PDP1 Polyclonal Antibody (E-AB-90879)

For research use only.
Verified Samples |
Verified Samples in WB: various cell lines Verified Samples in IF: L929 |
Dilution | WB 1:500-1:2000, IF 1:50-1:200 |
Isotype | IgG |
Host | Rabbit |
Reactivity | Human, Mouse, Rat |
Applications | WB, IF |
Clonality | Polyclonal |
Immunogen | Recombinant fusion protein of human PDP1 |
Abbre | PDP1 |
Synonyms | PDH, PDP, PDP1, PDPC, PPM2A, PPM2C |
Swissprot | |
Calculated MW | 61 kDa/63 kDa |
Observed MW |
61 kDa
The actual band is not consistent with the expectation.
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 | 1 mg/mL |
Buffer | Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer and 50% glycerol. |
Purification Method | Affinity purification |
Research Areas | Cancer, Metabolism, Signal Transduction |
Conjugation | Unconjugated |
Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
Shipping | The product is shipped with ice pack,upon receipt,store it immediately at the temperature recommended. |
background | Pyruvate dehydrogenase (E1) is one of the three components (E1, E2, and E3) of the large pyruvate dehydrogenase complex. Pyruvate dehydrogenase kinases catalyze phosphorylation of serine residues of E1 to inactivate the E1 component and inhibit the complex. Pyruvate dehydrogenase phosphatases catalyze the dephosphorylation and activation of the E1 component to reverse the effects of pyruvate dehydrogenase kinases. Pyruvate dehydrogenase phosphatase is a heterodimer consisting of catalytic and regulatory subunits. Two catalytic subunits have been reported; one is predominantly expressed in skeletal muscle and another one is is much more abundant in the liver. The catalytic subunit, encoded by this gene, is the former, and belongs to the protein phosphatase 2C (PP2C) superfamily. Along with the pyruvate dehydrogenase complex and pyruvate dehydrogenase kinases, this enzyme is located in the mitochondrial matrix. Mutation in this gene causes pyruvate dehydrogenase phosphatase deficiency. Multiple alternatively spliced transcript variants encoding different isoforms have been identified. |
Other Clones
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Other Formats
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Unconjugated
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