Recombinant Mouse Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1)

Code CSB-YP882537MO
MSDS
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Source Yeast
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Code CSB-EP882537MO
MSDS
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Source E.coli
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Code CSB-EP882537MO-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP882537MO
MSDS
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Source Baculovirus
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Code CSB-MP882537MO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Pin1
Uniprot No.
Alternative Names
Pin1; Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; EC 5.2.1.8; Peptidyl-prolyl cis-trans isomerase Pin1; PPIase Pin1
Species
Mus musculus (Mouse)
Expression Region
1-165
Target Protein Sequence
MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGG STVGGSSKNG QGEPAKVRCS HLLVKHSQSR RPSSWRQEKI TRSKEEALEL INGYIQKIKS GEEDFESLAS QFSDCSSAKA RGDLGPFSRG QMQKPFEDAS FALRTGEMSG PVFTDSGIHI ILRTE
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs. By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes. 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. 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. Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner. 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. May facilitate the ubiquitination and proteasomal degradation of RBBP8/CtIP through CUL3/KLHL15 E3 ubiquitin-protein ligase complex, hence favors DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR). Upon IL33-induced lung inflammation, catalyzes cis-trans isomerization of phosphorylated IRAK3/IRAK-M, inducing IRAK3 stabilization, nuclear translocation and expression of pro-inflammatory genes in dendritic cells.
Gene References into Functions
  1. Study using IL-33-induced type 2 immunity signaling in a combination of cell lines, mouse models, and primary cells from mouse models reveal critical roles of IRAK-M and PIN1 in IL-33-induced type 2 immunity. Upon IL-33-induced inflammation, activated PIN1 binds to and catalyzes cis-trans isomerization of phosphorylated IRAK-M, inducing IRAK-M stabilization and nuclear translocation. PMID: 29686383
  2. Pin1 serves as a modulator of SERCA2a and Na(2+)/Ca(2+) exchanger 1 Ca(2+) handling proteins, with loss of function resulting in impaired cardiomyocyte relaxation. PMID: 29018025
  3. expressed in developing periodontal tissue, in vitro PDLCs and cementoblasts and role in periodontal regeneration PMID: 28198538
  4. These results suggest that Pin1 promotes the progression of the mitotic cell cycle of SSC in steady-state, which is required for the sperm production from SSCs. PMID: 29432730
  5. Pin1 silencing in lymphomas retarded disease progression in mice, making Pin1 an attractive therapeutic target in Myc-driven tumors. PMID: 26943576
  6. Pin1 enhances adipocyte differentiation by regulating the function of PPARgamma. PMID: 27475846
  7. Pin1 serves as a positive regulatory molecule of proplatelet formation of megakaryocytes by enhancing the function of phosphorylated tau. PMID: 28943044
  8. Direct delivery of recombinant Pin1 via fibroin nanoparticle encapsulated cationic lipid complex successfully rescued osteoblast differentiation of pin-1 deficient cells. PMID: 27800612
  9. Pin1 plays important role in the cell cycle progression and increase oval cells proliferation which may be crucial in chronic liver injury. PMID: 28214206
  10. in vivo functional analyses of Pin1 in the GFAP-tTA;TRE-SmoA1 mouse model of Hedgehog-driven medulloblastoma demonstrate that the loss of Pin1 impairs tumor development and dramatically increases survival. PMID: 28167297
  11. Data, including data from studies conducted with knockout mice, suggest that Pin1 (prolyl isomerase 1) expression in pancreatic beta-cells is markedly elevated in obesity from diet high in fat/sucrose; Pin1 appears to be involved in proliferation of beta-cells and in regulation of secretion of insulin; Pin1 interacts with Sik2 (salt-inducible kinase 2) to regulate calcium signaling. PMID: 28566287
  12. Pin1 knockout in lupus-prone MRL lpr mice prevents expression of lupus phenotype. PMID: 27159270
  13. By interacting with PSD-95, Pin1 dampens PSD-95 ability to complex with NMDARs, thus negatively affecting NMDAR signaling and spine morphology. PMID: 27194325
  14. Oral administration of brown algae polyphenol, a Pin1 inhibitor, reduced fat buildup in mice. PMID: 28036348
  15. The findings provide evidence for a putative novel role of PIN1 in the development of the nociceptive system and indicate phosphorylation-mediated conformational changes as a mechanism for regulating the PRRXL1 role in the process. PMID: 28049756
  16. Data show that peptidyl-prolyl isomerase (Pin1) inhibition inhibits high glucose (HG)-induced cardiac fibroblasts (CFs) proliferation and migration. PMID: 27634219
  17. Pin1 knock-out mice exhibited disturbed neuronal projections from the cerebral cortex and reduced white matter tracks. PMID: 26991250
  18. Pin1 plays a vital role on the development of vascular inflammation and atherosclerosis in ApoE-/- mice. PMID: 28300760
  19. Studies indicate that Prolyl Isomerase Pin1 (Pin1) Is highly involved in the development of metabolic syndrome. PMID: 27618008
