Anti-GAPDH Antibody, clone 6C5, Alexa Fluor(R) 488 conjugate clone 6C5, from mouse, ALEXA FLUOR(R) 488

Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is an ubiquitous glycolytic enzyme present in reasonably high levels in almost all tissues. The complete and functional enzyme is a tetramer with each of four identical subunits occupying the vertex of a tetrahedron. Its binding domains also include one principally interacting with NAD+ and another interacting with glyceraldehyde 3-phosphate (GAP). As a 'house-keeping' enzyme, it catalyzes the synthesis of 1,3-biphosphoglycerate, a "high energy" intermediate used for the synthesis of ATP. Besides its cytoplasmic role in metabolism, it is also involved in the initial stages of apoptosis or oxidative stress response where it is translocated to the nucleus. Such actions may reflect the role of GAPDH in DNA repair or as one nuclear carrier for apoptotic molecules. GAPDH can also bind specifically to proteins implicated in the pathogenesis of a variety of neurodegenerative disorders, including the beta-amyloid precursor protein and the Huntingtin protein where reduced function of GAPDH is associated with Alzheimer's and Huntington's disease fibroblasts. GAPDH has also been identified as a potential target for nitric oxide (NO)-mediated cellular toxicity.