PPIG polyclonal antibody; host Rabbit; reactivity Human, Rat, Mouse
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catalytic activity:Peptidylproline (omega=180) = peptidylproline (omega=0).,domain:The RS domain is required for the interaction with the phosphorylated C-terminal domain of RNA polymerase II.,enzyme regulation:Cyclosporin A (CsA)-sensitive.,function:PPIases accelerate the folding of proteins.,function:PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.,function:PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing.,PTM:Phosphorylated upon DNA damage, probably by ATM or ATR.,similarity:Belongs to the cyclophilin-type PPIase family.,similarity:Contains 1 PPIase cyclophilin-type domain.,subcellular location:Colocalizes with RNA splicing factors at nuclear speckles.,subunit:Interacts with CLK1, PNN and with the phosphorylated C-terminal domain of RNA polymerase II.,tissue specificity:Ubiquitous.,
Fully tested in-house by ABMIUM, or supported by an advanced validation report from a partner reviewed by ABMIUM. Highest confidence. Non-conformities fully supported under the ABMIUM Product Promise.
Quality verified. Independent collaborator or expected-performance data available. Product meets ABMIUM quality standards.
Expected to work based on structural and biochemical data. Not yet directly tested by ABMIUM or a collaborator. No non-conformity support for this combination.
Not recommended for this application or species/sample combination. This may indicate either evidence of unsuitability or that the combination has not been tested and therefore cannot currently be recommended.
Evidence status by application and model.
| Species / reactivity | WB | ELISA |
|---|---|---|
| Human,Rat,Mouse |
This product is manufactured by Reed Biotech and sold through ABMIUM without relabelling.
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