GAPDH is the amount of enzyme that will catalyze 1 μmol of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate at pH 8.0 and 37°C.
pH: 7.4
Constituents: 10.269% Trehalose, 0.727% Dibasic monohydrogen potassium phosphate, 0.248% Potassium phosphate monobasic
Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively (PubMed:11724794, PubMed:3170585). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (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).
Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
S-nitrosylation of Cys-152 leads to interaction with SIAH1, followed by translocation to the nucleus (By similarity). S-nitrosylation of Cys-247 is induced by interferon-gamma and LDL(ox) implicating the iNOS-S100A8/9 transnitrosylase complex and seems to prevent interaction with phosphorylated RPL13A and to interfere with GAIT complex activity (PubMed:22771119, PubMed:25417112).
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Glyceraldehyde-3-phosphate dehydrogenase commonly known as GAPDH is an enzyme involved in glycolysis. Its molecular weight (MW) is approximately 36 kDa. The protein is expressed ubiquitously in almost all tissues reflecting its essential role in energy production. GAPDH catalyzes the sixth step of glycolysis converting glyceraldehyde-3-phosphate into 13-bisphosphoglycerate. Due to its stable expression researchers often use GAPDH as a loading control in western blot experiments.
GAPDH serves important metabolic functions beyond its enzymatic role in glycolysis. It functions as part of a multi-enzyme complex within the cytoplasm which facilitates efficient substrate channeling during glycolysis. Additionally GAPDH has non-glycolytic roles including involvement in nuclear processes like RNA export and DNA repair. Its ubiquitous presence across different cellular compartments indicates its multiple functions beyond metabolic pathways.
GAPDH integrates into significant cellular functions like the glycolytic pathway and apoptotic pathways. In glycolysis GAPDH collaborates with enzymes like phosphoglycerate kinase forming a cohesive link in the energy conversion chain. Its participation in apoptotic pathways highlights GAPDH's involvement in cellular death processes interacting with proteins like Bcl-2 to influence apoptosis progression. These roles reinforce its presence in central metabolic and regulatory pathways.
GAPDH has associations with neurodegenerative diseases and cancer. In neurodegenerative disorders such as Alzheimer's disease GAPDH’s altered enzymatic activity is frequently observed influencing cellular energy homeostasis. Moreover overexpression or aberrant regulation of GAPDH relates to cancer cell proliferation and metastasis implicating proteins like p53 in these pathways. The diverse functions and interactions of GAPDH emphasize its importance in both normal cellular function and disease states.
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Functional analysis of ab291253.
Specific activity is ≥ 100 U/mg when assayed in 100 mM Hepes pH 8.0, 10 mM NaH2PO4, 0.1% NP-40 at 37°C for 30 minutes
SDS-PAGE (4-20% gel) analysis of ab291253 under reducing conditions.
Lane 1: 2.5 μg
Lane 2: 5 μg
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