Human Pyruvate Dehydrogenase Kinase Isozyme 1 (PDK1) Protein

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Description
Pyruvate Dehydrogenase Kinase Isozyme 1 Protein is a recombinant protein kinases.
Documents del producto
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Pyruvate Dehydrogenase Kinase Isozyme 1 (PDK1) |
| Host | E. coli |
| Recommended Dilution | Optimal dilutions/concentrations should be determined by the end user. |
| Origin | Human |
| Expression | Recombinant |
| Purity | > 95% (SDS-PAGE) |
| Size 1 | 10 µg |
| Size 2 | 50 µg |
| Size 3 | 1 mg |
| Form | Liquid |
| Tested Applications | SDS-PAGE |
| Availability | Shipped within 5-10 working days. |
| Dry Ice | No |
| UniProt ID | Q15118 |
| Background | Protein PDK1 |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Plays an important role in cellular responses to hypoxia and is important for cell proliferation under hypoxia. Protects cells against apoptosis in response to hypoxia and oxidative stress.
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Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Plays an important role in cellular responses to hypoxia and is important for cell proliferation under hypoxia. Protects cells against apoptosis in response to hypoxia and oxidative stress.
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