PRKAR2B Polyclonal Antibody (E-AB-90471)
For research use only.
| Verified Samples |
Verified Samples in WB: various cell lines |
| Dilution | WB 1:500-1:2000 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human, Mouse |
| Applications | WB |
| Clonality | Polyclonal |
| Immunogen | Recombinant fusion protein of human PRKAR2B |
| Abbre | PRKAR2B |
| Synonyms | PRKAR2, PRKAR2B, RII-BETA |
| Swissprot | |
| Calculated MW | 46 kDa |
| Observed MW |
50 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. |
| Concentration | 1 mg/mL |
| Buffer | Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer and 50% glycerol. |
| Purification Method | Affinity purification |
| Research Areas | Cancer, Signal Transduction |
| 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 | cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits have been identified in humans. The protein encoded by this gene is one of the regulatory subunits. This subunit can be phosphorylated by the activated catalytic subunit. This subunit has been shown to interact with and suppress the transcriptional activity of the cAMP responsive element binding protein 1 (CREB1) in activated T cells. Knockout studies in mice suggest that this subunit may play an important role in regulating energy balance and adiposity. The studies also suggest that this subunit may mediate the gene induction and cataleptic behavior induced by haloperidol. |
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}}
