Human Peptidyl-Prolyl Cis-Trans Isomerase NIMA-Interacting 1 (PIN1) Enzyme
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Description
Peptidyl-Prolyl Cis/Trans Isomerase NIMA-Interacting 1 is a recombinant enzyme.
Documents del producto
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Peptidyl-Prolyl Cis-Trans Isomerase NIMA-Interacting 1 (PIN1) |
| Host | E. coli |
| Recommended Dilution | Optimal dilutions/concentrations should be determined by the end user. |
| Origin | Human |
| Expression | Recombinant |
| Purity | > 95% (SDS-PAGE) |
| Size 1 | 5 µg |
| Size 2 | 20 µg |
| Size 3 | 1 mg |
| Form | Liquid |
| Tested Applications | SDS-PAGE |
| Availability | Shipped within 5-10 working days. |
| Storage | Store at 4 °C if the entire vial will be used within 2-4 weeks. Store at -20 °C for long term storage. For long term storage, it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | Q13526 |
| Background | Protein PIN1 |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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Human PIN1 (Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1) ELISA Kit
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PIN1 antibody
Peptidyl-prolyl cis/trans isomerase(PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro(pSer/Thr-Pro) motifs in a subset of proteins, resulting in conformational changes in the proteins(PubMed:21497122, PubMed:22033920). Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK(PubMed:16644721). Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation(PubMed:15664191). Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner(PubMed:17828269). Acts as a regulator of JNK cascade by binding to phosphorylated FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation: degradation of FBXW7 leads to subsequent stabilization of JUN(PubMed:22608923).
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