GAPDH Mouse mAb, Loading Contr

Not yet tested in other applications.
Optimal working dilutions must be determined by the end user.

Cancer > Cancer Metabolism > Metabolic signaling pathway > Metabolism of carbohydrates

Isotype/Loading Controls > Loading Controls > GAPDH

Metabolism > Pathways and Processes > Metabolic signaling pathways > Carbohydrate metabolism

Metabolism > Pathways and Processes > Metabolic signaling pathways > Energy transfer pathways > Energy Metabolism

Metabolism > Types of disease > Cancer

Metabolism > Types of disease > Neurodegenerative disease

Neuroscience > Neurology process > Neurodegenerative disease > Alzheimer's disease

Neuroscience > Neurology process > Neurodegenerative disease > Huntington's disease

Signal Transduction > Metabolism > Energy Metabolism

Homotetramer (PubMed:16239728, PubMed:16510976).
Interacts with TPPP; the interaction is direct (By similarity).
Interacts (when S-nitrosylated) with SIAH1; leading to nuclear translocation (By similarity).
Interacts with RILPL1/GOSPEL, leading to prevent the interaction between GAPDH and SIAH1 and prevent nuclear translocation (By similarity).
Interacts with CHP1; the interaction increases the binding of CHP1 with microtubules (By similarity).
Associates with microtubules (By similarity).
Interacts with EIF1AD, USP25, PRKCI and WARS1 (PubMed:11724794, PubMed:16501887, PubMed:15628863, PubMed:20644585).
Interacts with phosphorylated RPL13A; inhibited by oxidatively-modified low-densitity lipoprotein (LDL(ox)) (PubMed:22771119).
Component of the GAIT complex (PubMed:15479637).
Interacts with FKBP6; leading to inhibit GAPDH catalytic activity (PubMed:19001379).
Interacts with TRAF2, promoting TRAF2 ubiquitination (PubMed:23332158).
Interacts with TRAF3, promoting TRAF3 ubiquitination (PubMed:27387501).

Cytoplasm, cytosol. Nucleus. Cytoplasm, perinuclear region. Membrane. Note=Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal. Postnuclear and Perinuclear regions.

#Acetylation

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively (PubMed:3170585, PubMed:11724794).
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:3170585, PubMed:11724794).
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).