PSMD12 Polyclonal Antibody (E-AB-52752)
For research use only.
| Verified Samples |
Verified Samples in WB: Human cerebrum Verified Samples in IHC: Human tonsil, Human esophagus cancer |
| Dilution | WB 1:1000-1:5000, IHC 1:50-1:300 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | WB, IHC |
| Clonality | Polyclonal |
| Immunogen | Fusion protein of human PSMD12 |
| Abbre | PSMD12 |
| Synonyms | 26S proteasome non-ATPase regulatory subunit 12, 26S proteasome regulatory subunit RPN5, 26S proteasome regulatory subunit p55, MGC75406, PSD12, PSMD12, Proteasome 26S non ATPase subunit 12 isoform 2, R, macropain) 26S subunit, non ATPase12, p55, proteasome (prosome |
| Swissprot | |
| Calculated MW | 53 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 | Cytosol, Extracellular region or secreted, extracellular exosome, extracellular region, Nucleus, nuclear proteasome complex, nucleoplasm, Other locations: cytoplasm, ficolin-1-rich granule lumen, membrane, proteasome accessory complex, proteasome complex, proteasome regulatory particle, proteasome regulatory particle, lid subcomplex, secretory granule lumen. |
| Concentration | 0.9 mg/mL |
| Buffer | Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer and 50% glycerol. |
| Purification Method | Antigen affinity purification |
| Research Areas | 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 | The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a non-ATPase subunit of the 19S regulator. A pseudogene has been identified on chromosome 3. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. |
Other Clones
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Unconjugated
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