Description : |
The pyruvate dehydrogenase (PDH) complex is a nuclear-encoded mitochondrial multienzyme complex that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and provides the primary link between glycolysis and the tricarboxylic acid (TCA) cycle. The PDH complex is composed of multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). The E1 enzyme is a heterotetramer of two alpha and two beta subunits. This gene encodes the E1 alpha 1 subunit containing the E1 active site, and plays a key role in the function of the PDH complex. Mutations in this gene are associated with pyruvate dehydrogenase E1-alpha deficiency and X-linked Leigh syndrome. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. |
Source : |
HEK293 |
Species : |
Human |
Tag : |
Myc/DDK |
Molecular Mass : |
43.3 kDa |
AA Sequence : |
MRKMLAAVSRVLSGASQKPASRVLV ASRNFANDATFEIKKCDLHRLEEGP PVTTVLTREDGLKYYRMMQTVRRME LKADQLYKQKIIRGFCHLCDGQEAC CVGLEAGINPTDHLITAYRAHGFTF TRGLSVREILAELTGRKGGCAKGKG GSMHMYAKNFYGGNGIVGAQVPLGA GIALACKYNGKDEVCLTLYGDGAAN QGQIFEAYNMAALWKLPCIFICENN RYGMGTSVERAAASTDYYKRGDFIP GLRVDGMDILCVREATRFAAAYCRS GKGPILMELQTYRYHGHSMSDPGVS YRTREEIQEVRSKSDPIMLLKDRMV NSNLASVEELKEIDVEVRKEIEDAA QFATADPEPPLEELGYHIYSSDPPF EVRGANQWIKFKSVSTRTRPLEQKL ISEEDLAANDILDYKDDDDKV |
Purity : |
> 80% as determined by SDS-PAGE and Coomassie blue staining |
Stability : |
Stable for 3 months from receipt of products under proper storage and handling conditions. |
Storage : |
Store at -80 centigrade. Avoid repeated freeze-thaw cycles. |
Concentration : |
50 μg/mL as determined by BCA |
Storage Buffer : |
100 mM glycine, 25 mM Tris-HCl, pH 7.3. |