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Site-Selective Protein Chemical Modification of Exposed Tyrosine Residues Using Tyrosine Click Reaction.

Targeting less abundant amino acid residues on the protein surface may realize site-selective protein modification of natural proteins. The relative hydrophobicity of tyrosine combined with the π-π stacking tendency of the aromatic rings results in generally low accessibility. In this study, site-selective protein modification was achieved by targeting surface-exposed tyrosine residues without using a genetic encoding system. Tyrosine residues were modified with N-methylated luminol derivative under single-electron transfer (SET) reaction conditions. Horseradish peroxidase (HRP)-catalyzed SET and electrochemically activated SET modified surface-exposed tyrosine residues selectively. N-methylated luminol derivative modified tyrosine residues more efficiently than 4-arylurazole under tyrosine click conditions using HRP and electrochemistry. Tyrosine residues that are evolutionarily exposed only in the comple-mentarity-determining region (CDR) of an antibody were selectively modified by tyrosine click reactions. CDR-modified antibodies were applied to in vivo imaging and antibody-drug conjugate (ADC).

2955 related Products with: Site-Selective Protein Chemical Modification of Exposed Tyrosine Residues Using Tyrosine Click Reaction.

Human dopachrome tautomer anti-Protein Tyrosine pho Phospho-Tyrosine Hydroxyl Rabbit Anti-Rat Tyrosine Anti-BACE-1 (Memapsin-2, N-Acetyl-3-iodo-L-tyrosin Rabbit Anti-Tyrosine Hydr ReadiLink™ mFluor™ Vi N-Benzoyl-N-methyl-L-tyro Tyrosine Hydroxylase (Pho Rabbit Anti-Tyrosine Hydr Goat Anti-Human Tyrosine

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A challenge in biosensors: Is it better to measure a photon or an electron for ultrasensitive detection?

Biosensor development exploiting various transduction principles is characterized by a strong competition to reach high detectability, portability and robustness. Nevertheless, a literature-based comparison is not possible, as different conditions are employed in each paper. Herein, we aim at evaluating which measurement, photons or electrons, yields better biosensor performance. Upon outlining an update in recent achievements to boost analytical performance, amperometry and chemiluminescence (CL)-based biosensors are directly compared employing the same biospecific reagents and analytical formats. Horseradish peroxidase (HRP) and hydrogen peroxide concentrations were directly measured, while glucose and mouse IgG were detected employing an enzyme paper-based biosensor and an immunosensor, respectively. Detectability was down to picomoles of hydrogen peroxide (4 pmol for CL and 210 pmol for amperometry) and zeptomoles of HRP (45 zmol for CL and 20 zmol for amperometry); IgG was detected down to 12 fM (CL) and 120 fM (amperometry), while glucose down to 17 μM (CL) and 40 μM (amperometry). Results showed that amperometric and CL biosensors offered similar detectability and analytical performance, with some peculiarities that suggest complementary application fields. As they generally provided slightly higher detectability and wider dynamic ranges, CL-based biosensors appear more suitable for point-of-care testing of clinical biomarkers, where detectability is crucial. Nevertheless, as high detectability in CL biosensors usually requires longer acquisition times, their rapidity will allocate electrochemical biosensors in real-time monitoring and wearable biosensors. The analytical challenge demonstrated that these biosensors have competitive and similar performance, and between photons and electrons the competition is still open.

1522 related Products with: A challenge in biosensors: Is it better to measure a photon or an electron for ultrasensitive detection?

FDA Standard Frozen Tissu FDA Standard Frozen Tissu Oral squamous cell cancer FDA Standard Frozen Tissu FDA Standard Frozen Tissu Rabbit Anti-ITIH4 Polyclo Rabbit Anti-NOS-2 iNOS Po Rabbit Anti-TNIP2 ABIN2 T Rabbit Anti-G protein alp anti-Diazepam Binding Inh Rabbit Anti-Insulin Recep Anti AGO2 Human, Monoclon

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Assessing bladder hyper-permeability biomarkers using molecularly-targeted MRI.

