Search results for: Purified
#34562714 2021/09/15 To Up
Production, isolation and characterization of C-phycocyanin from a new halo-tolerant Cyanobacterium aponinum using seawater.A halo-tolerant Cyanobacterium aponinum PCC 10605 was applied for the first time to produce high-level C-phycocyanin (C-PC). Combined with chemical extraction with sodium phosphate buffer and physical treatment using high pressure homogenization, a higher titer of C-PC was achieved. The culture conditions were optimized by mixing nitrate and ammonia ions, 2% carbon dioxide, and conditional light intensity. Thus, strain PCC10605 produced the highest titer C-PC of 0.652Â g/g-DCW in the N1A2 medium with 10% light intensity and 16:8 light-period on day 7. PCC10605 accumulated 0.51Â g-CPC/g-DCW at 20Â g/L NaCl, while it grew normally in seawater with 30Â g/L salinity, thus confirmed that PCC10605 was halo-tolerant strain. Besides, PCC10605 survived in 0.12Â g/L phosphate medium that has never been reported. Finally, the purified C-PC exhibited DPPH, superoxide scavenging activity and antibacterial activity, which displayed 87.6%, and 18.7% removal of free radical, and 1.98Â cm of inhibition zone for Escherichia coli.
Jia-Yi Lin, I-Son Ng
1204 related Products with: Production, isolation and characterization of C-phycocyanin from a new halo-tolerant Cyanobacterium aponinum using seawater.25 mg1000 tests100ul50 assays1 kit200ul10 mg2.5 mg100 mg10 mg200ug10 reactions
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#34562539 2021/09/22 To Up
A simple method for obtaining human albumin and its use for in vitro interaction assays with indole-thiazole and indole-thiazolidinone derivatives.This work aimed to develop a simple and low-cost method to obtain Human serum albumin (HSA) and its consequent application for in vitro drug interaction assays. The HSA was purified by classic principles of plasma precipitation and thermocoagulation, using a multiple-stage fractionation. The quality of the final product was assessed by electrophoresis, protein dosage by the Lowry method and the pharmacopeial thermal stability. At the end, an isotonic solution of HSA with a total protein concentration of 2.7â¯mgÂ·mL was obtained, which was visualized as a single band corresponding to the molecular weight of 66â¯kDa. After the thermal stability test, there was no indication of turbidity or color change of the solution. Finally, the HSA was useful for interactions assays with indole-thiazole and indole-thiazolidinone derivatives through UV-vis absorption and fluorescence spectroscopic studies, as well as by docking molecular analysis. Derivatives quenched the intrinsic fluorescence of HSA, disrupted the tryptophan residues microenvironment, and probably bind at Sudlow's site I. Therefore, the simplified methodology developed in this work proved to be effective in obtaining HSA that can be applied to research goals including drug interaction assays.
Josival Emanuel Ferreira Alves, Maria Luiza Cavalcanti Lucena, AntÃ´nio Edson de Souza Lucena, Aurenice Arruda Dutra das Merces, Rafael David Souto de Azevedo, Gleyton Leonel Silva Sousa, Ricardo Olimpio de Moura, Maria do Carmo Alves de Lima, Luiz Bezerra de Carvalho JÃºnior, Sinara MÃ´nica Vitalino de Almeida
1105 related Products with: A simple method for obtaining human albumin and its use for in vitro interaction assays with indole-thiazole and indole-thiazolidinone derivatives.100 G 5 G 1 G50 assays 1 G500 MG 5 G96 Tests25 mg 100 G10 mg500 MG
#34562467 2021/09/22 To Up
RNA electroelution: Comparing two electroeluter models.RNA represents a vibrant area of research and many studies use techniques that require large amounts of purified RNA. One common purification method involves slicing a section of a polyacrylamide gel containing the RNA of interest and eluting the RNA out of the gel using electroelution. Various electroeluter models are available but sometimes a given model becomes discontinued, compelling researchers to choose a different model. Here, we have compared two electroeluters with different chamber designs for their ability to recover RNA from gel pieces. Our results show that both electroeluters are effective and recover comparable amounts of purified RNA.
Amber N Rogers, Maya K Mastronardo, Tsion G Mekonnen, Ana Maria Soto1000 units 1 kit(s) 10 nmol1 Bottle/Unit500ng200ul1000 units10 nmol25ul200ul1000 units
#34562449 2021/09/22 To Up
The predicted stem-loop structure in the 3'-end of the human norovirus antigenomic sequence is required for its genomic RNA synthesis by its RdRp.The norovirus genome consists of a single positive-stranded RNA. The mechanism by which this single-stranded RNA genome is replicated is not well understood. To reveal the mechanism underlying the initiation of the norovirus genomic RNA synthesis by its RNA-dependent RNA polymerase (RdRp), we used an in vitro assay to detect the complementary RNA synthesis activity. Results showed that the purified recombinant RdRp was able to synthesize the complementary positive-sense RNA from a 100-nt template corresponding to the 3'-end of the viral antisense genome sequence, but that the RdRp could not synthesize the antisense genomic RNA from the template corresponding to the 5'-end of the positive-sense genome sequence. We also predicted that the 31 nt region at the 3'-end of the RNA antisense template forms a stem-loop structure. Deletion of this sequence resulted in the loss of complementary RNA synthesis by the RdRp, and connection of the 31 nt to the 3'-end of the inactive positive-sense RNA template resulted in the gain of complementary RNA synthesis by the RdRp. Similarly, an electrophoretic mobility shift assay further revealed that the RdRp bound to the antisense RNA specifically, but was dependent on the 31 nt at the 3'-end. Therefore, based on this observation and further deletion and mutation analyses, we concluded that the predicted stem-loop structure in the 31 nt end and the region close to the antisense viral genomic stem sequences are both important for initiating the positive-sense human norovirus genomic RNA synthesis by its RdRp.
