Monoclonal Anti-GAPDH−Peroxidase antibody produced in mouse

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.

rabbit GAPDH.

Monoclonal Anti-GAPDH-Peroxidase antibody produced in mouse has been used in

• immunoblotting
• enzyme linked immunosorbent assay (ELISA)
• immunocytochemistry

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.

The antibody does not crossreact with non-vertebrate and prokaryote GAPDH.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 0.05% MIT.

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