The objective was to investigate if some of the key molecular players associated with bladder hyper-permeability in interstitial cystitis/bladder pain syndrome (IC/BPS) could be visualized with molecularly-targeted magnetic resonance imaging (mt-MRI) . IC/BPS is a chronic, painful condition of the bladder that affects primarily women. It has been demonstrated over the past several decades that permeability plays a substantial role in IC/BPS. There are several key molecular markers that have been associated with permeability, including glycolsaminoglycan (GAG), biglycan, chondroitin sulfate, decorin, E-cadherin, keratin 20, uroplakin, vascular endothelial growth factor receptor 1 (VEGF-R1), claudin-2 and zonula occludens-1 (ZO-1). We used molecularly-targeted MRI (mt-MRI) to assess specific urothelial biomarkers (decorin, VEGF-R1, and claudin-2) associated with bladder hyper-permeability in a protamine sulfate (PS)-induced rat model. The mt-MRI probes consisted of an antibody against either VEGF-R1, decorin or claudin-2 conjugated to albumin that had also Gd-DTPA (gadolinium diethylene triamine penta acetic acid) and biotin attached. mt-MRI- and histologically-detectable levels of decorin and VEGF-R1 were both found to decrease following PS-induced bladder urothelial hyper-permeability, whereas claudin-2, was found to increase in the rat PS model. Verification of the presence of the mt-MRI probes were done by targeting the biotin moiety for each respective probe with streptavidin-hose radish peroxidase (HRP). Levels of protein expression for VEGF-R1, decorin and claudin-2 were confirmed with immunohistochemistry. molecularly-targeted MRI (mt-MRI) was found to successfully detect alterations in the expression of decorin, VEGFR1 and claudin-2 in a PS-induced rat bladder permeability model. This molecularly-targeted imaging approach has the potential to provide invaluable information to enhance our understanding of bladder urothelium hyper-permeability in IC/BPS patients, and perhaps be used to assist in developing novel therapeutic strategies.

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Bladder cancer tissue arr Bladder cancer tissue arr Bladder disease spectrum Bladder cancer tissue arr Human Bladder Microvascul Bladder cancer test tissu Mid advanced stage bladde Bladder cancer tissue arr Bladder cancer mid densit Bladder cancer tissue arr Bladder cancer tissue arr Bladder disease spectrum

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Real-time detection of foodborne bacterial viability using a colorimetric bienzyme system in food and drinking water.

Foodborne bacterial infection poses a serious threat to human health. As most diseases are caused by living bacteria, real-time assessment of bacterial viability is vitally important to the public health sector. Herein, we developed a simple and novel colorimetric assay based on the Glucose oxidase (GOD)/Horseradish peroxidase (HRP) bienzyme system for real-time monitoring of bacterial viability in food and drinking water. This bienzyme system is free of any chemical synthesis and only requires 3 sample handling steps. The color response is easily observable with the naked eye or recordable with a smartphone for precise determination of bacterial viability. The proposed strategy was validated with various bacteria both Gram-positive and Gram-negative, indicating its capability for broad-spectrum bacteria viability detection. Therefore, the proposed strategy shows promise for rapid and reliable quality control in food and drinking water.

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Avian Influenza virus H5N Avian Influenza virus H5N Avian Influenza virus H5N MarkerGeneTM in vivo lacZ Avian Influenza Virus H5N  EpiQuik Total Histone H Glutathione Colorimetric EnzyChrom™ NAD NADH Ass Anti-Aquaporin 4(AQP4, WC EnzyChrom™ D-Lactate As Digestive system carcinom Beta Amyloid (1 42) High

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Preparation, Characterization and Diagnostic Valuation of Two Novel Anti-HPV16 E7 Oncoprotein Monoclonal Antibodies.

At present, the clinical detection method of human papillomavirus (HPV) is mainly based on the PCR method. However, this method can only be used to detect HPV DNA and HPV types, and cannot be used to accurately predict cervical cancer. HPV16 E7 is an oncoprotein selectively expressed in cervical cancers. In this study, we prepared an HPV16 E7-histidine (HIS) fusion oncoprotein by using a prokaryotic expression and gained several mouse anti-HPV16 E7-HIS fusion oncoprotein monoclonal antibodies (mAbs) by using hybridoma technology. Two mAbs, 69E2 (IgG2a) and 79A11 (IgM), were identified. Immunocytochemistry, immunofluorescence, immunohistochemistry, and Western blot were used to characterize the specificity of these mAbs. The sequences of the nucleotide bases and predicted amino acids of the 69E2 and 79A11 antibodies showed that they were novel antibodies. Indirect enzyme-linked immunosorbent assay (ELISA) with overlapping peptides, indirect competitive ELISA, and 3D structural modeling showed that mAbs 69E2 and 79A11 specifically bound to the three exposed peptides of the HPV16 E7 (HPV16 E7, HPV16 E7, and HPV16 E7). We used these two antibodies (79A11 as a capture antibody and 69E2 as a detection antibody) to establish a double-antibody sandwich ELISA based on a horseradish peroxidase (HRP)-labeled mAb and tetramethylbenzidine (TMB) detection system for quantitative detection of the HPV16 E7-HIS fusion oncoprotein, however, it was not ideal. Then we established a chemiluminescence immunoassay based on a labeled streptavidin-biotin (LSAB)-ELISA method and luminol detection system-this was sufficient for quantitative detection of the HPV16 E7-HIS fusion oncogenic protein in ng levels and was suitable for the detection of HPV16-positive cervical carcinoma tissues. Collectively, we obtained two novel mouse anti-HPV16 E7 oncoprotein mAbs and established an LSAB-lumino-dual-antibody sandwich ELISA method for the detection of the HPV16 E7-HIS fusion oncogenic protein, which might be a promising method for the diagnosis of HPV16-type cervical cancers in the early stage.

