Search results for: Expression Systems
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met1 DNA Methyltransferase Controls TERT Gene Expression: A New Insight to The Role of Telomerase in Development.DNA methylation systems are essential for proper embryo development. Methylation defects lead to developmental abnormalities. Furthermore, changes in telomerase gene expression can affect stability of chromosomes and produces abnormal growth. Therefore, defects in both methylation and telomerase gene expression can lead to developmental abnormalities. We hypothesized that mutation in the methylation systems may induce developmental abnormalities through changing telomerase gene expression.
1994 related Products with: met1 DNA Methyltransferase Controls TERT Gene Expression: A New Insight to The Role of Telomerase in Development.DNA (cytosine 5) methyltr FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu FDA Standard Frozen Tissu Mouse Anti-Insulin-Like G EpiQuik Histone Methyltra Oral squamous cell cancer Gene Expression: Rat P45 Multiple organ tumor tiss EpiQuik Histone Methyltra Toxoplasma gondii GRA8, r
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Zoledronate rescues immunosuppressed monocytes in sepsis patients.Severe sepsis is often accompanied by a transient immune paralysis, which is associated with enhanced susceptibility to secondary infections and poor clinical outcomes. The functional impairment of antigen-presenting cells is considered to be a major hallmark of this septic immunosuppression, with reduced HLA-DR expression on circulating monocytes serving as predictor of mortality. Unconventional lymphocytes like γδ T cells have the potential to restore immune defects in a variety of pathologies including cancer but their use to rescue sepsis-induced immunosuppression has not been investigated. Our own previous work showed that Vγ9/Vδ2 γδ T cells are potent activators of monocytes from healthy volunteers in vitro, and in individuals with osteoporosis after first-time administration of the anti-bone resorption drug zoledronate in vivo. We show here that zoledronate readily induces upregulation of HLA-DR, CD40 and CD64 on monocytes from both healthy controls and sepsis patients, which could be abrogated by neutralising the pro-inflammatory cytokines IFN-γ and TNF-α in the cultures. In healthy controls, the upregulation of HLA-DR on monocytes was proportional to the baseline percentage of Vγ9/Vδ2 T cells in the PBMC population. Of note, a proportion of sepsis patients studied here did not show a demonstrable response to zoledronate, predominantly patients with microbiologically confirmed bloodstream infections, compared to sepsis patients with more localised infections marked by negative blood cultures. Taken together, our results suggest that zoledronate can, at least in some individuals, rescue immunosuppressed monocytes during acute sepsis and thus may help improve clinical outcomes during severe infection.
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Stripe Rust Effector PstGSRE1 Disrupts Nuclear Localization of ROS-Promoting Transcription Factor TaLOL2 to Defeat ROS-Induced Defense in Wheat.Puccinia striiformis f. sp. tritici (Pst), a biotrophic plant pathogen, secretes numerous effectors to modulate host defense systems. Understanding the molecular mechanisms of Pst effectors that regulate wheat immunity is of great importance for the development of novel strategies for durable control of stripe rust. In this study, we identified a glycine-serine-rich effector gene, PstGSRE1, which is highly induced during early infection. Transgenic expression of PstGSRE1 RNAi constructs in wheat significantly reduced virulence of Pst and increased HO accumulation in wheat. PstGSRE1 was shown to target the ROS-associated transcription factor TaLOL2, a positive regulator of wheat immunity. PstGSRE1 disrupted the nuclear localization of TaLOL2 and suppressed ROS-mediated cell death induced by TaLOL2, thus compromising host immunity. This work reveals a novel strategy that rust fungi exploit effectors to modulate host defense and facilitate pathogen infection.
1820 related Products with: Stripe Rust Effector PstGSRE1 Disrupts Nuclear Localization of ROS-Promoting Transcription Factor TaLOL2 to Defeat ROS-Induced Defense in Wheat.TGF beta induced factor 2 Procarta Transcription Fa Bovine prolactin-induced Anti Apoptosis Inducing F Human Epstein-Barr Virus Nycodenz, non ionic, non Insulin promoter factor 1 Transcription factors: N Apoptosis Inducing Factor Anti AGO2 Human, Monoclon Goat Anti-Human Factor XI Rat monoclonal anti mouse
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TCF-1-Centered Transcriptional Network Drives an Effector versus Exhausted CD8 T Cell-Fate Decision.TCF-1 is a key transcription factor in progenitor exhausted CD8 T cells (Tex). Moreover, this Tex cell subset mediates responses to PD-1 checkpoint pathway blockade. However, the role of the transcription factor TCF-1 in early fate decisions and initial generation of Tex cells is unclear. Single-cell RNA sequencing (scRNA-seq) and lineage tracing identified a TCF-1Ly108PD-1 CD8 T cell population that seeds development of mature Tex cells early during chronic infection. TCF-1 mediated the bifurcation between divergent fates, repressing development of terminal KLRG1 effectors while fostering KLRG1 Tex precursor cells, and PD-1 stabilized this TCF-1 Tex precursor cell pool. TCF-1 mediated a T-bet-to-Eomes transcription factor transition in Tex precursors by promoting Eomes expression and drove c-Myb expression that controlled Bcl-2 and survival. These data define a role for TCF-1 in early-fate-bifurcation-driving Tex precursor cells and also identify PD-1 as a protector of this early TCF-1 subset.
