Human Peptidyl-Prolyl Cis-Trans Isomerase NIMA-Interacting 1 (PIN1) Protein
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Description
Human PIN1 Protein is a recombinant protein from Human produced in E. coli. A DNA sequence encoding the mature form of human PIN1 (Q13526-1) (Met 1-Glu 163) was expressed, with a polyhistide tag at the N-terminus.
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Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | PIN1 |
| Host | E. coli |
| Origin | Human |
| Observed MW | Molecular Weight: 20.3 kDa Sequence Fragment: Met1-Glu163 Tag: N-terminal His tag Validity: The validity for this protein is 12 months. |
| Expression | Recombinant |
| Purity | > 90% (SDS-PAGE) |
| Size 1 | 100 µg |
| Tested Applications | SDS-PAGE |
| Buffer | Lyophilized from sterile PBS, pH 7.4. |
| Availability | Shipped within 5-15 working days. |
| Storage | Aliquot and store at -20°C or -80°C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | Q13526-1 |
| 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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