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Rat monoclonal anti mouse Anti-monomethyl Histone H Rat monoclonal anti mouse Signal Transduction Anti Rat monoclonal anti mouse Rat monoclonal anti mouse Rat monoclonal anti mouse Rat monoclonal anti mouse MONOBODIES (Monoclonal An Rat monoclonal anti mouse Rat monoclonal anti mouse Rat monoclonal anti mouse

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Quantitative analysis of HO transport through purified membrane proteins.

Hydrogen peroxide (HO) is an important signal molecule produced in animal and plant cells. The balance of HO between the intra- and extracellular space is regulated by integral membrane proteins, which thereby modulate signaling. Several methods have been established to analyze aquaporin mediated transport of HO in whole cells with the intrinsic limitation that the amount of protein responsible for a certain activity cannot be standardized. As a consequence, the quantification of the transport and specific activity is difficult to extract making it problematic to compare isoforms and mutated variants of one specific target. Moreover, in cell-based assays, the expression of the target protein may alter the physiological processes of the host cell providing a complication and the risk of misleading results. To improve the measurements of protein based HO transport, we have developed an assay allowing quantitative measurements.•Using purified aquaporin reconstituted in proteoliposomes, transport of HO can be accurately measured.•Inside the liposomes, HO catalyzes the reaction between Amplex Red and horseradish peroxidase (HRP) giving rise to the fluorescent product resorufin.•Analysing pure protein provides direct biochemical evidence of a specific transport excluding putative cellular background.

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Recombinant Human HOMER1 MOUSE ANTI BORRELIA BURGD Octyl â D 1 thioglucopyr 1,1'-Dioctadecyl-3,3,3',3 Recombinant PKA holoenzym Proteins and Antibodies H Mouse AntiTransportin1 Ta Horse IgG Protein G Purif Polyclonal Antibody Gluco Purified Rabbit Anti Huma Recombinant PKA holoenzym Proteins and Antibodies H

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Entrapment of enzyme in the presence of proline: effective approach to enhance activity and stability of horseradish peroxidase.

In this report, activity and stability of horseradish peroxidase (HRP) entrapped in polyacrylamide gel in the presence of proline (HEP) are compared with that of enzyme entrapped in absence of proline (HE). Within polyacrylamide (8%) beads, 80% entrapment yield for peroxidase was observed in the presence as well as absence of proline. The HEP (1.5 M proline) showed 170% higher activity compared to HE. HEP also showed significant increase in , and . At 8th cycle of use, HEP retained 40% of its activity, whereas HE retained only 10% of activity. In addition, in comparison with HE, HEP showed increased storage stability and thermo-stability. HEP showed higher activity compared to HE over an extensive range of pH (4-8), temperature (30-80 °C) and inhibitors such as NaN, Cd and Pb. Our results suggest that peroxidase entrapment in polyacrylamide gel in the presence of proline can be a useful approach for increasing activity and stability of horseradish peroxidase.

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FDA Standard Frozen Tissu FDA Standard Frozen Tissu Ofloxacin CAS Number [824 Cell Meter™ Fluorimetri FDA Standard Frozen Tissu FDA Standard Frozen Tissu Cell Meter™ Fluorimetri Alkaline Phospatase (ALP) Pfu DNA Polymerase protei  EpiQuik Superoxide Dism Anti-human C1 Esterase In MarkerGeneTM in vivo lacZ

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LncRNA LEF1-AS1 silencing diminishes EZH2 expression to delay hepatocellular carcinoma development by impairing CEBPB-interaction with CDCA7.

