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Peptidyl-prolyl cis/trans isomerases (PPIases) catalyze the cis/trans isomerization of peptidyl-prolyl peptide bonds. Additionally we are shipping Peptidylprolyl Cis/trans Isomerase, NIMA-Interacting 1 Proteins (21) and Peptidylprolyl Cis/trans Isomerase, NIMA-Interacting 1 Kits (5) and many more products for this protein.
Showing 10 out of 185 products:
Human Polyclonal PIN1 Primary Antibody for EIA, WB - ABIN493364
Campaner, Kaldis, Izraeli, Kirsch: Sil phosphorylation in a Pin1 binding domain affects the duration of the spindle checkpoint. in Molecular and cellular biology 2005
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Mouse (Murine) Polyclonal PIN1 Primary Antibody for EIA, WB - ABIN493366
Lim, Balastik, Lee, Nakamura, Liou, Sun, Finn, Pastorino, Lee, Lu: Pin1 has opposite effects on wild-type and P301L tau stability and tauopathy. in The Journal of clinical investigation 2008
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Cow (Bovine) Polyclonal PIN1 Primary Antibody for EIA, WB - ABIN401395
Esnault, Shen, Whitesel, Malter: The peptidyl-prolyl isomerase Pin1 regulates granulocyte-macrophage colony-stimulating factor mRNA stability in T lymphocytes. in Journal of immunology (Baltimore, Md. : 1950) 2006
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Human Polyclonal PIN1 Primary Antibody for IF, ELISA - ABIN1532476
Lu, Hanes, Hunter: A human peptidyl-prolyl isomerase essential for regulation of mitosis. in Nature 1996
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Human Monoclonal PIN1 Primary Antibody for WB - ABIN1882275
Ota, Suzuki, Nishikawa, Otsuki, Sugiyama, Irie, Wakamatsu, Hayashi, Sato, Nagai, Kimura, Makita, Sekine, Obayashi, Nishi, Shibahara, Tanaka, Ishii, Yamamoto, Saito, Kawai, Isono, Nakamura, Nagahari et al.: Complete sequencing and characterization of 21,243 full-length human cDNAs. ... in Nature genetics 2003
Rat (Rattus) Polyclonal PIN1 Primary Antibody for ELISA, WB - ABIN185726
Pastorino, Sun, Lu, Zhou, Balastik, Finn, Wulf, Lim, Li, Li, Xia, Nicholson, Lu: The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production. in Nature 2006
results revealed a pivotal role of Pin1 in regulation of alcohol-induced mouse cardiomyocytes apoptosis by promoting reactive oxygen species (ROS (show ROS1 Antibodies)) accumulation and repressing eNOS (show NOS3 Antibodies) expression, which could be potential therapeutic targets for ACM.
diet containing high phosphate induces rapid renal fibrosis before a significant impact on renal function and Pin1 plays an important role in the fibrotic process.
Pin1 is indispensable for Wnt3a (show WNT3A Antibodies)-induced osteoblast differentiation.
Pin1 regulates the osteogenic activity of Osterix (show SP7 Antibodies).
Pin1-dependent signaling represents a mechanism to modulate GABAergic transmission by regulating NL2 (show MMEL1 Antibodies)/gephyrin (show GPHN Antibodies) interaction.
PIN1 regulates pulmonary effects of endotoxin and tumor necrosis factor-alpha (show TNF Antibodies) in mice.
Thus, Pin1 could be developed as a major therapeutic target in many skeletal diseases
Results show that DLX5 (show DLX5 Antibodies), p63 (show CKAP4 Antibodies), Pin1 and FGF8 (show FGF8 Antibodies) participate to the same time- and location-restricted regulatory loop essential for apical ectodermal ridge stratification, hence for normal patterning and skeletal morphogenesis of the limb buds.
Pin1 induction during liver fibrosis is involved in hepatic stellate cell activation, TGFbeta1 (show TGFB1 Antibodies) expression, and TGFbeta1 (show TGFB1 Antibodies)-mediated fibrogenesis signalling.
