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Key Documents

07-091

Sigma-Aldrich

Anti-Pin1 Antibody

Upstate®, from rabbit

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

polyclonal

species reactivity

human, rat, mouse

manufacturer/tradename

Upstate®

technique(s)

immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgG

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... UBL5(59286)

General description

Pin1 is a peptidyl-prolyl isomerase (PPI) that targets phosphorylated Ser or Thr residues followed by a Pro (S/T-P). Isomerization of phosphorylated Ser or Thr residues may alter protein confirmation and, subsequently, modify activity. Pin1 is overexpressed in many human breast cancers, and has been shown to modify numerous proteins including p53,
NF-κB, c-Jun, cyclin D1, and β-catenin.

Specificity

Pin1

Immunogen

Full-length His tagged human Pin-1

Application

Anti-Pin1 Antibody is a high quality Rabbit Polyclonal Antibody for the detection of Pin1 & has been validated in IP & WB.
Research Category
Epigenetics & Nuclear Function
Research Sub Category
Cell Cycle, DNA Replication & Repair

Quality

Routinely evaluated by immunoblot on RIPA lysates from mouse 3T3/A31 cells

Target description

18kDa

Physical form

Format: Purified
Presentation: 100 µg of protein A purified rabbit IgG in 100 µL of 0.014 M phosphate buffer, pH 7.6, 0.175 M NaCl, 0.07% Sodium Azide and 30% glycerol. Liquid at -20°C.
Protein A chromatography

Storage and Stability

2 years at -20°C

Analysis Note

Control
Positive Antigen Control: Catalog #12-305, 3T3/A31 lysate. Add 2.5 μL of 2-mercapto-ethanol/100 μL of lysate and boil for 5 minutes to reduce the preparation. Load 20 μg of reduced lysate per lane for minigels.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Legal Information

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 1


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Activation of beta-catenin signaling in prostate cancer by peptidyl-prolyl isomerase Pin1-mediated abrogation of the androgen receptor-beta-catenin interaction.
Chen, SY; Wulf, G; Zhou, XZ; Rubin, MA; Lu, KP; Balk, SP
Molecular and cellular biology null
Lucía Barbier-Torres et al.
Nature communications, 13(1), 557-557 (2022-01-30)
MATα1 catalyzes the synthesis of S-adenosylmethionine, the principal biological methyl donor. Lower MATα1 activity and mitochondrial dysfunction occur in alcohol-associated liver disease. Besides cytosol and nucleus, MATα1 also targets the mitochondria of hepatocytes to regulate their function. Here, we show
K P Lu et al.
Nature, 380(6574), 544-547 (1996-04-11)
The NIMA kinase is essential for progression through mitosis in Aspergillus nidulans, and there is evidence for a similar pathway in other eukaryotic cells. Here we describe the human protein Pin1, a peptidyl-prolyl cis/trans isomerase (PPIase) that interacts with NIMA.
Y Liao et al.
Oncogene, 28(26), 2436-2445 (2009-05-19)
The serine/threonine protein kinase B (PKB, also known as Akt) plays a pivotal role in diverse cellular functions. Elevated expression of activated Akt has been detected in a wide variety of human cancers; however, the mechanism of Akt protein stability
Praveen Rajendran et al.
Molecular cancer, 10, 68-68 (2011-06-01)
Histone deacetylase (HDAC) inhibitors are currently undergoing clinical evaluation as anti-cancer agents. Dietary constituents share certain properties of HDAC inhibitor drugs, including the ability to induce global histone acetylation, turn-on epigenetically-silenced genes, and trigger cell cycle arrest, apoptosis, or differentiation

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