1381 related Products with: TCF-1-Centered Transcriptional Network Drives an Effector versus Exhausted CD8 T Cell-Fate Decision.Mouse Anti-Human Mast Cel Non small cell lung carci BAFF (B cell activating f Cultrex In Vitro Angiogen Anti-BTG1(B-cell transloc D (+) Glucose anhydrous c Mouse AntiT cell receptor Kidney clear cell carcino Mouse Anti-Human Mast Cel Esophageal squamous cell Small cell lung carcinoma Diffuse large-B cell lymp
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Expression of authentic post-translationally modified proteins in organisms with expanded genetic codes.Cellular signaling and regulatory cascades often rely on post-translational modification of proteins, particularly phosphorylation, to quickly and effectively relay signals from a variety of inputs. Numerous kinases, the effectors of phosphorylation, and kinase networks have been implicated in human diseases. Until recently, an inability to produce high yields of physiologically phosphorylated proteins has proven to be a substantial barrier toward our understanding of many enzymatic processes. Orthogonal translation systems provide the means to overcome many of these limitations by enabling site-specific incorporation of phosphorylated amino acids into recombinantly expressed proteins. Site-by-site, combinatorial assessment of phosphorylation site function is unique to orthogonal translation system based approaches and offers unmatched precision in the study of PTM-enzymology, extending well beyond the scope of kinase biology.
1352 related Products with: Expression of authentic post-translationally modified proteins in organisms with expanded genetic codes.Native Influenza HA (A Pa Recombinant Influenza HA Native Influenza HA (B Vi Native Influenza HA (A Be Native Influenza HA (B Fl Recombinant Influenza HA Recombinant Influenza HA Influenza A (H5N1) HA Pep Proteins and Antibodies H Native Influenza HA (A Wi Recombinant Influenza HA Recombinant Influenza HA
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Methods for the expression, purification, and crystallization of histone deacetylase 6-inhibitor complexes.Histone deacetylase (HDAC) isozymes modulate numerous regulatory signals and pathways in biological systems, hence serving as targets for drug design. For example, HDAC6 is the cytosolic tubulin deacetylase and its inhibition compromises microtubule dynamics, leading to cancer cell cycle arrest and apoptosis. The design of inhibitors that selectively target HDAC6 is desirable to avoid side effects resulting from the inhibition of off-target HDACs. High resolution X-ray crystal structures of HDAC6 have accelerated structure-based approaches to drug design targeting HDAC6. Crystal structure analysis reveals that the tubulin deacetylase domain of human HDAC6 (catalytic domain 2, also known as CD2) is very similar to that of HDAC6 CD2 from Danio rerio (zebrafish, designated zCD2). Thus, zCD2 is a valid surrogate of human HDAC6 CD2, the actual drug target; moreover, zCD2 is much more easily prepared and crystallized. A plasmid containing the zCD2 construct for heterologous expression in Escherichia coli is available through Addgene (#122031). In this chapter, we review the preparation, purification, and crystallization of zCD2-inhibitor complexes. These methods enable the rapid acquisition of structural data regarding optimal zinc-binding groups, capping groups, and linkers in the discovery of new and selective HDAC6 inhibitors.
1234 related Products with: Methods for the expression, purification, and crystallization of histone deacetylase 6-inhibitor complexes.SAHA (Vorinostat) Mechani Tubastatin A Mechanisms: SB-939 Mechanisms: Histon MS-275 (Entinostat) Mecha JNJ-26481585 Mechanisms: LBH-589 (Panobinostat) Me Histone H2A Polyclonal An Theobromine CAS Number [8 AZD-2014 Mechanisms: mTOR Recombinant Human PKC the Gene Expression: Mouse N 5α-Androstan-3β-ol �
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Crosstalk between cellular metabolism and histone acetylation.Dynamic interplay between cellular metabolism and histone acetylation is a key mechanism underlying metabolic control of epigenetics. In particular, the central metabolite acetyl-coenzyme A (acetyl-CoA) acts as the acetyl-donor for histone acetylation in both an enzymatic and non-enzymatic manner. Since members of the family of histone acetyl transferases (HATs) that catalyze the acetylation of histone tails possess a Michaelis constant (Km) within the range of physiological cellular acetyl-CoA concentrations, changing concentrations of acetyl-CoA can restrict or promote enzymatic histone acetylation. Likewise, non-enzymatic histone acetylation occurs at physiological concentrations. These concepts implicate acetyl-CoA as a rheostat for nutrient availability acting, in part, by controlling histone acetylation. Histone acetylation is an important epigenetic modification that controls gene expression and acetyl-CoA dependent changes in both histone acetylation and gene expression have been shown in yeast and mammalian systems. However, quantifying the metabolic conditions required to achieve specific changes in histone acetylation is a major challenge. The relationship between acetyl-CoA and histone acetylation may be influenced by a variety of factors including sub-cellular location of metabolites and enzymes, relative quantities of metabolites, and substrate availability/preference. A diversity of substrates can contribute the two-carbon acyl-chain to acetyl-CoA, a number of pathways can create or degrade acetyl-CoA, and only a handful of potential mechanisms for the crosstalk between metabolism and histone acetylation have been explored. The centrality of acetyl-CoA in intermediary metabolism means that acetyl-CoA levels may change, or be resistant to change, in unexpected ways. Thus, quantification of relevant metabolites is critical evidence in understanding how the nutrient rheostat is set in normal and pathological contexts. Coupling metabolite quantitation with isotope tracing to examine fate of specific metabolites is critical to the crosstalk between metabolism and histone acetylation, including but not limited to acetyl-CoA provides necessary context. This chapter provides guidance on experimental design of quantification with isotope dilution and/or tracing of acetyl-CoA within a targeted or highly multiplexed multi-analyte workflow.