  20. results revealed a pivotal role of Pin1 in regulation of alcohol-induced mouse cardiomyocytes apoptosis by promoting reactive oxygen species (ROS) accumulation and repressing eNOS expression, which could be potential therapeutic targets for ACM. PMID: 26697133
  21. diet containing high phosphate induces rapid renal fibrosis before a significant impact on renal function and Pin1 plays an important role in the fibrotic process. PMID: 26914452
  22. Pin1 regulates the osteogenic activity of Osterix. PMID: 25463757
  23. Pin1-dependent signaling represents a mechanism to modulate GABAergic transmission by regulating NL2/gephyrin interaction. PMID: 25297980
  24. Thus, Pin1 could be developed as a major therapeutic target in many skeletal diseases PMID: 25187260
  25. The identification of Pin1 as a factor involved in cell fusion contributes to the understanding of osteoclast-associated diseases, including osteoporosis, and opens new avenues for therapeutic targets. PMID: 24891219
  26. Studied genome-wide mRNA expression microarray using the RNA isolation from Pin1 (+/+) and Pin1 (-/-) mouse embryonic fibroblast (MEF) cells. Signaling pathways regulated by Pin1 were analyzed with the utility of KEGG pathway and GO annotation. PMID: 23563987
  27. Pin1 acts as a negative regulator of the G2/M transition by interacting with the Aurora-A-Bora complex. PMID: 23970419
  28. Pin1-mediated structural modification of Runx2 is an indispensable step connecting phosphorylation and acetylation and, consequently, transcriptional activation of Runx2 by FGF signaling PMID: 24509851
  29. Pin1 has pleiotropic roles in CPCs and may be a molecular target to promote survival, enhance repair, improve differentiation, and antagonize senescence. PMID: 24375406
  30. Pin1 is a novel regulator of osteoblast differentiation that acts through the regulation of Runx2 function. PMID: 24113655
  31. Pin1 null mice exhibit low bone mass and attenuation of BMP signaling. PMID: 23675491
  32. Identify a novel form of histone H1 regulation through phosphorylation-dependent pin1 mediated proline isomerization, which has consequences on overall H1 phosphorylation levels and the stability of H1 binding to chromatin. PMID: 24100296
  33. Data indicate that Pin1 is up-regulated in dopaminergic neurons in cell culture, animal models, and human Parkinson disease (PD) brains. Pin1 inhibition protects dopaminergic neurons in PD models. PMID: 23754278
  34. Study defines a D1-dopamine receptor-signaling pathway that potentiates the ability of mGluR5 to activate NMDARs and implicates this pathway in cocaine-induced plasticity; Pin1 catalysis on mGluR5(pS1126) is central to this signaling. PMID: 23911326
  35. Pin1 and c-Myc are cooverexpressed in cancer, and this drives a gene expression pattern that is enriched in poor-outcome breast cancer subtypes. PMID: 23716601
  36. UVA-induced COX-2 expression is mediated by Pin1 activation and is associated with malignant transformation of epidermal cells. PMID: 23380442
  37. Data support a role for Pin1 as a central modulator of the intensity and duration of 2 major hypertrophic signaling pathways. PMID: 23487407
  38. the isomerase activity of Pin1 inhibited PIP4K activity. PMID: 23193159
  39. Pin1 expression remained constant but Pin1 posttranslational two-dimensional pattern was modified by tau overexpression in a tau-inducible mouse neuroblastoma cell line and in a THY-Tau22 mouse model of tauopathy PMID: 22926167
  40. Isomerase Pin1 stimulates dephosphorylation of tau protein at cyclin-dependent kinase (Cdk5)-dependent Alzheimer phosphorylation sites PMID: 23362255
  41. Pin1 KO mice were resistant to nonalcoholic steatohepatitis development. PMID: 23112047
  42. Data indicate that peptidyl-prolyl isomerase Pin1(-/-) mouse embryonic fibroblasts (MEFs) showed higher cyclin-dependent kinase 10 (CDK10) expression than Pin1(+/+) MEFs. PMID: 22158035
  43. Pin1 plays a critical role in tumorigenesis plausibly via physical interaction with RSK2 and reciprocal phosphorylation PMID: 22562304
  44. Results indicate that peptidyl-prolyl isomerase Pin1 Associates with Smad3 and Smad6. PMID: 22613712
  45. Pin1 is a regulator of neural progenitor cell differentiation by acting on beta-catenin and provides a new postphosphorylation signaling mechanism to regulate developmental stage-specific functioning of beta-catenin signaling in neuronal differentiation. PMID: 22645310
  46. Physiological levels of Pin1 are important to control the intracellular localization and metabolic fate of Thr668-phosphorylated AbetaPP. PMID: 22430533
  47. Pin1 down-regulation could be a potential approach in obesity-related dysfunctions, such as high blood pressure, diabetes, non-alcoholic steatohepatitis. PMID: 22412843
  48. Pin1 binds the hydrophobic motif of conventional PKC isozymes to catalyze the isomerization of the phospho-Thr-Pro peptide bond at the turn motif, thus converting these PKC isozymes into species that can be efficiently down-regulated following activation. PMID: 22318721
  49. Via regulation of CD8+ cDC production, Pin1 may serve as an important modulator of adaptive immunity. PMID: 22238658
  50. Pin1 overexpression in the liver of the experimental mice attenuated acute liver injury induced by carbon tetrachloride. PMID: 22192799

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Subcellular Location
Nucleus. Nucleus speckle. Cytoplasm.
Tissue Specificity
Expressed in dendritic cells (at protein level).
Database Links
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