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#26370088   2015/10/31 Save this To Up

Two hydrophobic residues can determine the specificity of mitogen-activated protein kinase docking interactions.

MAPKs bind to many of their upstream regulators and downstream substrates via a short docking motif (the D-site) on their binding partner. MAPKs that are in different families (e.g. ERK, JNK, and p38) can bind selectively to D-sites in their authentic substrates and regulators while discriminating against D-sites in other pathways. Here we demonstrate that the short hydrophobic region at the distal end of the D-site plays a critical role in determining the high selectivity of JNK MAPKs for docking sites in their cognate MAPK kinases. Changing just 1 or 2 key hydrophobic residues in this submotif is sufficient to turn a weak JNK-binding D-site into a strong one, or vice versa. These specificity-determining differences are also found in the D-sites of the ETS family transcription factors Elk-1 and Net. Moreover, swapping two hydrophobic residues between these D-sites switches the relative efficiency of Elk-1 and Net as substrates for ERK versus JNK, as predicted. These results provide new insights into docking specificity and suggest that this specificity can evolve rapidly by changes to just 1 or 2 amino acids.

1875 related Products with: Two hydrophobic residues can determine the specificity of mitogen-activated protein kinase docking interactions.

Multiple organ cancer tis Breast cancer membrane pr Docking protein 3 antibod Native Canine CASQ2 Prote Native Canine CASQ2 Prote Native Canine CASQ2 Prote Recombinant Canine ApoJ C Recombinant Canine ApoJ C Recombinant Canine ApoJ C Recombinant Canine ApoJ C Recombinant Canine ApoJ C Recombinant Canine ApoJ C

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#25100239   2014/11/26 Save this To Up

A switch from canonical to noncanonical Wnt signaling mediates early differentiation of human neural stem cells.

Wnt/β-catenin signaling is essential for neurogenesis but less is known about β-catenin-independent Wnt signals. We show here that Wnt/activator protein-1 (AP-1) signaling drives differentiation of human embryonic stem cell and induced pluripotent stem cell-derived neural progenitor cells. Neuronal differentiation was accompanied by a reduction in β-catenin/Tcf-dependent transcription and target gene expression, increased levels and/or phosphorylation of activating transcription factor 2 (ATF2), cyclic AMP response element-binding protein, and c-Jun, and increased AP-1-dependent transcription. Inhibition of Wnt secretion using the porcupine inhibitors IWP-2 and Wnt-C59 blocked neuronal differentiation, while activation or inhibition of Wnt/β-catenin signaling had no effect. Neuronal differentiation increased expression of several Wnt genes, including WNT3A, silencing of which reduced differentiation. Addition of recombinant Wnt-3a to cells treated with IWP-2 or Wnt-C59 increased AP-1 levels and restored neuronal differentiation. The effects of Wnt-3a could not be blocked by addition of Dkk-1 or IWR-1, suggesting the involvement of noncanonical signaling. Consistent with this, restoration of neuronal differentiation by Wnt-3a was reduced by inhibition of Jun N-terminal kinase (JNK) and by gene silencing of ATF2. Together, these observations suggest that β-catenin-independent Wnt signals promote neural stem/progenitor cell differentiation in a signaling pathway involving Wnt-3a, JNK, and ATF2.

1281 related Products with: A switch from canonical to noncanonical Wnt signaling mediates early differentiation of human neural stem cells.

Epidermal Growth Factor ( Epidermal Growth Factor ( Mouse Anti-Human CD34 Tar Anti C Reactive Protein A Growth Differentiation Fa Macrophage Colony Stimula Macrophage Colony Stimula glial cells missing homol TOM1-like protein 2 antib WNT11 antibody Source Rab TOK-1 alpha antibody Sour WNT10A antibody Source Ra

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#24344258   2014/01/08 Save this To Up

Epstein-Barr virus nuclear antigen 3C binds to BATF/IRF4 or SPI1/IRF4 composite sites and recruits Sin3A to repress CDKN2A.

