Recombinant UBA52 Monoclonal Antibody (AN300653L)
For research use only.
| Verified Samples | Verified Samples in WB: Jurkat |
| Dilution | WB 1:2000-1:10000 |
| Isotype | IgG,κ |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant Human UBA52 protein |
| Abbre | UBA52 |
| Synonyms | Uba, UBCEP, UBCEP2, UBA52, 60S ribosomal protein L40, CEP52, HUBCEP52, L40, MGC126879, MGC57125, RPL40, UBA 52, Ubiquitin 52 amino acid fusion protein, Ubiquitin 60S ribosomal protein L40, Ubiquitin A 52 residue ribosomal protein fusion product 1, Ubiquitin A-52 residue ribosomal protein fusion product 1, Ubiquitin carboxyl extension protein 52, Ubiquitin CEP52, Ribosomal Protein L40 |
| Swissprot | |
| Calculated MW | 15 kDa |
| Observed MW |
10 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 | Cytoplasm, Nucleus, Cytoplasm. |
| Concentration | 0.2 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A |
| Research Areas | Epigenetics and Nuclear Signaling, Cell Biology, Neuroscience |
| Clone No. | 9F3 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Ubiquitin is a highly conserved nuclear and cytoplasmic protein that has a major role in targeting cellular proteins for degradation by the 26S proteosome. It is also involved in the maintenance of chromatin structure, the regulation of gene expression, and the stress response. Ubiquitin is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin moiety fused to an unrelated protein. This gene encodes a fusion protein consisting of ubiquitin at the N terminus and ribosomal protein L40 at the C terminus, a C-terminal extension protein (CEP). Multiple processed pseudogenes derived from this gene are present in the genome. |
Other Clones
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Unconjugated
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