Recombinant Human Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1)

Code CSB-YP615698HU
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Source Yeast
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Code CSB-EP615698HU
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Source E.coli
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Code CSB-EP615698HU-B
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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-BP615698HU
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Source Baculovirus
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Code CSB-MP615698HU
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Source Mammalian cell
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Product Details

>85% (SDS-PAGE)
Target Names
Uniprot No.
Alternative Names
DOD; DODO, Drosophila, homolog of; FLJ40239; FLJ77628; MGC10717; NIMA interacting 1; Peptidyl prolyl cis trans isomerase NIMA interacting 1; Peptidyl prolyl cis/trans isomerase NIMA interacting; Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; Peptidyl-prolyl cis-trans isomerase pin1; Peptidylprolyl cis/trans isomerase NIMA interacting 1; Pin 1; Pin1; PIN1_HUMAN; PPIase Pin1; Prolyl isomerase; Protein (peptidylprolyl cis/trans isomerase) NIMA interacting 1; Protein NIMA interacting 1; Rotamase Pin1; UBL 5; UBL5
Homo sapiens (Human)
Expression Region
Target Protein Sequence
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.
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
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.
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Please contact us to get it.

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Target Background

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 acidic residues located N-terminally to the proline bond to be isomerized. 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. NIMA-Interacting Peptidylprolyl Isomerase Pin1 (Pin1) is a direct target for miR-140-5p in hepatocellular carcinoma (HCC). PMID: 28383568
  2. Clinical trial with house dust mite allergen challenge of asthmatic patients reveal that IRAK-M is a PIN1 target critical for IL-33 signaling in allergic asthma. NMR analysis and docking simulations suggest that PIN1 might regulate IRAK-M conformation and function in IL-33 signaling. PMID: 29686383
  3. We discuss evidence that enables us to speculate about the role of Pin1 as molecular link in the pathogenesis of type 3 diabetes i.e., the clinical association of dementia/AD and T2D. PMID: 30096758
  4. our results indicated different prognostic roles of subcellular Pin1expression in colorectal cancer PMID: 30244946
  5. Multivalent Interactions with Fbw7 and Pin1 Facilitate Recognition of c-Jun by the Fbw7. PMID: 29225075
  6. Results indicate that although PIN1 increases p27 levels, it also attenuates p27's inhibitory activity on CDK2 and thereby contributes to increased G1-S phase transitions and cell proliferation. PMID: 29118189
  7. Pin1 plays a role as a vital modulator of vascular smooth muscle cell senescence PMID: 28986099
  8. PIN1 rs2233682 A allele might be related with a decreased risk of hepatitis B virus-related liver cirrhosis in a Guangxi population. PMID: 30170446
  9. Downregulation of miR-370 in esophageal squamous cell carcinoma is associated with cancer progression and promotes cancer cell proliferation via upregulating PIN1, which might be a potential therapeutic target and adverse prognostic factor in the clinic. PMID: 29605603
  10. Study investigated the allosteric mechanism of full-length Pin1 using several microsecond-long molecular dynamics simulations; show that binding of the substrate to the WW domain is directly coupled to the dynamics of the catalytic domain, causing rearrangement of the residue-residue contact dynamics from the WW domain to the catalytic domain. PMID: 27077947
  11. Pin1 is a fast-acting enzyme which may be utilised by cells to protect the phosphorylation state of Tissue Factor (TF) in activated cells prolonging TF activity and release, and therefore ensuring adequate haemostasis. PMID: 28962834
  12. Studies results suggest that loss of peptidyl-prolyl isomerase (Pin1) activity could lead to the loss of synaptic plasticity in the development of Alzheimer disease. PMID: 28458925
  13. Parallel folding pathways of PIN1 Fip35 WW domain have been explained by infrared spectra and their computer simulations. PMID: 28881468
  14. High PIN1 expression is associated with stomach neoplasms. PMID: 28481868
  15. Pin1 is a novel regulator of ATF1 at Thr184. PMID: 28032861
  16. The dynamic basis for signal propagation in Pin1 N-terminal binding domain WW has been described. PMID: 27499442
  17. The endoplasmic reticulum (ER) stress decreased Pin1 expression through p53 activation, and this mechanism may be associated with ER stress-induced cell death. These data reported here support the importance of Pin1 as a potential target molecule mediating tumor development. PMID: 25451271
  18. our data suggested that miR-874-3p plays a tumour suppressive role in HCC through down-regulation of PIN1. PMID: 28076852
  19. The study demonstrates the oncogenic role of PIN1 in NPC tumorigenesis, and shows that its overexpression can enhance tumor cell growth via the upregulation of cyclinD1. PMID: 27258148
  20. Pin1 expression was decreased remarkably in temporal lobe epilepsy patients compared to controls. PMID: 28239767
  21. 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
  22. Knockdown of PIN1 potently blocks TLR-7/TLR-9/Pin1/IRAK-1/IRF-7 signaling in vitro. PMID: 27159270
  23. Data indicate the complexity of interactions between Pin1 and activated IRAK1, suggesting that phosphorylation of neighboring Ser/Thr-Pro motifs in proteins might provide competitive advantage at cellular concentrations for engaging with Pin1. PMID: 27790836
