DS-PB-00847 recognizes an epitope within the C-terminal region (CT) of Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a glycolytic enzyme which plays a key role in energy production, and has also been implicated in numerous cellular processes. GAPDH is a homotetramer molecule consisting of four 36kDa subunits, constitutively expressed in most cells and tissues, and is responsible for the generation of energy during carbohydrate metabolism, catalyzing the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate. The role of GAPDH as a multifunctional protein has emerged from many studies, confirming its involvement in critical nuclear pathways, apoptosis, membrane transport and fusion, DNA replication and repair and phosphotransferase activity. Furthermore, the ability of GAPDH to bind with high affinity to beta-amyloid precursor protein (Alzheimer's disease) and selectively with CAG mutated proteins, including huntingtin (Huntingdon's disease) and the androgen receptor (spinobulbar muscular atrophy), has focused many studies towards the role of GAPDH in the pathogenesis of neurodegenerative diseases (1). Western BlotDS-PB-00847 detects a band of approximately 37kDa in HeLa cell lysates.
交叉反应
小鼠, 大鼠
纯化方法
Purified
免疫原
Antisera to human GAPDH (CT) were raised by repeated immunisation of rabbits with highly purified antigen.Purified IgG prepared by affinity chromatography.