SENP6 Polyclonal Antibody (E-AB-91862)

For research use only.
Verified Samples |
Verified Samples in WB: various cell lines |
Dilution | WB 1:500-1:2000 |
Isotype | IgG |
Host | Rabbit |
Reactivity | Rat |
Applications | WB |
Clonality | Polyclonal |
Immunogen | Recombinant fusion protein of human SENP6 |
Abbre | SENP6 |
Synonyms | SENP6, SSP1, SUSP1 |
Swissprot | |
Observed MW |
126 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, cytosol, nucleoplasm, nucleus. |
Concentration | 1 mg/mL |
Buffer | Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer and 50% glycerol. |
Purification Method | Affinity purification |
Research Areas | Cell Biology, 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 | Ubiquitin-like molecules (UBLs), such as SUMO1 (UBL1; MIM 601912), are structurally related to ubiquitin (MIM 191339) and can be ligated to target proteins in a similar manner as ubiquitin. However, covalent attachment of UBLs does not result in degradation of the modified proteins. SUMO1 modification is implicated in the targeting of RANGAP1 (MIM 602362) to the nuclear pore complex, as well as in stabilization of I-kappa-B-alpha (NFKBIA; MIM 164008) from degradation by the 26S proteasome. Like ubiquitin, UBLs are synthesized as precursor proteins, with 1 or more amino acids following the C-terminal glycine-glycine residues of the mature UBL protein. Thus, the tail sequences of the UBL precursors need to be removed by UBL-specific proteases, such as SENP6, prior to their conjugation to target proteins (Kim et al., 2000 [PubMed 10799485]). SENPs also display isopeptidase activity for deconjugation of SUMO-conjugated substrates (Lima and Reverter, 2008 [PubMed 18799455]).[supplied by OMIM, Jun 2009] |
Other Clones
{{antibodyDetailsPage.numTotal}} Results
-
{{item.title}}
Citations ({{item.publications_count}}) Manual MSDS
Cat.No.:{{item.cat}}
{{index}} {{goods_show_value}}
Other Formats
{{formatDetailsPage.numTotal}} Results
Unconjugated
-
{{item.title}}
Citations ({{item.publications_count}}) Manual MSDS
Cat.No.:{{item.cat}}
{{index}} {{goods_show_value}}
-
IF:{{item.impact}}
Journal:{{item.journal}} ({{item.year}})
DOI:{{item.doi}}Reactivity:{{item.species}}
Sample Type:{{item.organization}}
-
Q{{(FAQpage.currentPage - 1)*pageSize+index+1}}:{{item.name}}