Recombinant Pyruvate Dehydrogenase E1 α Monoclonal Antibody (AN301007L)
For research use only.
| Verified Samples |
Verified Samples in WB: HEK293 Verified Samples in IHC: Human kidney tissue, Mouse kidney tissue |
| Dilution | IHC 1:200-1:1000, WB 1:1000-1:5000 |
| Isotype | IgG,κ |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | WB, IHC |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant Human Pyruvate Dehydrogenase E1 α protein |
| Abbre | Pyruvate Dehydrogenase E1 α |
| Synonyms | PDHA1, PDHA, PDHAD, PDHCE1A, PHE1A, E1 alpha polypeptide 1, mitochondrial, ODPA, PDH, PDHE1 A type I, PDHE1-A type I, PDHα, Pyruvate Dehydrogenase (lipoamide) alpha 1, Pyruvate dehydrogenase complex, Pyruvate Dehydrogenase E1 alpha, Pyruvate dehydrogenase E1 component subunit alpha, somatic form |
| Swissprot | |
| Calculated MW | 43 kDa |
| Observed MW |
43 kDa
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Cellular Localization | Mitochondrion matrix |
| Concentration | 0.2 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A |
| Research Areas | Signal Transduction, Cancer, Metabolism |
| Clone No. | 1A5 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | 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. |
Other Clones
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Unconjugated
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