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Validated All-in-One™ qPCR Primer for PIN1(NM_006221.3) Search again
Product ID:
HQP013168
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
DOD, UBL5
Gene Description:
peptidylprolyl cis/trans isomerase, NIMA-interacting 1
Target Gene Accession:
NM_006221.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
The human PIN1 gene encodes an essential nuclear peptidylprolyl cis-trans isomerase (PPIase; EC 5.2.1.8) involved in regulation of mitosis. PIN1 belongs to a class of PPIases that includes the E. coli parvulin, yeast Ess1, and Drosophila dodo (dod) gene products (Lu et al., 1996 [PubMed 8606777]).[supplied by OMIM].
Gene References into function
- binds phosphorylated hSpt5
- induction of expression by IGF-1 and role in promoting cell cycle S-phase entry
- Interactions between protein kinase CK2 and Pin1. Evidence for phosphorylation-dependent interactions.
- A signaling mechanism is proposed, whereby Pin1 specifically isomerizes only the phosphorylated Ser/Thr-Pro bonds in proteins, regulating protein function by inducing conformational changes following phosphorylation.
- conformational change of Bcl2 due to association with peptidyl prolyl isomerase can contribute to irreversible apoptotic signaling.
- Pin1 is an E2F target gene that is essential for the Neu/Ras-induced transformation of mammary epithelial cells through activation of cyclin D1
- 1H, 13C and 15N backbone resonance assignment of the peptidyl-prolyl cis-trans isomerase Pin1.
- role in regulating p53 function during DNA damage
- The prolyl isomerase Pin1 is a regulator of p53 in genotoxic response
- following stress-induced phosphorylation, p53 needs to form a complex with Pin1 and to undergo a conformational change to fulfil its biological roles
- Neurons containing Pin1 granules were devoid of neurofibrillary tangles. Granular accumulation of Pin1 may correspond to an absence of neurofibrillary lesions in these cells and might be associated with other mechanisms of neuronal degeneration.
- Pin1 is overexpressed in oral squamous cell carcinoma and its levels correlate with cyclin D1 overexpression
- Peptide binding induces large scale changes in inter-domain mobility in human Pin1
- analysis of pin1 domain architecture and substrate binding
- Pin1 is a regulator of Cyclin D1 expression in oral squamous cell carcinoma and might have a role in oncogenesis
- Appearance of Pin1 granules in the early stages of Alzheimer's disease, Pick's disease, and FTDP-17 (P301L) tauopathy implicates Pin1 in their pathogenesis, but not in progressive supranuclear palsy.
- Data show that NF-kappaB function is regulated by Pin1-mediated prolyl isomerization and ubiquitin-mediated proteolysis of its p65/RelA subunit.
- An additional interaction site between Pin1 and neuronal Tau protein identified at phospho-Thr212-Pro213 of Tau raises the question of functional cooperativity between the WW and catalytic domain of Pin1 while it interacts with hyperphosphorylated Tau.
- Pin1 can suppress transformed phenotypes and inhibit tumor cell growth
- The ability of c-Abl and p300 to increase p73 stability and transcriptional activity requires Pin1. Pin1 is essential for activation of the apoptotic response by endogenous p73.
- Pin1 redistribution and shortfalls occur in frontotemporal dementias characterized by abnormal protein aggregates of tau and other cytoskeletal proteins. may be unifying, contributory factor towards neuronal death in these dementias.
- Pin1 binding was favored when at least two of the three threonine residues were phosphorylated
- Phosphorylation-dependent prolyl isomerization by Pin1 remains a unique mode for the modulation of signal transduction [review].
- Taken together, these results provide evidence supporting a direct link between oxidative damage to neuronal Pin1 and the pathobiology of Alzheimer disease.
- Mutations in proline 82 of p53 impair its activation by PIN1 and CHK2 in response to DNA damage.
- We conclude that Pin1 is a very well conserved gene, whose rare nucleotide variations have no effect on the individual genetic risk for AD.
- c-Fos represents a novel target for the isomerizing activity of Pin1, which has a role in the mechanism by which c-Jun and c-Fos cooperate to regulate AP-1-dependent gene transcription
- Overexpression of Pin1 and beta-catenin may be closely related with the development and/or progression of colorectal carcinoma and further supports that Pin1 overexpression might contribute to the upregulation of beta-catenin.
- Thus, Pin1 interacts with C99 and promotes its gamma-cleavage, generating Abeta40 and Abeta42.
- Pin1 functions as a transcriptional coactivator of nuclear receptors by modulating SRC-3 coactivator protein-protein complex formation and by also promoting the turnover of the activated SRC-3 oncoprotein.
- Pin1 is a key mediator of granulocyte-macrophage colony-stimulating factor (GM-CSF) production
- High Pin1 expression in primary prostate cancer markedly inhibits the beta-catenin interaction with androgen receptor.
- Pin1 overexpression correlates with centrosome amplification in breast cancer tissues.