The identification of Pin1 as a factor involved in cell fusion contributes to the understanding of osteoclast-associated diseases, including osteoporosis, and opens new avenues for therapeutic targets.
Pin1 is an essential factor regulating CPEB degradation
Pin1 binding is required for the inactivation of XeWee1B at M phase, presumably causing isomerization of the phospho-TP motif and thereby impairing the function of the Wee (show WEE1 Antibodies)-box
the role of hydration in the structural integrity of Pin1
Results indicate that PIN1 may be a valuable target to hit in cancer cells characterized by increased aggressive potential, overexpression of erbB (show EGFR Antibodies) receptor family members, and defective p53 (show TP53 Antibodies).
Structural Analysis of the Pin1-CPEB1 (show CPEB1 Antibodies) interaction and its potential role in CPEB1 (show CPEB1 Antibodies) degradation has been described.
Data show that Prolyl isomerase Pin1 is expressed in an epidermal growth factor receptor (EGFR (show EGFR Antibodies))-mutant lung cancer tissue that has undergone partial epithelial-mesenchymal transition (EMT (show ITK Antibodies)) and acquired resistance to EGFR (show EGFR Antibodies) tyrosine kinase (show TXK Antibodies) inhibitors (TKIs).
Report shows that PIN1 binds to and stabilizes HIF-1alpha (show HIF1A Antibodies), consequently enhancing the angiogenesis.
This shows that Pin1 is implemented in maintaining the susceptibility to the genotoxic drugs by controlling P-gp (show ABCB4 Antibodies) level as well as p53 (show TP53 Antibodies)-dependent apoptosis and cell cycle signaling pathways.
Activation of BAX (show BAX Antibodies) through the concerted action of cytosolic p53 (show TP53 Antibodies) and Pin1 may integrate cell stress signals to induce a direct apoptotic response.
The roles of the three tryptophan residues (W11, W34 and W73)in maintaining the structure and the function of Pin1
Expression of Pin1 was decreased at or above the Cd IC50 value and was inversely correlated with the level of phospho-Ser (show SIGLEC1 Antibodies)-GSK3alphabeta in oral squamous cell carcinoma.
ZBP-89 (show ZNF148 Antibodies) attenuates HDAC3 (show HDAC3 Antibodies) by increasing IkappaB degradation, dependent on Pin1 but independent of NF-Kappab (show NFKB1 Antibodies)
The data provide the first evidence that Pin 1 expression in the granulosa cells but not the theca cells changes during follicular development, and that FSH (show BRD2 Antibodies) stimulate the expression of the Pin 1 gene.
Peptidyl-prolyl cis/trans isomerases (PPIases) catalyze the cis/trans isomerization of peptidyl-prolyl peptide bonds. This gene encodes one of the PPIases, which specifically binds to phosphorylated ser/thr-pro motifs to catalytically regulate the post-phosphorylation conformation of its substrates. The conformational regulation catalyzed by this PPIase has a profound impact on key proteins involved in the regulation of cell growth, genotoxic and other stress responses, the immune response, induction and maintenance of pluripotency, germ cell development, neuronal differentiation, and survival. This enzyme also plays a key role in the pathogenesis of Alzheimer's disease and many cancers. Multiple alternatively spliced transcript variants have been found for this gene.
peptidylprolyl cis/trans isomerase, NIMA-interacting 1
, peptidylprolyl cis/trans isomerase, NIMA-interacting 1, pseudogene 1
, prolyl isomerase Pin1 b
, prolyl isomerase Pin1
, peptidylprolyl cis/trans isomerase, NIMA-interacting 1 b
, protein (peptidylprolyl cis/trans isomerase) NIMA-interacting 1
, peptidylprolyl cis/trans isomerase, NIMA-interacting 1 a
, peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
, PPIase Pin1
, protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1
, rotamase Pin1
, peptidyl-prolyl cis-trans isomerase Pin1