Recombinant NDUFA1 Monoclonal Antibody (AN300778L)
For research use only.
| Verified Samples | Verified Samples in WB: HeLa |
| Dilution | WB 1:1000-5000 |
| Isotype | IgG,κ |
| Host | Rabbit |
| Reactivity | Human |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant Human NDUFA1 protein |
| Abbre | NDUFA1 |
| Synonyms | ZNF, NDUFA, NDUFA1, CI-MWFE, MWFE, ZNF183, B. taurus, CI MWFE, Complex I MWFE, complex I MWFE subunit, Complex I-MWFE, homolog of, NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 1, NADH dehydrogenase (ubiquinone) 1 alpha subcomplex 1 7.5kDa, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1, NADH oxidoreductase subunit MWFE, NADH ubiquinone oxidoreductase (complex 1), NADH ubiquinone oxidoreductase MWFE subunit, NADH-ubiquinone oxidoreductase 1 alpha subcomplex, NADH-ubiquinone oxidoreductase MWFE subunit, NDUA1, NDUFA 1, Type I dehydrogenase, ZNF 183 |
| Swissprot | |
| Observed MW |
8 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 inner membrane; Single-pass membrane protein; Matrix side. |
| Concentration | 0.2 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A |
| Research Areas | Tags & Cell Markers, Signal Transduction, Cancer, Metabolism |
| Clone No. | 5D3 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | The human NDUFA1 gene codes for an essential component of complex I of the respiratory chain, which transfers electrons from NADH to ubiquinone. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha-helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and might act as an anchor for the NADH:ubiquinone oxidoreductase complex at the inner mitochondrial membrane. However, the NDUFA1 peptide is one of about 31 components of the "hydrophobic protein" (HP) fraction of complex I which is involved in proton translocation. Thus the NDUFA1 peptide may also participate in that function. |
Other Clones
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Unconjugated
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