Epstein-Barr virus nuclear antigen 3C (EBNA3C) repression of CDKN2A p14(ARF) and p16(INK4A) is essential for immortal human B-lymphoblastoid cell line (LCL) growth. EBNA3C ChIP-sequencing identified >13,000 EBNA3C sites in LCL DNA. Most EBNA3C sites were associated with active transcription; 64% were strong H3K4me1- and H3K27ac-marked enhancers and 16% were active promoters marked by H3K4me3 and H3K9ac. Using ENCODE LCL transcription factor ChIP-sequencing data, EBNA3C sites coincided (±250 bp) with RUNX3 (64%), BATF (55%), ATF2 (51%), IRF4 (41%), MEF2A (35%), PAX5 (34%), SPI1 (29%), BCL11a (28%), SP1 (26%), TCF12 (23%), NF-κB (23%), POU2F2 (23%), and RBPJ (16%). EBNA3C sites separated into five distinct clusters: (i) Sin3A, (ii) EBNA2/RBPJ, (iii) SPI1, and (iv) strong or (v) weak BATF/IRF4. EBNA3C signals were positively affected by RUNX3, BATF/IRF4 (AICE) and SPI1/IRF4 (EICE) cooccupancy. Gene set enrichment analyses correlated EBNA3C/Sin3A promoter sites with transcription down-regulation (P < 1.6 × 10(-4)). EBNA3C signals were strongest at BATF/IRF4 and SPI1/IRF4 composite sites. EBNA3C bound strongly to the p14(ARF) promoter through SPI1/IRF4/BATF/RUNX3, establishing RBPJ-, Sin3A-, and REST-mediated repression. EBNA3C immune precipitated with Sin3A and conditional EBNA3C inactivation significantly decreased Sin3A binding at the p14(ARF) promoter (P < 0.05). These data support a model in which EBNA3C binds strongly to BATF/IRF4/SPI1/RUNX3 sites to enhance transcription and recruits RBPJ/Sin3A- and REST/NRSF-repressive complexes to repress p14(ARF) and p16(INK4A) expression.

2220 related Products with: Epstein-Barr virus nuclear antigen 3C binds to BATF/IRF4 or SPI1/IRF4 composite sites and recruits Sin3A to repress CDKN2A.

FIV Core Ag, recombinant Toxoplasma gondii MIC 3 r Toxoplasma gondii P24 (GR Toxoplasma gondii P29 (GR Toxoplasma gondii P30 (SA Human Epstein-Barr Virus Mouse Epstein-Barr Virus Recombinant Tobacco Etch Recombinant Tobacco Etch Recombinant Tobacco Etch Cell Meter™ Fluorimetri Normal human top 10 organ

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#24338393   2013/12/16 Save this To Up

Critical evaluation of transcription factor Atf2 as a candidate modulator of alcohol preference in mouse and human populations.

In prior work, congenic strains carrying the DBA/2Igb (D2) region of chromosome 2 (Chr2) for alcohol preference were bred onto a C57BL/6Ibg (B6) background and as predicted were found to reduce voluntary consumption. Subsequently, interval-specific congenic recombinant strains (ISCRS) were generated and also tested. These ISCRS strains reduced the quantitative trait loci (QTL) interval to a comparatively small 3.4 Mb region. Here, we have exploited an integrative approach using both murine and human populations to critically evaluate candidate genes within this region. First, we used bioinformatics tools to search for genes relevant to alcohol preference within the QTL region. Second, we searched for single nucleotide polymorphisms (SNPs) within exons of every gene in this region. Third, we conducted follow-up microarray analyses to identify differentially expressed genes between the B6 and ISCRS strains in mice from each group. Fourth, we analyzed correlations between the expression level of candidate genes and phenotypes of alcohol preference in a large family of BXD recombinant inbred strains derived from B6 and D2. Finally, we evaluated SNP segregation in both BXD mouse strains and in humans who were heavy alcohol drinkers or non-drinkers. Among several potential candidate genes in this region, we identified activating transcription factor 2 (Atf2) as the most plausible gene that would influence alcohol preference. However, the candidacy of Atf2 was only weakly supported when we used a genetic network approach and by focused reanalysis of genome-wide association study data from European-American and African-American populations. Thus, we cannot conclude that Atf2 plays a role in the regulation of the QTL of mouse Chr2.

1597 related Products with: Critical evaluation of transcription factor Atf2 as a candidate modulator of alcohol preference in mouse and human populations.

Goat Anti-Human, Mouse As Goat Anti-Human, Mouse, R Mouse Anti-Insulin-Like G anti CD16 monoclonal anti Mouse anti-human type I c Goat Anti-Human, Mouse HI Goat Anti-Human FTO (Mous Goat Anti-Human, Mouse EB Goat Anti-Human, Mouse, R Goat Anti-Human, Mouse, R Goat Anti-Human, Mouse AR Goat Anti-Human Apolipopr

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#24106799   2013/12/09 Save this To Up

Conductometric monitoring of protein-protein interactions.

Conductometric monitoring of protein-protein and protein-sterol interactions is here proved feasible by coupling quartz crystal microbalance with dissipation monitoring (QCM_D) to nucleic acid programmable protein arrays (NAPPA). The conductance curves measured in NAPPA microarrays printed on quartz surface allowed the identification of binding events between the immobilized proteins and the query. NAPPA allows the immobilization on the quartz surface of a wide range of proteins and can be easily adapted to generate innumerous types of biosensors. Indeed multiple proteins on the same quartz crystal have been tested and envisaged proving the possibility of analyzing the same array for several distinct interactions. Two examples of NAPPA-based conductometer applications with clinical relevance are presented herein, the interaction between the transcription factors Jun and ATF2 and the interaction between Cytochrome P540scc and cholesterol.

