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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 (19) and Peptidylprolyl Cis/trans Isomerase, NIMA-Interacting 1 Kits (8) and many more products for this protein.
Showing 10 out of 212 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
Show all 2 Pubmed References
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
These results suggest that Pin1 promotes the progression of the mitotic cell cycle of SSC (show CYP11A1 Antibodies) 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 (show MYC Antibodies)-driven tumors.
Pin1 enhances adipocyte differentiation by regulating the function of PPARgamma (show PPARG Antibodies).
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 (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.
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
Pin1 is a fast-acting enzyme which may be utilised by cells to protect the phosphorylation state of Tissue Factor (show F3 Antibodies) (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 (show NOS3 Antibodies) and diastolic blood pressure in the norm tension Alzheimer's disease patients, between serum levels of PIN1, eNOS (show NOS3 Antibodies) and systolic blood pressure, and between serum eNOS (show NOS3 Antibodies) 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 (show P2RY1 Antibodies) stabilization.
In this study, we were aimed to investigate whether the cross talk between pin1 and Notch1 (show NOTCH1 Antibodies) 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 (show DRP2 Antibodies) 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 (show AFT1 Antibodies) at Thr184.
The dynamic basis for signal propagation in Pin1 N-terminal binding domain WW has been described.
The endoplasmic reticulum (ER) stress decreased Pin1 expression through p53 (show TP53 Antibodies) activation, and this mechanism may be associated with ER stress-induced cell death. These data reported here support the importance of Pin1 as a potential target molecule mediating tumor development.
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.
, 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