RAD23B Polyclonal Antibody (E-AB-52631)
For research use only.
| Verified Samples |
Verified Samples in WB: 293T, HUVEC, Hela Verified Samples in IHC: Human lung cancer |
| Dilution | WB 1:500-1:2000, IHC 1:30-1:150 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human, Rat |
| Applications | WB, IHC |
| Clonality | Polyclonal |
| Immunogen | Fusion protein of human RAD23B |
| Abbre | RAD23B |
| Synonyms | HR 23B, HR23B, RAD 23B, RAD23 (S. cerevisiae) homolog B, RAD23 homolog B, RAD23 homolog B (S. cerevisiae), RAD23 yeast homolog of B, RD23B, Rad23b, UV excision repair protein RAD23 homolog B, XP C repair complementing complex 58 kD, hHR 23b, hHR23B, mHR 23B, mHR23B, p58 |
| Swissprot | |
| Calculated MW | 43 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, Cytoplasm, The intracellular distribution is cell cycle dependent, Localized to the nucleus and the cytoplasm during G1 phase, Nuclear levels decrease during S-phase, upon entering mitosis, relocalizes in the cytoplasm without association with chromatin. |
| Concentration | 0.84 mg/mL |
| Buffer | Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer and 50% glycerol. |
| Purification Method | Antigen affinity purification |
| Research Areas | Cancer, Epigenetics and Nuclear Signaling |
| 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 | The protein encoded by this gene is one of two human homologs of Saccharomyces cerevisiae Rad23, a protein involved in the nucleotide excision repair (NER).This protein was found to be a component of the protein complex that specifically complements the NER defect of xeroderma pigmentosum group C (XP-c) cell extracts in vitro.This protein was also shown to interact with, and elevate the nucleotide excision activity of 3-methyladenine-DNA glycosylase (MPG), which suggested a role in DNA damage recognition in base excision repair.This protein contains an N-terminal ubiquitin-like domain, which was reported to interact with 26S proteasome, and thus this protein may be involved in the ubiquitin mediated proteolytic pathway in cells.Alternative splicing results in multiple transcript variants encoding distinct isoforms. |
Other Clones
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Unconjugated
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