1170 related Products with: Conductometric monitoring of protein-protein interactions.

Myelin Basic Protein Heat Shock Protein 70 (H Heat Shock Protein 70 (H nm23 (NDPK-A Protein); C nm23 (NDPK-A Protein); C MIC2 Gene Protein, CD99; MIC2 Gene Protein, CD99; Glial Fibrillary Acidic Glial Fibrillary Acidic nm23 (NDPK-A Protein); C MIC2 Gene Protein, CD99; Glial Fibrillary Acidic

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#22980665   2012/09/17 Save this To Up

[Construction and identification of small interfering RNA expression vector targeting ATF-2 gene].

To construct an eukaryotic expression vector for RNA interference targeting activating transcription factor 2 (ATF-2) gene, and explore its effect on proliferation and apoptosis of HepG2 cells.

1825 related Products with: [Construction and identification of small interfering RNA expression vector targeting ATF-2 gene].

pCdgCAT Mammalian CAT Exp pCAMBIA0305.1 Vector, (Gu pCAMBIA0380 Vector (No Re pCAMBIA1391Z Vector (gusA pYLEX1 - Expression Vect Lenti RNAi Vector Lineari Lenti EGFP RNAi Vector Li pCMVbeta Mammalian lacZ E pSV40beta Mammalian lacZ pCMVbeta Mammalian lacZco pSV40beta Mammalian lacZc pCMVbeta Mammalian lacZnl

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#22278222   2012/03/12 Save this To Up

Adenosine deaminase acting on RNA 1 (ADAR1) suppresses the induction of interferon by measles virus.

ADAR1, the interferon (IFN)-inducible adenosine deaminase acting on RNA, catalyzes the C-6 deamination of adenosine (A) to produce inosine (I) in RNA substrates with a double-stranded character. Because double-stranded RNA is a known inducer of IFN, we tested the role of ADAR1 in IFN induction following virus infection. HeLa cells made stably deficient in ADAR1 (ADAR1(kd)) were compared to vector control (CON(kd)) and protein kinase PKR-deficient (PKR(kd)) cells for IFN-β induction following infection with either parental (wild-type [WT]) recombinant Moraten vaccine strain measles virus (MV) or isogenic knockout mutants deficient for either V (V(ko)) or C (C(ko)) protein expression. We observed potent IFN-β transcript induction in ADAR1(kd) cells by all three viruses; in contrast, in ADAR1-sufficient CON(kd) cells, only the C(ko) mutant virus was an effective inducer and the IFN-β RNA induction was amplified by PKR. The enhanced IFN-β transcript-inducing capacity of the WT and V(ko) viruses seen in ADAR1-deficient cells correlated with the enhanced activation of PKR, IFN regulatory factor IRF3, and activator of transcription ATF2, reaching levels similar to those seen in C(ko) virus-infected cells. However, the level of IFN-β protein produced was not proportional to the level of IFN-β RNA but rather correlated inversely with the level of activated PKR. These results suggest that ADAR1 functions as an important suppressor of MV-mediated responses, including the activation of PKR and IRF3 and the induction of IFN-β RNA. Our findings further implicate a balanced interplay between PKR and ADAR1 in modulating IFN-β protein production following virus infection.

2889 related Products with: Adenosine deaminase acting on RNA 1 (ADAR1) suppresses the induction of interferon by measles virus.

Measles Virus Nucleoprote Recombinant Measles Virus Recombinant Measles Virus Recombinant Measles Virus Recombinant Measles Virus Recombinant Measles Virus Recombinant Measles Virus Recombinant Measles Virus Recombinant Measles Virus Adenosine Deaminase antib Rabbit Anti-Hepatitis C V Rabbit Anti-Hepatitis C V

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#21384452   2011/04/14 Save this To Up

GST pi modulates JNK activity through a direct interaction with JNK substrate, ATF2.

