Pyruvate dehydrogenase (PDH) is a mitochondrial multienzyme complex that catalyzes the oxidative decarboxylation of pyruvate and is one of the major enzymes responsible for the regulation of homeostasis of carbohydrate fuels in mammals. The enzymatic activity is regulated by a phosphorylation/dephosphorylation cycle. Phosphorylation of PDH by a specific pyruvate dehydrogenase kinase (PDK) results in inactivation. Multiple alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jun 2013]
Host
Rabbit
Immunogen
The antiserum was produced against synthesized phosphopeptide derived from human PDK1 around the phosphorylation site of serine 241 (A-N-SP-F-V).
Quantity
100 µg
Reactivity
Rat, Mouse, Human
Recombinant
FALSE
Regulatory
RUO
Shipping Condition
Ice Packs
Buffer
phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Concentration
1µg/ul
Description
Specificity: PDK1 (phospho-Ser241) antibody detects endogenous levels of PDK1 only when phosphorylated at serine 241.
Format
Liquid
Purity
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatogramphy using non-phosphopeptide corresponding to the phosphorylation site.
Storage
This product is stable for several weeks at 4°C as an undiluted liquid. Dilute only prior to immediate use. For extended storage, aliquot contents and freeze at -20°C or below. Avoid cycles of freezing and thawing. Expiration date is one (1) year from date of receipt.