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

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Images

SDS-PAGE - Recombinant human Pin1 protein (AB51230), expandable thumbnail

Publications

  • Communications biology 4:3812021
    Pin1 inhibition improves the efficacy of ralaniten compounds that bind to the N-terminal domain of androgen receptor.
    Applications:
    Unspecified application
    Reactive species:
    Unspecified reactive species
    Jacky K Leung,Yusuke Imamura,Minoru Kato,Jun Wang,Nasrin R Mawji,Marianne D Sadar
    PubMed 33753863
  • FASEB journal : official publication of the Federation of American Societies for Experimental Biology 30:564-772015
    Chaperome screening leads to identification of Grp94/Gp96 and FKBP4/52 as modulators of the α-synuclein-elicited immune response.
    Applications:
    Unspecified application
    Reactive 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
    PubMed 26443817

Key facts

Purity

>95% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

Escherichia coli

Tags

Tag free

Applications

SDS-PAGE, FuncS

Biologically active

Yes

Amino acid sequence

M A D E E K L P P G W E K R M S R S S G R V Y Y F N H I T N A S Q W E R P S G N S S S G G K N G Q G E P A R V R C S H L L V K H S Q S R R P S S W R Q E K I T R T K E E A L E L I N G Y I Q K I K S G E E D F E S L A S Q F S D C S S A K A R G D L G A F S R G Q M Q K P F E D A S F A L R T G E M S G P V F T D S G I H I I L R T E

Reactivity data

Application

SDS-PAGE

Reactivity

Reacts

Dilution info

-

Notes

-

Application

FuncS

Reactivity

Reacts

Dilution info

-

Notes

-

Target data

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).

Alternative names

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

Alternative names

Key facts

Purity

>95% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

Escherichia coli

Applications

SDS-PAGE, FuncS

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
Q13526-1
Animal free

No

Species

Human

Concentration
Loading...
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

Sequence info

Amino acid sequence

M A D E E K L P P G W E K R M S R S S G R V Y Y F N H I T N A S Q W E R P S G N S S S G G K N G Q G E P A R V R C S H L L V K H S Q S R R P S S W R Q E K I T R T K E E A L E L I N G Y I Q K I K S G E E D F E S L A S Q F S D C S S A K A R G D L G A F S R G Q M Q K P F E D A S F A L R T G E M S G P V F T D S G I H I I L R T E

Accession

Q13526

Protein length

Full Length

Nature

Recombinant

Specifications

Form

Liquid

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, Nucleus speckle

Storage

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

This product is an active protein and may elicit a biological response in vivo, handle with caution.

Supplementary info

Activity summary

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.

Associated diseases and disorders

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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1 product image

  • SDS-PAGE - Recombinant human Pin1 protein (ab51230), expandable thumbnail

    SDS-PAGE - Recombinant human Pin1 protein (ab51230)

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

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Product protocols

For this product, it's our understanding that no specific protocols are required. You can:

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