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AB51230

Recombinant human Pin1 protein (Tag Free)

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(2 Publications)

Recombinant human Pin1 protein (Tag Free) is a Human Full Length protein, expressed in Escherichia coli, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, FuncS.

View Alternative Names

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, Peptidyl-prolyl cis-trans isomerase Pin1, Rotamase Pin1, PPIase Pin1, PIN1

1 Images
SDS-PAGE - Recombinant human Pin1 protein (Tag Free) (AB51230)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human Pin1 protein (Tag Free) (AB51230)

ab51230 run on a 14% SDS-PAGE gel with molecular weight markers.

Key facts

Purity

>95% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

Escherichia coli

Tags

Tag free

Applications

FuncS, SDS-PAGE

applications

Biologically active

Yes

Biological activity

Specific activity is > 1,200nmol/min/mg, and is defined as the amount of enzyme that cleaves of suc-AAPF-pNA per minute at 37C

Accession

Q13526

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 20% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.316% Tris HCl, 0.077% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGNSSSGGKNGQGEPARVRCSHLLVKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARGDLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q13526","tags":[]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Pin1 also known as Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 is a small isomerase enzyme with a molecular weight of approximately 18 kDa. This protein is unique because of its specificity for phosphorylated serine/threonine-proline bonds. Pin1 catalyzes the cis-trans isomerization of these bonds with high efficiency. Expression of the Pin1 protein occurs widely across various tissues such as the brain heart and liver. It predominantly functions in the cytoplasm and nucleus where it modulates the activity of its target proteins by inducing conformational changes.
Biological function summary

Pin1 is essential in regulating cell cycle progression and cellular signaling. It influences a variety of cellular processes including cell proliferation transcriptional regulation and apoptosis. By altering the conformation of specific phosphorylated proteins Pin1 ensures the precise control of cell cycle checkpoints impacting the stability of many proteins such as cyclin D1 and p53. Despite not being part of a large protein complex Pin1 interacts with numerous other proteins thereby coordinating complex regulatory networks essential for maintaining normal cell function.

Pathways

Pin1 plays an important role in both the Wnt signaling pathway and the MAPK signaling pathway. In the Wnt pathway Pin1 maintains stability and the accumulation of β-catenin which affects transcription of target genes critical for cell proliferation. Within the MAPK pathway Pin1 regulates the activity of proteins like c-Jun and ERK1/2 which are vital for transmitting extracellular signals to cellular responses. Through these pathways Pin1 helps modulate responses to external stimuli and maintains cellular homeostasis by adjusting protein function dynamically in response to changes in phosphorylation status.

Changes in Pin1 activity have been linked to cancer and Alzheimer's disease. In cancer increased Pin1 expression accelerates the degradation of tumor suppressor proteins like p53 contributing to uncontrolled cell proliferation and reduced apoptosis. In Alzheimer's disease Pin1 dysfunction leads to the accumulation of phosphorylated tau protein which forms neurofibrillary tangles and disrupts normal neuronal function. Through these connections Pin1 represents a potential therapeutic target for developing treatments aimed at restoring balance in these pathways and alleviating disease symptoms.
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Specifications

Form

Liquid

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General info

Function

Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs (PubMed : 21497122, PubMed : 23623683, PubMed : 29686383). By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes (PubMed : 21497122, PubMed : 22033920, PubMed : 23623683). 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 (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). 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) (PubMed : 23623683, PubMed : 27561354). 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 (PubMed : 29686383).

Post-translational modifications

Phosphorylation at Ser-71 by DAPK1 results in inhibition of its catalytic activity, nuclear localization, and its ability to induce centrosome amplification, chromosome instability and cell transformation (PubMed:21497122). Ser-71 is dephosphorylated upon IL33-stimulation of dendritic cells (By similarity).

Subcellular localisation

Nucleus

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Product protocols

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Target data

Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs (PubMed : 21497122, PubMed : 23623683, PubMed : 29686383). By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes (PubMed : 21497122, PubMed : 22033920, PubMed : 23623683). 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 (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). 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) (PubMed : 23623683, PubMed : 27561354). 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 (PubMed : 29686383).
See full target information PIN1
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Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Communications biology 4:381 PubMed33753863

2021

Pin1 inhibition improves the efficacy of ralaniten compounds that bind to the N-terminal domain of androgen receptor.

Applications

Unspecified application

Species

Unspecified reactive species

Jacky K Leung,Yusuke Imamura,Minoru Kato,Jun Wang,Nasrin R Mawji,Marianne D Sadar

FASEB journal : official publication of the Federation of American Societies for Experimental Biology 30:564-77 PubMed26443817

2015

Chaperome screening leads to identification of Grp94/Gp96 and FKBP4/52 as modulators of the α-synuclein-elicited immune response.

Applications

Unspecified application

Species

Unspecified reactive species

Adahir Labrador-Garrido,Marta Cejudo-Guillén,Soumya Daturpalli,María M Leal,Rebecca Klippstein,Erwin J De Genst,Javier Villadiego,Juan J Toledo-Aral,Christopher M Dobson,Sophie E Jackson,David Pozo,Cintia Roodveldt
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