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Purpose – The purpose of this paper is to investigate service quality of e-commerce Websites in online platform and their contribution on e-business promotion. Design/methodology/approach – The online survey was performed on a survey portal provided by Nepal Telecom in Nepal. Findings – The findings of this study suggest that information quality and online service quality were the key determinants for user satisfaction and sustainability of e-commerce technology. Research limitations/implications – Research opportunities of web services and e-commerce area are fruitful and important for both academics and practitioners. Practical implications – The findings on online service quality of e-commerce technology will be useful for current management practice such as making business policies and strategies and sharing information to managers and organization leaders. This study can be used for e-commerce Website operators wishing to enhance the competitiveness of their Websites in the highly competitive online market. Originality/value – E-commerce is considered an excellent alternative for individuals and companies to reach new customers. Service quality delivery through Internet is an essential strategy to success, more important than price and web presence. The e-commerce Website has been identified as having a significant impact on business activities in solving the geographical problem. A number of performance problems have been observed for e-commerce Websites, and much work has gone into characterizing the performance of web-servers and Internet applications.

Human telomerase is a ribonucleoprotein complex which adds the repeats of TTAGGG on the telomeric ends of chromosomal DNA. Even though the vast majority of human cancers express telomerase activity, most human somatic cells lack the telomerase activity; consequently, telomerase has been regarded as both a biomarker for early cancer diagnosis and a therapeutic target. Here we develop a simple, rapid and highly sensitive method for the detection of telomerase activity at the single-cell level using telomeres-induced two-stage isothermal amplification-mediated chemiluminescence assay. In the presence of telomerase, the telomere repeats of (TTAGGG)n are added to the 3' end of telomerase substrate primer, which can be converted to the template of strand displacement amplification (SDA) for the generation of short oligonucleotides, catalytic DNAzymes, and the telomere repeats of (TTAGGG)n. The short oligonucleotide might function as a new trigger to bind the free telomerase substrate primer and consequently initiate an isothermally exponential amplification reaction (EXPAR), generating a large number of catalytic DNAzymes. Both the DNAzymes and the G-rich telomeric repeat units can interact with hemin to form the catalytic hemin-G-quadruplex nanostructures, which can catalyze the generation of amplified chemiluminescence signals in the presence of luminol and H2O2. While in the absence of telomerase, the two-stage isothermal amplification cannot be initiated, and no chemiluminescence signal is observed. Owing to the high amplification efficiency of two-stage isothermal amplification as well as the high sensitivity and wide dynamic range of the chemiluminescence assay, the proposed method can sensitively measure the synthetic telomerase product TPC8 with a detection limit of as low as 0.1 aM and a large dynamic range of 10 orders of magnitude from 0.1 aM to 1 nM and can even detect the telomerase activity from a single HeLa cancer cell without the need for any labeled DNA probes. The proposed method can be further used to screen the anticancer drugs and might provide a promising approach for the discovery of new anticancer drugs.

Abstract-We tested the hypothesis that transient receptor potential canonical type 3 (TRPC3) channels are increased in vascular smooth muscle cells and aortic tissue from spontaneously hypertensive rats (SHR) compared with normotensive Wistar Kyoto rats. Expression of TRPC3 was analyzed by immunohistochemistry and Western blotting. TRPC3 gene knockdown was performed by specific small interfering RNA and TRPC3 overexpression using the pAdEasy-1 system. Cytosolic calcium was measured using fluorescence spectrophotometry and vasoconstriction of aortic rings using a force transducer. In SHR, the expression of TRPC3 channel protein was significantly higher in aortic rings (

DNA glycosylase is an initiating enzyme of cellular base excision repair pathway which is responsible for the repair of various DNA lesions and the maintenance of genomic stability, and the dysregulation of DNA glycosylase activity is associated with a variety of human pathology. Accurate detection of DNA glycosylase activity is critical to both clinical diagnosis and therapeutics, but conventional methods for the DNA glycosylase assay are usually time-consuming with poor sensitivity. Here, we demonstrate the base-excision-repair-induced construction of a single quantum dot (QD)-based sensor for highly sensitive measurement of DNA glycosylase activity. We use human 8-oxoguanine-DNA glycosylase 1 (hOGG1), which is responsible for specifically repairing the damaged 8-hydroxyguanine (8-oxoG, one of the most abundant and widely studied DNA damage products), as a model DNA glycosylase. In the presence of biotin-labeled DNA substrate, the hOGG1 may catalyze the removal of 8-oxo G from 8-oxoG·C base pairs to generate an apurinic/apyrimidinic (AP) site. With the assistance of apurinic/apyrimidinic endonuclease (APE1), the cleavage of the AP site results in the generation of a single-nucleotide gap. Subsequently, DNA polymerase β incorporates a Cy5-labeled dGTP into the DNA substrate to fill the gap. With the addition of streptavidin-coated QDs, a QD-DNA-Cy5 nanostructure is formed via specific biotin-streptavidin binding, inducing the occurrence of fluorescence resonance energy transfer (FRET) from the QD to Cy5. The resulting Cy5 signal can be simply monitored by total internal reflection fluorescence (TIRF) imaging. The proposed method enables highly sensitive measurement of hOGG1 activity with a detection limit of 1.8 × 10(-6) U/μL. Moreover, it can be used to measure the enzyme kinetic parameters and detect the hOGG1 activity in crude cell extracts, offering a powerful tool for biomedical research and clinical diagnosis.

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