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Peptidyl-prolyl cis/trans isomerases (PPIases) catalyze the cis/trans isomerization of peptidyl-prolyl peptide bonds. Zusätzlich bieten wir Ihnen Peptidylprolyl Cis/trans Isomerase, NIMA-Interacting 1 Proteine (18) und Peptidylprolyl Cis/trans Isomerase, NIMA-Interacting 1 Kits (9) und viele weitere Produktgruppen zu diesem Protein an.
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Human Polyclonal PIN1 Primary Antibody für 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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Rat (Rattus) Polyclonal PIN1 Primary Antibody für 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
Downregulation of miR (zeige MLXIP Antikörper)-370 in esophageal squamous cell carcinoma is associated with cancer progression and promotes cancer cell proliferation via upregulating PIN1, which might be a potential therapeutic target and adverse prognostic factor in the clinic.
Study investigated the allosteric mechanism of full-length Pin1 using several microsecond-long molecular dynamics simulations; show that binding of the substrate to the WW domain (zeige DRP2 Antikörper) is directly coupled to the dynamics of the catalytic domain, causing rearrangement of the residue-residue contact dynamics from the WW domain (zeige DRP2 Antikörper) to the catalytic domain.
Pin1 is a fast-acting enzyme which may be utilised by cells to protect the phosphorylation state of Tissue Factor (zeige F3 Antikörper) (TF) in activated cells prolonging TF activity and release, and therefore ensuring adequate haemostasis.
statistically significant correlation didn't exist between serum level of PIN1 and the systolic and diastolic blood pressure, between serum level of eNOS (zeige NOS3 Antikörper) and diastolic blood pressure in the norm tension Alzheimer's disease patients, between serum levels of PIN1, eNOS (zeige NOS3 Antikörper) and systolic blood pressure, and between serum eNOS (zeige NOS3 Antikörper) and systolic and diastolic blood pressure in the patients with hypertension.
Studies results suggest that loss of peptidyl-prolyl isomerase (Pin1) activity could lead to the loss of synaptic plasticity in the development of Alzheimer disease.
Pin1 induces the ADP-induced migration of human dental pulp cells through P2Y1 (zeige P2RY1 Antikörper) stabilization.
In this study, we were aimed to investigate whether the cross talk between pin1 and Notch1 (zeige NOTCH1 Antikörper) has a role in this event. Our results indicated that the expression level of Pin1 in resistant SKBR3 cells increased by about twofold relative to sensitive SKBR3 cells. Besides, Pin1 inhibition via juglone reduced the extent of proliferation, colony formation and migration capacity of resistant SKBR3 cells
Parallel folding pathways of PIN1 Fip35 WW domain (zeige DRP2 Antikörper) have been explained by infrared spectra and their computer simulations.
High PIN1 expression is associated with stomach neoplasms.
Pin1 is a novel regulator of ATF1 (zeige AFT1 Antikörper) at Thr184.
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 (zeige WEE1 Antikörper)-box
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 (zeige BRD2 Antikörper) stimulate the expression of the Pin 1 gene.
Pin1 serves as a modulator of SERCA2a (zeige ATP2A2 Antikörper) and Na(2+)/Ca(2 (zeige CA2 Antikörper)+) exchanger 1 Ca(2 (zeige CA2 Antikörper)+) handling proteins, with loss of function resulting in impaired cardiomyocyte relaxation.
These results suggest that Pin1 promotes the progression of the mitotic cell cycle of SSC (zeige CYP11A1 Antikörper) in steady-state, which is required for the sperm production from SSCs.
Pin1 silencing in lymphomas retarded disease progression in mice, making Pin1 an attractive therapeutic target in Myc (zeige MYC Antikörper)-driven tumors.
Pin1 enhances adipocyte differentiation by regulating the function of PPARgamma (zeige PPARG Antikörper).
Pin1 serves as a positive regulatory molecule of proplatelet formation of megakaryocytes by enhancing the function of phosphorylated tau.
Direct delivery of recombinant Pin1 via fibroin nanoparticle encapsulated cationic lipid complex successfully rescued osteoblast differentiation of pin-1 deficient cells.
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 (zeige GFAP Antikörper)-tTA;TRE (zeige TREH Antikörper)-SmoA1 mouse model of Hedgehog (zeige SHH Antikörper)-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 (zeige INS Antikörper); Pin1 interacts with Sik2 (salt-inducible kinase 2 (zeige SIK2 Antikörper)) to regulate calcium signaling.
Pin1 knockout in lupus-prone MRL lpr (zeige FAS Antikörper) mice prevents expression of lupus phenotype.
analysis of Pin1 overexpression showed alterations on zebrafish development and the presence of p53 (zeige TP53 Antikörper)-dependent apoptosis. Collectively, our results suggest that specific mechanisms are operated in different cell types to regulate Pin1 function
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.
, peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
, protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1
, rotamase Pin1
, protein (peptidylprolyl cis/trans isomerase) NIMA-interacting 1
, prolyl isomerase Pin1
, peptidylprolyl cis/trans isomerase, NIMA-interacting 1 a
, peptidyl-prolyl cis-trans isomerase Pin1
, prolyl isomerase Pin1 b
, peptidylprolyl cis/trans isomerase, NIMA-interacting 1 b
, Pin1-type peptidyl-prolyl cis/trans isomerase
, Rotamase Pin1