CUL4A Polyclonal Antibody (E-AB-19279)
For research use only.
| Verified Samples |
Verified Samples in WB: 231, HepG2 Verified Samples in IHC: Human esophagus cancer, Human thyroid cancer |
| Dilution | WB 1:500-1:2000, IHC 1:50-1:300 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human, Mouse |
| Applications | WB, IHC |
| Clonality | Polyclonal |
| Immunogen | Synthetic peptide of human CUL4A |
| Abbre | CUL4A |
| Synonyms | 2810470J21Rik, AW495282, CUL 4A, CUL-4A, CUL4A, Cul4a, Cul4a protein, Cullin-4A, MGC36573, MGC64071 |
| Swissprot | |
| Calculated MW | 88 kDa |
| Observed MW |
Refer to figures
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 | Nucleus, nucleoplasm, Other locations: Cul4-RING E3 ubiquitin ligase complex, Cul4A-RING E3 ubiquitin ligase complex. |
| Concentration | 1.62 mg/mL |
| Buffer | Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer and 50% glycerol. |
| Purification Method | Antigen affinity purification |
| Research Areas | Cancer, Cell Biology |
| 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 | Cullin proteins assemble a large number of RING E3 ubiquitin ligases,participating in the proteolysis through the ubiquitin-proteasome pathway. Two cullin 4 (CUL4) proteins,CUL4A (87 kDa) and CUL4B(104 kDa),have been identified. The two CUL4 sequences are 83% identical. They target certain proteins for degradation by binding protein DDB1 to form a CUL4-DDB1 ubiquitin ligase complex with DDB. They form two individual E3 ligases,DDB1-CUL4ADDB2 and DDB1-CUL4BDDB2 in this process. CUL4A appeared in both the nucleus and the cytosol,suggesting a more complex mechanism for entering the nucleus. CUL4B is localized in the nucleus and facilitates the transfer of DDB1 into the nucleus independently of DDB2. |
Other Clones
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Unconjugated
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