Recombinant MTCO2 Monoclonal Antibody (AN301103L)
For research use only.
| Verified Samples |
Verified Samples in WB: Hela, MCF7 Verified Samples in IHC: Human kidney tissue |
| Dilution | IHC 1:200-1000, WB 1:1000-5000 |
| Isotype | IgG,κ |
| Host | Rabbit |
| Reactivity | Human |
| Applications | WB, IHC |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant Human MTCO2 rabbit protein |
| Abbre | MTCO2 |
| Synonyms | COX, Mtco, Cytochrome c oxidase subunit, MT-CO, MT CO, MT-CO2, COII, MTCO2, COX2, Cytochrome c oxidase II, Cytochrome c oxidase polypeptide II, Cytochrome c oxidase subunit 2, MT CO2, COXII, COX2, COX2, COXII, Cytochrome c oxidase II, MT-CO2, COII, COX2 |
| Swissprot | |
| Calculated MW | 26 kDa |
| Observed MW |
21 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 | Cytoplasmic |
| 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. | 10F7 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Cofactor:Copper A.,disease:Defects in MT-CO2 are a cause of cytochrome c oxidase deficiency (COX deficiency) [MIM:220110]; also called mitochondrial complex IV deficiency. COX deficiency is a clinically heterogeneous disorder. The clinical features are ranging from isolated myopathy to severe multisystem disease, with onset from infancy to adulthood.,disease:Defects in MT-CO2 are associated with tumor formation.,Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1.,similarity:Belongs to the cytochrome c oxidase subunit 2 family. |
Other Clones
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Unconjugated
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