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AB189321

Anti-Pin1 antibody - N-terminal

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(1 Publication)

Rabbit Polyclonal PIN1 antibody. N-terminal. Suitable for IHC-P, ICC/IF and reacts with Human, Mouse samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Human PIN1 aa 1-50.

View Alternative Names

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

2 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Pin1 antibody - N-terminal (AB189321)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Pin1 antibody - N-terminal (AB189321)

Immunohistochemical analysis of formalin-fixed, paraffin-embedded Human cerebellum tissue labeling Pin1 with ab189321 at 20 μg/ml.

Immunocytochemistry/ Immunofluorescence - Anti-Pin1 antibody - N-terminal (AB189321)
  • ICC/IF

Supplier Data

Immunocytochemistry/ Immunofluorescence - Anti-Pin1 antibody - N-terminal (AB189321)

Immunofluorescent analysis of NIH 3T3 cells labeling Pin1 with ab189321 at 1/100 dilution, in the presence (right panel) or absence (left panel) of immunizing peptide.

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Mouse, Human

Applications

IHC-P, ICC/IF

applications

Immunogen

Synthetic Peptide within Human PIN1 aa 1-50. The exact immunogen used to generate this antibody is proprietary information.

Q13526

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "IHCP" : {"fullname" : "Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections)", "shortname":"IHC-P"}, "ICCIF" : {"fullname" : "Immunocytochemistry/ Immunofluorescence", "shortname":"ICC/IF"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "IHCP-species-checked": "testedAndGuaranteed", "IHCP-species-dilution-info": "20 µg/mL", "IHCP-species-notes": "<p></p>", "ICCIF-species-checked": "guaranteed", "ICCIF-species-dilution-info": "", "ICCIF-species-notes": "" }, "Mouse": { "IHCP-species-checked": "guaranteed", "IHCP-species-dilution-info": "", "IHCP-species-notes": "", "ICCIF-species-checked": "testedAndGuaranteed", "ICCIF-species-dilution-info": "1/100 - 1/500", "ICCIF-species-notes": "<p></p>" }, "Rat": { "IHCP-species-checked": "predicted", "IHCP-species-dilution-info": "", "IHCP-species-notes": "", "ICCIF-species-checked": "predicted", "ICCIF-species-dilution-info": "", "ICCIF-species-notes": "" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.4 Preservative: 0.02% Sodium azide Constituents: 50% Glycerol (glycerin, glycerine), 49% PBS, 0.87% Sodium chloride
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

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.

Product protocols

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

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

Publications (1)

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

Genome biology 19:37 PubMed29548335

2018

Mutational signatures reveal the role of RAD52 in p53-independent p21-driven genomic instability.

Applications

Unspecified application

Species

Unspecified reactive species

Panagiotis Galanos,George Pappas,Alexander Polyzos,Athanassios Kotsinas,Ioanna Svolaki,Nickolaos N Giakoumakis,Christina Glytsou,Ioannis S Pateras,Umakanta Swain,Vassilis L Souliotis,Alexandros G Georgakilas,Nicholas Geacintov,Luca Scorrano,Claudia Lukas,Jiri Lukas,Zvi Livneh,Zoi Lygerou,Dipanjan Chowdhury,Claus Storgaard Sørensen,Jiri Bartek,Vassilis G Gorgoulis
View all publications

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