This antibody recognises glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a 36 kDa protein whose main function is to catalyse the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate, in conjunction with inorganic phosphate and nicotinamide adenine dinucleotide (NAD). This reaction is an important energy yielding step in carbohydrate metabolism. GAPDH has also been shown to translocate to the nucleus under a variety of stressors, most of which are associated with oxidative stress, whereby it mediates cell death. GAPDH binds to several proteins responsible for neurodegenerative diseases, such as amyloid precursor protein and Huntingtin.
Applications
WB, ELISA, IF, IHC-Fr, IP
Reactivity
Human, Bovine, Pig, Goat, Cat, Rat, Mouse, Dog, Rabbit, Fish
Immunogen
Human cardiac muscle GADPH.
Host
Mouse
Clonality
Monoclonal
Clone ID
4G5
Isotype
IgG1
Conjugate
Unconjugated
Purification
Protein A affinity chromatography of ascites.
Concentration
1 mg/ml
Product Form
Liquid
Formulation
Supplied in Phosphate Buffered Saline with <0.1% Sodium Azide.
Storage
Shipped at ambient temperature. Upon delivery aliquot and store at -20°C. When thawed, aliquot the sample as needed. Short term (up to 4 weeks): store at 4°C. Long term: store at -20°C. Avoid freeze / thaw cycles. Storage in frost free freezers is not recommended.
General Notes
Mouse anti Human GAPDH antibody, clone 4G5 recognizes glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a 36 kDa protein whose main function is to catalyse the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate, in conjunction with inorganic phosphate and nicotinamide adenine dinucleotide (NAD). This reaction is an important energy yielding step in carbohydrate metabolism. GAPDH has also been shown to translocate to the nucleus under a variety of stressors, most of which are associated with oxidative stress, whereby it mediates cell death (Chuang & Ishitani 1996). GAPDH binds to several proteins responsible for neurodegenerative diseases, such as amyloid precursor protein and Huntingtin (Burke et al. 1996).