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#DATG-200 QuantiChrom™ ATPase_GTPase Assay Kit
Product name : QuantiChrom™ ATPase_GTPase Assay Kit
Catalog number : DATG-200
Quantity: 200 Tests
Supplier name : Bioassays
Data sheet: Ask more or other datasheet now !
About this Product :QuantiChrom™ ATPase_GTPase Assay Kit antibody storage GENTAUR recommends for long therm storage to freeze at -24 C. For short time storage up to 30 days we suggest fridge storage at 1 to 10 C. Prevent multiple freeze taw cycles of QuantiChrom™ ATPase_GTPase Assay Kit.
More Details about
For quantitative determination of ATPase or GTPase activity and high-throughput screen for their inhibitors.
Samples: ATPase and GTPase.
Procedure: 30 min.
Size: 200 tests.
Detection limit: 0.007 U/L.
ATPases and GTPases catalyze the decomposition of ATP or GTP into
ADP or GDP and free phosphate ion. These enzymes play key roles in
transport, signal transduction, protein biosynthesis and cell differentiation.
BioAssay Systems’ QuantiChromTM ATPase/GTPase Assay Kit offers a
highly sensitive method for determining ATPase/GTPase activities in a
microplate format. Its proprietary formulation features a single reagent for
accurate determination of enzyme activity in 30 min at room temperature.
The improved malachite green reagent forms a stable dark green color with
liberated phosphate, which is measured on a plate reader (600 - 660 nm).
High sensitivity: detection of 0.007 U/L ATPase or GTPase activity.
Fast and convenient: single reagent, homogeneous “mix-and-measure”
assay allows quantitation of enzyme activity within 30 minutes.
Robust and amenable to HTS: detection at 620nm greatly reduces
potential interference by colored compounds. Z’ factors of >0.7 are
observed in 96-well and 384-well plates. Can be readily automated on HTS
liquid handling systems.
Determination of ATPase and GTPase activity.
Drug Discovery: high-throughput screen for ATPase or GTPase inhibitors.
KIT CONTENTS: 200 ASSAYS IN 96-WELL PLATE
Reagent: 50 mL Assay Buffer: 10 mL
Standard: 1mL 1 mM phosphate
Storage conditions. The kit is shipped at room temperature. The reagents
and standard are stable for one year when stored at 4°C.
Precautions: reagent contains 0.27 M H2SO4. Normal precautions for
laboratory reagents should be exercised while using the reagents.
Sample Type: ATPase
Species: bacterium, human
References: Suematsu, T et al (2010). A bacterial elongation factor G homologue exclusively functions in ribosome recycling in the spirochaete Borrelia burgdorferi. Mol Microbiol. 75(6):1445-54
Pubmed ID: 20132446
Pubmed link: http://www.ncbi.nlm.nih.gov/pubmed?term=20132446
Abstract: Translation elongation factor G (EF-G) in bacteria plays two distinct roles in different phases of the translation system. EF-G catalyses the translocation of tRNAs on the ribosome in the elongation step, as well as the dissociation of the post-termination state ribosome into two subunits in the recycling step. In contrast to this conventional view, it has very recently been demonstrated that the dual functions of bacterial EF-G are distributed over two different EF-G paralogues in human mitochondria. In the present study, we show that the same division of roles of EF-G is also found in bacteria. Two EF-G paralogues are found in the spirochaete Borrelia burgdorferi, EF-G1 and EF-G2. We demonstrate that EF-G1 is a translocase, while EF-G2 is an exclusive recycling factor. We further demonstrate that B. burgdorferi EF-G2 does not require GTP hydrolysis for ribosome disassembly, provided that translation initiation factor 3 (IF-3) is present in the reaction. These results indicate that two B. burgdorferi EF-G paralogues are close relatives to mitochondrial EF-G paralogues rather than the conventional bacterial EF-G, in both their phylogenetic and biochemical features.