  24. Surprisingly, the authors discover that Pin1 does not promote phosphorylated tau-induced microtubule formation in vitro, refuting the commonly accepted model in which Pin1 binding and catalysis on the A180 epitope restores the function of the Alzheimer's associated phosphorylated tau in tubulin assembly. PMID: 26996940
  25. Importantly, site-specific measurements of Pin1-catalysis of CDK2/CycA-phosphorylated full-length tau reveal a number of sites that are catalyzed simultaneously with different efficiencies. PMID: 26996941
  26. Results show that Pin1 plays a dual role, both positive and negative, in regulating NO production and in mediating the pathogenesis of cardiovascular diseases. Pin1 functions may vary a lot under different circumstances. PMID: 27057935
  27. reciprocal regulation of Pin1 and XBP1s is associated with the activation of oncogenic pathways, and the relationship of PIN1 and XBP1 may be an attractive target for novel therapy in cancers PMID: 27334111
  28. When combined with the BRAF(V600E)-inhibitor PLX4032 a robust repression in melanoid viability was obtained, establishing preclinical value of patient-derived melanoids for prognostic use of drug sensitivity and further underscoring the beneficial effect of Pin1-FOXM1 inhibitory peptides as anti-melanoma drugs. PMID: 26279295
  29. Pin1 represents a regulatory effector of lamina disassembly that promotes the nuclear pore-independent egress of herpesviral capsids PMID: 27556400
  30. Considering that the WW domain participates in the catalytic activity of the Pin1 isomerase, our study represents a novel approach for studying Pin1 function through the analysis of its naturally occurring mutants. PMID: 28431929
  31. TNFalpha reduces bovine eNOS activity through serine 116 phosphorylation and Pin1 binding. PMID: 27073025
  32. The role of PIN1 in hepatocellular carcinoma tumourigenesis is discussed by reviewing the interactions between PIN1 and various cellular and viral proteins that are involved in beta-catenin, NOTCH, and PI3K/Akt/mTOR pathways, apoptosis, angiogenesis and epithelial-mesenchymal transition. [Review] PMID: 28018099
  33. The -667T genetic variants in the Pin1 promoter contribute to an increased risk of secondary hyperparathyroidism of chronic kidney disease ( CKD SHPT ) and may be biomarkers of susceptibility to CKD SHPT. PMID: 27876426
  34. Studies indicate that Prolyl Isomerase Pin1 (Pin1) Is highly involved in the development of metabolic syndrome. PMID: 27618008
  35. Our results suggest that PIN1 plays a role in cancer cell proliferation, migration and invasion in a different manner according to the TP53 gene mutation status in hepatocellular carcinoma PMID: 27499097
  36. Our results suggest that Pin1 plays an important role in tumorigenesis of prostate cancer PMID: 26497355
  37. this study's findings suggest that the PIN1 rs2233679 TT genotype, the rs2233682GA genotype, and A alleles might be associated with the HBV-related HCC in a Guangxi study population. PMID: 26643892
  38. In this context, Pin1 epigenetic regulation seems to be differently involved in frontotemporal dementia and Alzheimer's disease and might explain the altered amyloid protein precusor metabolism and tau phosphorylation in neurodegenerative diseases PMID: 26944164
  39. High Pin1 expression is associated with papillary thyroid carcinoma. PMID: 27029791
  40. The expression of PIN1 was associated with risk of malignancy, tumour location, tumour size, and mitotic counts in gastrointestinal stromal tumors. PMID: 26977025
  41. the role of hydration in the structural integrity of Pin1 PMID: 26651388
  42. Results indicate that PIN1 may be a valuable target to hit in cancer cells characterized by increased aggressive potential, overexpression of erbB receptor family members, and defective p53. PMID: 26917410
  43. Structural Analysis of the Pin1-CPEB1 interaction and its potential role in CPEB1 degradation has been described. PMID: 26456073
  44. Data show that Prolyl isomerase Pin1 is expressed in an epidermal growth factor receptor (EGFR)-mutant lung cancer tissue that has undergone partial epithelial-mesenchymal transition (EMT) and acquired resistance to EGFR tyrosine kinase inhibitors (TKIs). PMID: 26752745
  45. Report shows that PIN1 binds to and stabilizes HIF-1alpha, consequently enhancing the angiogenesis. PMID: 26784107
  46. This shows that Pin1 is implemented in maintaining the susceptibility to the genotoxic drugs by controlling P-gp level as well as p53-dependent apoptosis and cell cycle signaling pathways. PMID: 26874277
  47. Activation of BAX through the concerted action of cytosolic p53 and Pin1 may integrate cell stress signals to induce a direct apoptotic response. PMID: 26236013
  48. The roles of the three tryptophan residues (W11, W34 and W73)in maintaining the structure and the function of Pin1 PMID: 25837727
  49. Expression of Pin1 was decreased at or above the Cd IC50 value and was inversely correlated with the level of phospho-Ser-GSK3alphabeta in oral squamous cell carcinoma. PMID: 26381174
  50. ZBP-89 attenuates HDAC3 by increasing IkappaB degradation, dependent on Pin1 but independent of NF-Kappab PMID: 25623232

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Subcellular Location
Nucleus. Nucleus speckle. Cytoplasm.
Tissue Specificity
Expressed in immune cells in the lung (at protein level). The phosphorylated form at Ser-71 is expressed in normal breast tissue cells but not in breast cancer cells.
Database Links

HGNC: 8988

OMIM: 601052

KEGG: hsa:5300

STRING: 9606.ENSP00000247970

UniGene: Hs.465849

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