MT-CO3 Polyclonal Antibody (E-AB-91951)
For research use only.
| Verified Samples |
Verified Samples in WB: Mouse kidney |
| Dilution | WB 1:500-1:2000 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | WB |
| Clonality | Polyclonal |
| Immunogen | A synthetic peptide of human MT-CO3 |
| Abbre | MT-CO3 |
| Synonyms | COIII, COX3, MT-CO3, MTCO3 |
| Swissprot | |
| Calculated MW | 30 kDa |
| Observed MW |
30 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 | Mitochondrial inner membrane, mitochondrial respiratory chain complex IV, mitochondrion. |
| Concentration | 1 mg/mL |
| Buffer | Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer and 50% glycerol. |
| Purification Method | Affinity purification |
| Research Areas | Cardiovascular, Signal Transduction, Cell Biology, Cancer, Metabolism |
| 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 | Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII, ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII and cytochrome c oxidase (complex IV, CIV, that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS are transferred via the dinuclear copper A center (CU(A of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC formed by heme A3 and copper B (CU(B. The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. |
Other Clones
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Unconjugated
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