Human PDHA1 protein (Recombinant) (N-His) (STJP003846)
SPECIFICATIONS
HostE.coli
ImmunogenHomo sapiens (Human)
General Information
| Short Description | Recombinant-Human PDHA1-N-His protein was developed from e.coli for the region N-His. For use in research applications. |
| Applications | ELISA/Immunogen/SDS-PAGE/WB |
| Host | E.coli |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Dilution Range | Reconstitute in sterile water for a stock solution. |
| Formulation | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
| Storage Instruction | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at-20 to-80°C for twelve months from the date of receipt. |
Target Information
| Gene Symbol | PDHA1 |
| Gene ID | 5160 |
| Uniprot ID | ODPA_HUMAN |
| Immunogen | Homo sapiens (Human) |
| Immunogen Region | Phe30-Ser390 |
Additional Info
| Post Translational Modifications | Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme.for this phosphorylation at a single site is sufficient. Dephosphorylation at all three sites, i.e. at Ser-232, Ser-293 and Ser-300, is required for reactivation. Acetylation alters the phosphorylation pattern. Deacetylated by SIRT3. |
| Function | The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle. |
| Protein Name | Pyruvate Dehydrogenase E1 Component Subunit Alpha - Somatic Form - MitochondrialPdhe1-A Type I |
| Database Links | Reactome: R-HSA-204174Reactome: R-HSA-5362517Reactome: R-HSA-9837999Reactome: R-HSA-9861559 |
| Cellular Localisation | Mitochondrion Matrix |
| Alternative Protein Names | Pyruvate Dehydrogenase E1 Component Subunit Alpha - Somatic Form - Mitochondrial proteinPdhe1-A Type I proteinPDHA1 proteinPHE1A protein |
Information sourced from Uniprot.org