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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 (8) and many more products for this protein.
Showing 10 out of 219 products:
Human Polyclonal PIN1 Primary Antibody for ICC, IF - ABIN438364
Islam, Bae, Yoon, Woo, Baek, Kim, Uchida, Ryoo: Pin1 regulates osteoclast fusion through suppression of the master regulator of cell fusion DC-STAMP. in Journal of cellular physiology 2014
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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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Rat (Rattus) Polyclonal PIN1 Primary Antibody for ELISA, WB - ABIN251689
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
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
Pin1 plays important role in the cell cycle progression and increase oval cells proliferation which may be crucial in chronic liver injury.
in vivo functional analyses of Pin1 in the GFAP (show GFAP Antibodies)-tTA;TRE (show TREH Antibodies)-SmoA1 mouse model of Hedgehog (show SHH Antibodies)-driven medulloblastoma demonstrate that the loss of Pin1 impairs tumor development and dramatically increases survival.
Data, including data from studies conducted with knockout mice, suggest that Pin1 (prolyl isomerase 1) expression in pancreatic beta-cells is markedly elevated in obesity from diet high in fat/sucrose; Pin1 appears to be involved in proliferation of beta-cells and in regulation of secretion of insulin (show INS Antibodies); Pin1 interacts with Sik2 (salt-inducible kinase 2 (show SIK2 Antibodies)) to regulate calcium signaling.
Pin1 knockout in lupus-prone MRL lpr mi (show TLR7 Antibodies)ce pre (show TLR9 Antibodies)vents expres (show IRAK1 Antibodies)sion o (show IRF7 Antibodies)f lupus phenotype.
By interacting with PSD-95 (show DLG4 Antibodies), Pin1 dampens PSD-95 (show DLG4 Antibodies) ability to complex with NMDARs, thus negatively affecting NMDAR (show GRIN1 Antibodies) signaling and spine morphology.
Oral administration of brown algae polyphenol, a Pin1 inhibitor, reduced fat buildup in mice.
The findings provide evidence for a putative novel role of PIN1 in the development of the nociceptive system and indicate phosphorylation-mediated conformational changes as a mechanism for regulating the PRRXL1 (show DRGX Antibodies) role in the process.
Data show that peptidyl-prolyl isomerase (Pin1) inhibition inhibits high glucose (HG)-induced cardiac fibroblasts (CFs) proliferation and migration.
Pin1 knock-out mice exhibited disturbed neuronal projections from the cerebral cortex and reduced white matter tracks.
Pin1 plays a vital role on the development of vascular inflammation and atherosclerosis in ApoE (show APOE Antibodies)-/- mice.
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
in in silico gene expression analysis of human T-ALL samples we observed a significant correlation between Pin1 and Notch3 (show NOTCH3 Antibodies) expression levels, which may further suggest a key role of the newly identified Notch3 (show NOTCH3 Antibodies)-Pin1 axis in T-cell Acute Lymphoblastic Leukemia (T-ALL) aggressiveness and progression. Thus, combined suppression of Pin1 and Notch3 (show NOTCH3 Antibodies) proteins may be exploited as an additional target therapy for T-ALL
The study demonstrates the oncogenic role of PIN1 in NPC (show NPC1 Antibodies) tumorigenesis, and shows that its overexpression can enhance tumor cell growth via the upregulation of cyclinD1.
Pin1 expression was decreased remarkably in temporal lobe epilepsy patients compared to controls.
Data, including data from studies conducted with knockout mice, suggest that PIN1 (prolyl isomerase 1) expression in pancreatic beta-cells is markedly elevated in obesity from diet high in fat/sucrose; PIN1 appears to be involved in proliferation of beta-cells and in regulation of secretion of insulin (show INS Antibodies); PIN1 interacts with Sik2 (salt-inducible kinase 2 (show SIK2 Antibodies)) to regulate calcium signaling.
Knockdown of PIN1 potently blocks TLR-7 (show TLR7 Antibodies)/TLR-9 (show TLR9 Antibodies)/Pin1/IRAK-1 (show IRAK1 Antibodies)/IRF-7 (show IRF7 Antibodies) signaling in vitro.
Data indicate the complexity of interactions between Pin1 and activated IRAK1 (show IRAK1 Antibodies), suggesting that phosphorylation of neighboring Ser (show SIGLEC1 Antibodies)/Thr (show TRH Antibodies)-Pro motifs in proteins might provide competitive advantage at cellular concentrations for engaging with Pin1.
Surprisingly, the authors discover that Pin1 does not promote phosphorylated tau-induced microtubule formation in vitro, refuting the commonly accepted model in which Pin1 binding and catalysis on the A180 epitope restores the function of the Alzheimer's associated phosphorylated tau in tubulin (show TUBB Antibodies) assembly.
Importantly, site-specific measurements of Pin1-catalysis of CDK2 (show CDK2 Antibodies)/CycA (show CCNA2 Antibodies)-phosphorylated full-length tau reveal a number of sites that are catalyzed simultaneously with different efficiencies.
Results show that Pin1 plays a dual role, both positive and negative, in regulating NO production and in mediating the pathogenesis of cardiovascular diseases. Pin1 functions may vary a lot under different circumstances.
reciprocal regulation of Pin1 and XBP1s is associated with the activation of oncogenic pathways, and the relationship of PIN1 and XBP1 (show XBP1 Antibodies) may be an attractive target for novel therapy in cancers
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