EpiQuik Total Histone H Anti monomethyl Histone H EpiQuik Global Histone EpiQuik Total Histone H EpiQuik Global Histone H3 EpiQuik Global Histone EpiQuik Global Histone EpiQuik Total Histone H EpiQuik Global Histone H3 EpiQuik Global Histone EpiQuik Total Histone H EpiQuik Global Acetyl H
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Genomic analysis of the four ecologically distinct cactus host populations of Drosophila mojavensis.Relationships between an organism and its environment can be fundamental in the understanding how populations change over time and species arise. Local ecological conditions can shape variation at multiple levels, among these are the evolutionary history and trajectories of coding genes. This study examines the rate of molecular evolution at protein-coding genes throughout the genome in response to host adaptation in the cactophilic Drosophila mojavensis. These insects are intimately associated with cactus necroses, developing as larvae and feeding as adults in these necrotic tissues. Drosophila mojavensis is composed of four isolated populations across the deserts of western North America and each population has adapted to utilize different cacti that are chemically, nutritionally, and structurally distinct.
2803 related Products with: Genomic analysis of the four ecologically distinct cactus host populations of Drosophila mojavensis.Mouse (monoclonal) AntiFM Mouse AntiFMR1 (Drosophil Ofloxacin CAS Number [824 E. coli O157 antibody, Mo MARCKS (phospho Ser170) A anti-PKC ε, Rabbit polyc HBsAg antibody, Monoclona p95 NBS1 (Ab 343) Antibod Rat AntiNidogen EnactinG2 Polyclonal Antibody PDE10 Mouse anti Human IgE anti Histone H3.1 (Ab 10) Anti
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Dual roles of glutathione S-transferase mu 1 in the development and metastasis of hepatocellular carcinoma.Reactive oxygen species (ROS) are implicated in carcinogenesis, and cellular antioxidant systems are important for detoxifying ROS and reversing oxidant-mediated modifications. Glutathione S-transferase mu (GSTM) belongs to a family of phase II detoxification enzymes that catalyze the conjugation of reduced glutathione (GSH) to a wide range of endogenous and exogenous electrophilic compounds. The genotype of GSTM1 was associated with the risk and prognosis of cancer in several meta-analyses. This study explored the function of GSTM1 in hepatocellular carcinoma (HCC).
1640 related Products with: Dual roles of glutathione S-transferase mu 1 in the development and metastasis of hepatocellular carcinoma.Multi organ carcinoma tis Colorectal carcinoma and Liver hepatocellular carc glutathione transferase a High density (188 cases 2 Breast fibroadenoma tissu Hepatocellular carcinoma Hepatocellular carcinoma Normal liver and hepatoce Multiple lung carcinoma ( glutathione S-transferase Multiple ovarian carcinom
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Ibuprofen-mediated potential inhibition of biofilm development and quorum sensing in Pseudomonas aeruginosa.Pseudomonas aeruginosa is one of the leading causes of opportunistic and hospital-acquired infections worldwide, which is frequently linked with clinical treatment difficulties. Ibuprofen, a widely used non-steroidal anti-inflammatory drug, has been previously reported to exert antimicrobial activity with the specific mechanism. We hypothesized that inhibition of P. aeruginosa with ibuprofen is involved in the quorum sensing (QS) systems.
1351 related Products with: Ibuprofen-mediated potential inhibition of biofilm development and quorum sensing in Pseudomonas aeruginosa.Mouse Anti P.aeruginosa s Mouse Anti P. aeruginosa Mouse Anti P.aeruginosa s BACTERIOLOGY PSEUDOMONAS EpiQuik Histone Methyltra EpiQuik Superoxide Dism Mouse Anti-Lipoprotein Li EpiQuik Histone Methyltra DNA (cytosine 5) methyltr EpiQuik MBD2 Binding Ac EpiQuik Histone Methyltra EpiQuik Superoxide Dism
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