Hepatocellular carcinoma (HCC) is recognized for its high mortality rate worldwide. Based on intensive studies, long non-coding RNA (lncRNA) expression exerts significant effects on tumor suppression. Herein, we investigated the molecular mechanism of lymphoid enhancer-binding factor-1 antisense RNA 1 (LEF1-AS1) in HCC cells. Microarray-based gene expression analysis was adopted to predict and verify the differentially expressed genes in HCC, which predicted cell division cycle-associated 7 (CDCA7) and LEF1-AS1 to be highly expressed in HCC. The expression of LEF1-AS1, CDCA7, CCAAT/enhancer-binding protein beta (CEBPB) and enhancer of zeste homolog 2 (EZH2) was determined by means of reverse transcription quantitative polymerase chain reaction (RT-qPCR) and western blot analysis. LncMap was used to predict the lncRNA-transcription factor-gene interaction in HCC. ChIP, RIP assay and dual luciferase reporter gene assay were employed to verify the relationship between the transcription factor and gene. Silencing of LEF1-AS1 could downregulate CDCA7 expression through CEBPB. Overexpression of LEF1-AS1, EZH2 and CDCA7 promoted proliferation and invasion in HCC cells. LEF1-AS1 promoted CDCA7 expression to further upregulate EZH2. Tumor formation in nude mice was assessed to verify the experimental results. Silencing of LEF1-AS1 inhibited the growth of tumors . Collectively, silencing LEF1-AS1 inhibited the proliferation and invasion of HCC cells by down-regulating EZH2 through the CEBPB-CDCA7 signaling pathway, which provides scientific evidence for the treatment of HCC.: HCC: Hepatocellular carcinoma; lncRNA: long non-coding RNA; LEF1-AS1: lymphoid enhancer-binding factor-1 antisense RNA 1; EZH2: enhancer of zeste homolog 2; CDCA7: cell division cycle-associated 7; GEO: Gene Expression Omnibus; NC: negative control; oe: overexpressed; RT-qPCR: reverse transcription quantitative polymerase chain reaction; PBS: phosphate buffered saline; HRP: horseradish peroxidase; OD: optical density; RIP: Radioimmunoprecipitation; ChIP: Chromatin immunoprecipitation; WT: wild type.

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Camel hydatidosis diagnostic kit: optimization of turnip and horseradish peroxidase conjugates using glutaraldehyde method.

Echinococcosis/hydatidosis is one of the most important parasitic zoonotic diseases in the world. Cystic echinococcosis increases public health and socio-economic concern due to considerable morbidity rates that give rise to elevated economic losses both in the public health part and in the farm animal field. The enzyme linked immunosorbent assay (ELISA) is consider the more accurate tool for diagnosis of hydatidosis in camels. In the present study, affinity purified () antigens (APA) were purified from crude hydatide germinal layer proteins for detection of antibodies in infected camels, using affinity matrix (camel IgGs coupled to CNBr-activated Sepharose). The electrophoretic profile of the APA showed that it was separated into two bands; one major band of 130 kDa and one minor band at 55 kDa. These antigens were used successfully as specific coating antigenic proteins in detection of echinococcosis in camel. In a trial to prepare an anti-camel IgGs peroxidase conjugate; peroxidase enzyme was purified from turnip roots (TPOD) using ammonium sulfate precipitation and affinity chromatography on phenyl Sepharose CL-4B. The purified TPOD showed a major band at 35 kDa. Rabbit anti-camel IgG antibodies (AC IgGs) were prepared then purified using affinity chromatography on Protein G-Sepharose. The TPOD, and commercial HRP for comparison, enzymes were conjugated to AC IgGs using 1%, 5% and 10% glutaraldehyde. The results revealed that the HRP was much better than TPOD in conjugation with AC-IgG antibodies and the 10% glutaraldehyde concentration was the most efficient concentration with ELISA titer 1:50.

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Biosensing of prostate specific antigen (PSA) in human plasma samples using biomacromolecule encapsulation into KCC-1-npr-NH: A new platform for prostate cancer detection.

Prostate-specific antigen (PSA) is a high molecular weight glycoprotein that is used as a marker for the diagnosis of prostate cancer and is therefore important in the medical field. In this study, a novel sandwich type immunoassay was designed based on encapsulation of biotinylated antibody into KCC-1-npr-NH. KCC-1-npr-NH stabilized the stability of the primary antibody. So, encapsulated Ab1 was immobilized on the surface of glassy carbon electrode. Field emission scanning electron microscope (FE-SEM) was employed to monitor the sensor fabrication. The engineered immunosensor was used for the detection of PSA using differential pulse voltammetry (DPVs) and square wave voltammetry (SWVs) techniques. The proposed interface lead to enhancement of accessible surface area for immobilizing a high amount of anti-PSA antibody, increasing electrical conductivity, boosting stability, catalytic properties and biocompatibility. The intensity of electrochemical signals is also increased by the use of AuNPs functionalized with CysA used in secondary antibody (HRP conjugated PSA) structure. Under optimal conditions, the designed immuno-assay provide a good analytical performance for quantifying the PSA marker in the linear range of 1 to 60 μg/l.

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