Human GSTpi, an important detoxification enzyme, has been shown to modulate the activity of JNKs by inhibiting apoptosis and by causing cell proliferation and tumor growth. In this work, we describe a detailed analysis of the interaction in vitro between GSTpi and JNK isoforms (both in their inactive and active, phosphorylated forms). The ability of active JNK1 or JNK2 to phosphorylate their substrate, ATF2, is inhibited by two naturally occurring GSTpi haplotypes (Ile105/Ala114, WT or haplotype A, and Val105/Val114, haplotype C). Haplotype C of GSTpi is a more potent inhibitor of JNK activity than haplotype A, yielding 75-80% and 25-45% inhibition, respectively. We show that GSTpi is not a substrate of JNK, as was earlier suggested by others. Through binding studies, we demonstrate that the interaction between GSTpi and phosphorylated, active JNKs is isoform specific, with JNK1 being the preferred isoform. In contrast, GSTpi does not interact with unphosphorylated, inactive JNKs unless a JNK substrate, ATF2, is present. We also demonstrate, for the first time, a direct interaction: between GSTpi and ATF2. GSTpi binds with similar affinity to active JNK + ATF2 and to ATF2 alone. Direct binding experiments between ATF2 and GSTpi, either alone or in the presence of glutathione analogs or phosphorylated ATF2, indicate that the xenobiotic portion of the GSTpi active site and the JNK binding domain of ATF2 are involved in this interaction. Competition between GSTpi and active JNK for the substrate ATF2 may be responsible for the inhibition of JNK catalysis by GSTpi.

2840 related Products with: GST pi modulates JNK activity through a direct interaction with JNK substrate, ATF2.

KinaseSTAR JNK Activity S KinaseSTAR JNK Activity A SAPK JNK (Phospho Thr183) SAPK JNK (Ab 183) Antibod Recombinant Human JNK2, a Recombinant Human JNK2, a Recombinant Human JNK2, a Recombinant Human JNK2, a Recombinant Human JNK2, a Recombinant Human JNK2, a JNK1 antibody Source Rabb Phospho-JNK/SAPK Antibody

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#21128306   2010/12/24 Save this To Up

An ATF2-based luciferase reporter to monitor non-canonical Wnt signaling in Xenopus embryos.

Non-canonical/planar cell polarity (PCP) Wnt signaling plays important roles in embryonic development and tissue homeostasis, and is implicated in human disease. Monitoring Wnt/PCP signaling relies mostly on semi-quantitative bioassays or biochemical analysis. Here we describe a luciferase reporter assay based on an ATF2 response element, which faithfully monitors non-canonical Wnt signaling in Xenopus embryos. The assay is simple, quantitative, and robust. It can be used to detect non-canonical Wnt signaling changes following gain and loss of function of pathway components, including Wnt, Frizzled, Ror2, Disheveled, Rac1, MKK7, and JNK. Wnt/PCP signaling has recently been implicated in left-right asymmetry and our reporter assay suggests that in gastrula embryos there is a right-ward bias in Wnt/PCP signaling. We also mapped Wnt/PCP signaling in the early Xenopus embryo and find that it peaks in the dorso-vegetal region, paralleling Wnt/β-catenin signaling.

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Wnt Signaling Pathway TCF AKT PKB Signaling Phospho AMPK Signaling Phospho-Sp ErbB Her Signaling Phosph ERK Signaling Phospho-Spe GPCR Signaling to MAPK ER IGF-1R Signaling Phospho- NF-kB II Phospho-Specific p53 Signaling Phospho-Spe T-Cell Receptor Signaling TGF-Beta Signaling Phosph MAPK3 & ATF2 Protein Prot

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#20709173   2010/11/24 Save this To Up

Activation by phosphorylation and purification of human c-Jun N-terminal kinase (JNK) isoforms in milligram amounts.

c-Jun N-terminal kinases (JNKs) are part of the mitogen-activated protein kinase (MAPK) signaling cascade. They are activated through dual phosphorylation of two residues in the activation loop, a threonine and a tyrosine, by MAP2 kinases (MKK4 and 7) in response to various extracellular stresses such as UV or osmotic shock, as well as by cytokines and growth factors. Only small amounts of phosphorylated, active JNKs have previously been produced because of difficulties in expressing these phosphorylated kinases in Escherichia coli, which lack the appropriate upstream kinases. We have now established a novel activation and purification method that allows for reproducible production of milligram amounts of active, phosphorylated JNKs suitable for a variety of enzymatic, biophysical and structural characterizations. We utilize N-terminally His-tagged MKK4 that is coexpressed in E. coli with a constitutively active form of MEKK1. This phosphorylated, active His-MKK4 is purified by Ni-NTA chromatography and used to phosphorylate milligram amounts of three different isoforms of human JNKs (JNK1α1, JNK1α2 and JNK2α2) that had separately been expressed and purified from E. coli in their inactive forms. These in vitro activated JNKs are phosphorylated on both residues (T183, Y185) in their activation loops and are active towards their substrate, ATF2.

2000 related Products with: Activation by phosphorylation and purification of human c-Jun N-terminal kinase (JNK) isoforms in milligram amounts.

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