Takashi Shimoike, Tsuyoshi Hayashi, Tomoichiro Oka, Masamichi Muramatsu
1744 related Products with: The predicted stem-loop structure in the 3'-end of the human norovirus antigenomic sequence is required for its genomic RNA synthesis by its RdRp.11mg102 100ul
#34562255 // To Up
Measuring Smoothened (SMO)-Mediated Activation of the G Protein.The oncoprotein Smoothened (SMO) can transduce the Hedgehog signal from the tumor suppressor Patched-1 (PTCH1) to glioma-associated-oncogene (Gli) transcription factors. Previous studies have shown that SMO is a G-protein-coupled receptor (GPCR) of the Frizzled-class (class-F) that can activate G family of heterotrimeric G proteins. Here, we describe [S]-GTPÎ³S assay using SMO cell membranes and purified G protein to measure the level of G protein activation following the activation of SMO by agonists.
Heng Liu, Cheng Zhang100 μg1 Set50ug250ul10reactions 100ug Lyophilized1 Set150ug100ug Lyophilized50ug1 Set
#34562250 // To Up
Biochemical Assays to Directly Assess Smoothened Activation by a Conformationally Sensitive Nanobody.The Hedgehog signaling pathway coordinates early development and is important in various cancers. Classic approaches to test pathway activation rely on transcriptional readouts or ciliary accumulation of specific pathway components. Although these assays have laid the foundation for studying Hedgehog pathway activation, they integrate the complex molecular actions of the transporter Patched and the seven transmembrane protein Smoothened. Though it is clear that cellular sterols are critical for pathway activity, direct dissection of which sterols drive Smoothened activity is precluded by the complex biosynthetic pathways responsible for cellular sterols. Here we describe a direct method of measuring Smoothened activity in vitro. This assay measures the binding of Smoothened to NbSmo8, a single-domain antibody that is selective for the active-state of Smoothened. Binding of purified Smoothened, reconstituted with specific sterols, to fluorescently labeled NbSmo8 can be rapidly evaluated using a fluorescence-detection size-exclusion chromatography assay. This approach enables a reductionist approach to precisely interrogate the regulatory activities of cellular lipids and sterols during Hedgehog signaling.
Ishan Deshpande, Aashish Manglik
1999 related Products with: Biochemical Assays to Directly Assess Smoothened Activation by a Conformationally Sensitive Nanobody.100 assays100 assays100 assays100 assays100 assays200 assays400 assays1 mg
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#34561750 2021/09/25 To Up
Production of a monoclonal antibody against a galactose-binding protein of Acanthamoeba castellanii and its cytotoxicity.In this study, it was confirmed whether the galactose-binding protein (GBP) was present in Acanthamoeba castellanii, and its function on a target cell was confirmed by production of an antibody against the GBP. Since the genes for GBP have not yet been identified at all, the purification of GBP was done using galactose-beads from amoebial lysates, and monoclonal antibodies were produced using cell fusion. GBP was confirmed to have a size of about 35Â kDa. After the third immunization with purified GBP in BALB/c mice, monoclonal antibody production was analyzed. The clone cultured before limiting dilution was named 2AB2 and showed the highest antibody titer in the culture supernatant of a 24-well plate. AF6 clone cultured after limiting dilution showed an antibody titer of 0.259 in a 75-T flask. Antibodies generated by collecting ascites by injecting monoclonal colonies into the abdominal cavity of mice were confirmed through gel analysis and were observed to belong to the isotype of the IgM having kappa chains. Since the cytotoxicity of A. castellanii was inhibited by about 26% by the monoclonal antibody against GBP, it was confirmed that the antibody against GBP had an inhibitory effect on cytotoxicity. This study was the first report on GBP isolated and purified from A. castellanii, and similarly to a mannose-binding protein (MBP), its involvement in contact-dependent cytotoxicity was demonstrated with monoclonal antibody production.
Dong-Youn Kim, Dae-Hyun Son, Abdul Matin, Suk-Yul Jung
1903 related Products with: Production of a monoclonal antibody against a galactose-binding protein of Acanthamoeba castellanii and its cytotoxicity.100ul100 ul100.00 ug 100ul100ug Lyophilized100100ug 100ul 100ul100ug 50 UG100ul
#34560963 2021/08/12 To Up
Structural diversity of fucoidans and their radioprotective effect.Fucoidans are biologically active sulfated polysaccharides of brown algae. They have a great structural diversity and a wide spectrum of biological activity. This review is intended to outline what is currently known about the structures of fucoidans and their radioprotective effect. We classified fucoidans according to their composition and structure, examined the structure of fucoidans of individual representatives of algae, summarized the available data on changes in the yields and compositions of fucoidans during algae development, and focused on information about underexplored radioprotective effect of these polysaccharides. Based on the presented in the review data, it is possible to select algae, which are the sources of fucoidans of desired structures and to determine the best time to harvest them. The use of high purified polysaccharides with established structures increase the value of studies of their biological effects and the determination of the dependence "structure - biological effect".
Tatiana N Zvyagintseva, Roza V Usoltseva, Natalia M Shevchenko, Valerii V Surits, Tatiana I Imbs, Olesya S Malyarenko, Natalia N Besednova, Lyudmila A Ivanushko, Svetlana P Ermakova10 mg100ug500 mg25 mg2.5 mg50 ug 5 G100ul25 mg 5 G96 wells (1 kit)1000 TESTS/0.65ml
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