GAPDH Positive Control for STJ501278 peptide (STJ505881)

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STJ505881-5

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Applications: WB
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: GAPDH Positive Control for STJ501278 is synthetically produced from the sequence and is suitable for use in western blot applications.
Formulation: Provided as 100 uL ready-to-use, in SDS-PAGE sample buffer (Laemelli's buffer) containing Tris, pH 6.8, 1 % SDS, Glycerol and Bromophenolblue blue as tracking dye. The sample is reduced by adding 2% beta mercaptoethanol. The protein concentration is
Storage Instruction: Store at-20°C for long term storage. Avoid freeze-thaw cycles.
Gene Symbol: Gapdh
Gene ID: 14433
Uniprot ID: G3P_MOUSE
Specificity: This is positive control is recommended for use in combination with GAPDH antibody STJ501278.
Post Translational Modifications ISGylated. S-nitrosylation of Cys-150 leads to interaction with SIAH1, followed by translocation to the nucleus S-nitrosylation of Cys-245 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. Sulfhydration at Cys-150 increases catalytic activity. Oxidative stress can promote the formation of high molecular weight disulfide-linked GAPDH aggregates, through a process called nucleocytoplasmic coagulation. Succination of Cys-150 and Cys-245 by the Krebs cycle intermediate fumarate, which leads to S-(2-succinyl)cysteine residues, inhibits glyceraldehyde-3-phosphate dehydrogenase activity. Fumarate concentration as well as succination of cysteine residues in GAPDH is significantly increased in muscle of diabetic mammals. It was proposed that the S-(2-succinyl)cysteine chemical modification may be a useful biomarker of mitochondrial and oxidative stress in diabetes and that succination of GAPDH and other thiol proteins by fumarate may contribute to the metabolic changes underlying the development of diabetes complications.
Function Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. 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. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. 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. 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. Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC.
Peptide Name Glyceraldehyde-3-Phosphate Dehydrogenase
Gapdh
Peptidyl-Cysteine S-Nitrosylase Gapdh
Database Links Reactome: R-MMU-70171
Reactome: -MMU-70263
Cellular Localisation Cytoplasm
Cytosol
Cytoskeleton
Nucleus
Translocates To The Nucleus Following S-Nitrosylation And Interaction With Siah1
Which Contains A Nuclear Localization Signal
Colocalizes With Chp1 To Small Punctate Structures Along The Microtubules Tracks
Alternative Peptide Names Glyceraldehyde-3-Phosphate Dehydrogenase protein
Gapdh protein
Peptidyl-Cysteine S-Nitrosylase Gapdh protein
Gapdh protein
Gapd protein

Information sourced from Uniprot.org

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