Human Peptidyl-Prolyl Cis-Trans Isomerase Nima-Interacting 1 (PIN1) Protein
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Description
Peptidyl-Prolyl Cis-Trans Isomerase Nima-Interacting 1 (PIN1) protein is a recombinant Human protein expressed in E. coli.
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Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Peptidyl-Prolyl Cis-Trans Isomerase Nima-Interacting 1 (PIN1) |
| Host | E. coli |
| Assay Type | Activity: Not tested Sequence Fragment: Met1-Glu163 Tag: N-terminal His tag |
| Origin | Human |
| Observed MW | 20.3 kDa |
| Expression | Recombinant |
| Purity | > 90% (SDS-PAGE) |
| Size 1 | 100 µg |
| Form | Lyophilized |
| Tested Applications | SDS-PAGE |
| Buffer | Prior to lyophilization: Sterile PBS, pH 7.4. |
| Availability | Shipped within 5-15 working days. |
| Storage | Storage: Store lyophilized between -20 °C and -80°C. Stability: Stable when stored reconstituted at 2-8°C for up to 1 week. Reconstituted aliquots are stable at -20°C for up to 3 months. Shelf Life: 12 months. |
| Dry Ice | No |
| UniProt ID | Q13526-1 |
| Background | Protein PIN1 |
| Status | RUO |
| Note | THIS PRODUCT IS FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC, THERAPEUTIC OR COSMETIC PROCEDURES. NOT FOR HUMAN OR ANIMAL CONSUMPTION. |
Descripción
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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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