Monoclonal Anti-GAPDH (mouse IgM isotype) is derived from the hybridoma GAPDH-71.1 produced by the fusion of mouse myeloma cells (NS1 cells) and splenocytes from BALB/c mice immunized with rabbit GAPDH.
The gene glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is mapped to human chromosome 12p13. The protein localizes in the cytoplasm but can be translocated to the nucleus depending on cellular conditions.
The antibody does not crossreact with non-vertebrate and prokaryote GAPDH.
Monoclonal Anti-GAPDH-Peroxidase antibody produced in mouse has been used in
- enzyme linked immunosorbent assay (ELISA)
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a tetramer containing identical chains. It catalyzes the reversible oxidative phosphorylation of glyceraldehyde-phosphate, which is a critical energy-yielding step in carbohydrate metabolism. It binds to several proteins including actin, tubulin, amyloid precursor, polyglutamine peptides, DRPLA (dentatorubral-pallidoluysian atrophy), and huntingtin. Protein kinase Cι/λbinds and phosphorylates GAPDH. Phosphorylated GAPDH associates with cytoskeletal elements and controls microtubule dynamics in the early secretory pathway. Poly(ADP-ribose) polymerase-1 (PARP1) interacts with GAPDH and thereby mediates brain damage in the presence of oxidative/nitrosative stress. GAPDH forms a part of OCA-S, the multicomponent OCT1 (octamer-motif-binding factor) coactivator complex, which is involved in the S phase-dependent histone H2B transcription. This association is responsible for linking H2B transcriptional machinery to cell cycle regulation and to the cellular metabolic state. GAPDH is also a component of the functional GAIT (interferon-γ-activated inhibitor of translation) mRNP (messenger ribonucleoprotein). GAPDH expression is dysregulated during melanoma progression.
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 0.05% MIT.
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