- we found that Pin1 could interact with Nek6, one of the human NIMA-related kinases (Neks). Significant correlations between Nek6 and Pin1 mRNA expression levels in 40 pairs of hepatocellular carcinoma cases.
- Pin1 level was found strongly increased during neuronal differentiation and tightly correlated with Tau dephosphorylation at Thr231
- two promoter polymorphisms (rs2233678 and rs2233679)in PIN1 do not make a significant contribution to AD risk.
- Pin1 expression is correlated with cyclinD1 expression and may have a role in esophageal squamous cell carcinoma
- High levels of Pin1 expression is associated with salivary adenoid cystic carcinoma
- Pin1 may not play a role in the development or progression of gastric cancer.
- In human neuroblastoma cells, Pin1 is downregulated in response to endoplasmic reticulum stress in neuroblastoma cells.
- Pin1 is implicated in granulocyte-macrophage colony-stimulating factor (GM-CSF) mRNA turnover, accumulation, and cytokine production by human T lymphocytes.
- In this review, the authors show that Pin1 specifically regulates the degradation of amyloid precursor protein (APP), and they propose an alternative model for Pin1 regulation of APP processing.
- A model for the reaction trajectory of Pin1 catalysis.
- Pin1 deregulation may provide a link between formation of tangles and plaques in Alzheimer's disease [review]
- These results suggest that sequences of recognition motifs may reflect natural selection of not only chemical properties but also dynamic modes that augment specificity.
- This first side-chain dynamics study of human Pin1 lays the foundation for analysis of how different substrates elicit different dynamic responses from Pin1.
- PIN1 overexpression in hepatocellular carcinoma and its significance is reported.
- the interaction of Pin1 with chromatin is greatly elevated in G2/M phase, and this correlates with the presence on chromosomes of several mitotic phosphoproteins, especially topoisomerase (Topo) IIalpha
- Che-1 as a new Pin1 and HDM2 target and confirm its important role in the cellular response to DNA damage.
- none of the six common SNPs in Pin1, including the two promoter SNPs, rs223678 and rs223679, was associated with increased late-onset Alzheimer's disease risk
- PIN1 down-regulates BIRC5.
- Isomerization of lys-ser-pro repeat residues that are abundant in NF-H tail domains by Pin1 can regulate NF-H phosphorylation.
- Interaction between Pin1 and hepatitis B virus protein HBx leads to hepatocarcinogenesis.
- Replacement of two nearest neighbor non-hydrogen-bonded residues on adjacent beta-strands with tryptophan residues increases beta-sheet thermodynamic stability of the Pin1 WW domain.
- Data suggest that Pin1 is required for efficient loading of p53 on target promoters upon stress, and that after phosphorylation of p53 triggered by cytotoxic stimuli, Pin1 mediates p53's dissociation from iASPP, promoting cell death.
- Pin1-mediated prolyl isomerization plays an important role in the negative regulation of Daxx and thereby inhibits the oxidative stress-induced cellular apoptotic response, particularly in malignant tumor cells where Pin1 is often overexpressed.
- PIN1 modulates RNA polymerase II activity during the transcription cycle.
- polymorphisms of the PIN-1 gene can affect neurodegeneration and its clinical progression.
- Binding to Pin1 results in degradation of PML in a phosphorylation-dependent manner. Degradation of PML due to Pin1 acts both to protect a breast cancer tumor cell line from hydrogen peroxide-induced death and to increase the rate of proliferation.
- Recombinant Pin1 was modulated by I-2, and binding to individual mitotic phosphoproteins was increased, decreased or unaffected by I-2, showing that I-2 allosterically modifies Pin1 specificity.
- Pin1 promoted the stability of TGF-beta1 mRNA in human Eos.
- These results imply that Pin1 stimulates VEGF expression by activating HIF-1alpha and AP-1, and suggest that Pin1 is a potential therapeutic target of angiogenesis during cancer development.
- Pin1 as a possible modulator of stress-induced NF-H phosphorylation as seen in neurodegenerative disorders like AD and amyotrophic lateral sclerosis
- Erk could phosphorylate Mcl-1 at two consensus residues, Thr 92 and 163, which is required for the association of Mcl-1 and Pin1, resulting in stabilization of Mcl-1
- Results show that the prolyl isomerase Pin1 modulates APOBEC3G expression.
- Pin1 is identified as a novel negative FOXO regulator, interconnecting FOXO phosphorylation and monoubiquitination in response to cellular stress to regulate p27(kip1).
- H59 and H157 are not required for hydrogen bonding within the active site, and in contrast to the active site C113, they do not participate directly in catalysis.
- Point mutations of several basic amino acids in the PPIase domain of Pin1 significantly compromise its nuclear localization.
- In human breast cancers, we observed a strong correlation between Pin1 overexpression and high levels of activated Notch1. Thus, the molecular circuitry established by Notch1 and Pin1 may have a key role in cancer.