PMID:20132446[PubMed - indexed for MEDLINE]
Sample Type: GTPase
References: Hussey, GS et al (2011). Identification of an mRNP complex regulating tumorigenesis at the translational elongation step. Mol Cell. 41(4):419-31
Pubmed ID: 21329880
Pubmed link: http://www.ncbi.nlm.nih.gov/pubmed?term=21329880
Abstract: ranscript-selective translational regulation of epithelial-mesenchymal transition (EMT) by transforming growth factor-β (TGF-β) is directed by the hnRNP E1-containing TGF-β-activated-translational (BAT) mRNP complex. Herein, eukaryotic elongation factor-1 A1 (eEF1A1) is identified as an integral component of the BAT complex. Translational silencing of Dab2 and ILEI, two EMT transcripts, is mediated by the binding of hnRNP E1 and eEF1A1 to their 3'UTR BAT element, whereby hnRNP E1 stalls translational elongation by inhibiting the release of eEF1A1 from the ribosomal A site. TGF-β-mediated hnRNP E1 phosphorylation, through Akt2, disrupts the BAT complex, thereby restoring translation of target EMT transcripts. Attenuation of hnRNP E1 expression in two noninvasive breast epithelial cells (NMuMG and MCF-7) not only induced EMT but also enabled cells to form metastatic lesions in vivo. Thus, translational regulation by TGF-β at the elongation stage represents a critical checkpoint coordinating the expression of EMT transcripts required during development and in tumorigenesis and metastatic progression.
Copyright © 2011 Elsevier Inc. All rights reserved. Comment in Dev Cell. 2011 Mar 15;20(3):289-90. [PubMed - indexed for MEDLINE] PMCID: PMC3061437[Available on 2012/2/18]
Sample Type: purified protein
References: Binder, M et al (2011). Molecular Mechanism of Signal Perception and Integration by the Innate Immune Sensor Retinoic Acid-inducible Gene-I (RIG-I). J Biol Chem. 286(31):27278-87
Pubmed ID: 21659521
Pubmed link: http://www.ncbi.nlm.nih.gov/pubmed?term=21659521
Abstract: RIG-I is a major innate immune sensor for viral infection, triggering an interferon (IFN)-mediated antiviral response upon cytosolic detection of viral RNA. Double-strandedness and 5'-terminal triphosphates were identified as motifs required to elicit optimal immunological signaling. However, very little is known about the response dynamics of the RIG-I pathway, which is crucial for the ability of the cell to react to diverse classes of viral RNA while maintaining self-tolerance. In the present study, we addressed the molecular mechanism of RIG-I signal detection and its translation into pathway activation. By employing highly quantitative methods, we could establish the length of the double-stranded RNA (dsRNA) to be the most critical determinant of response strength. Size exclusion chromatography and direct visualization in scanning force microscopy suggested that this was due to cooperative oligomerization of RIG-I along dsRNA. The initiation efficiency of this oligomerization process critically depended on the presence of high affinity motifs, like a 5'-triphosphate. It is noteworthy that for dsRNA longer than 200 bp, internal initiation could effectively compensate for a lack of terminal triphosphates. In summary, our data demonstrate a very flexible response behavior of the RIG-I pathway, in which sensing and integration of at least two distinct signals, initiation efficiency and double strand length, allow the host cell to mount an antiviral response that is tightly adjusted to the type of the detected signal, such as viral genomes, replication intermediates, or small by-products.
[PubMed - in process] PMCID: PMC3149321[Available on 2012/8/5]
Sample Type: Hsp90 inhibition
References: Sheikha, GA et al (2010). Some sulfonamide drugs inhibit ATPase activity of heat shock protein 90: investigation by docking simulation and experimental validation. J Enzyme Inhib Med Chem. 2010 Dec 29. [Epub ahead of print]
Pubmed ID: 21190426
Pubmed link: http://www.ncbi.nlm.nih.gov/pubmed?term=21190426
Abstract: Eight selected sulfonamide drugs were investigated as inhibitors of heat shock protein 90 (Hsp90). The investigation included simulated docking experiments to fit the selected compounds within the binding pocket of Hsp90. The selected molecules were found to readily fit within the ATP-binding pocket of Hsp90 in low-energy poses. The sulfonamides torsemide, sulfathiazole, and sulfadiazine were found to inhibit the ATPase activity of Hsp90 with IC(50) values of 1.0, 2.6, and 1.5 μM, respectively. Our results suggest that these well-established sulfonamides can be good leads for subsequent optimization into potent Hsp90 inhibitors.
PMID:21190426 [PubMed - in process]
Sample Type: Na(+)K(+)ATPase
Species: human, monkey
References: Bertol, JW et al (2011). Antiherpes activity of glucoevatromonoside, a cardenolide isolated from a Brazilian cultivar of Digitalis lanata. Antiviral Res. 2011 Jul 7. [Epub ahead of
Pubmed ID: 21763352
Pubmed link: http://www.ncbi.nlm.nih.gov/pubmed?term=21763352
Abstract: Cardiac glycosides, known ligands of the sodium pump, are widely used in the treatment of heart failure, such as digoxin and digitoxin. Besides this important activity, other biological activities, such as the antiviral activity, have been described for this group. HSV are responsible for many infections of oral, ocular and genital regions. Treatment with nucleoside analogs such as acyclovir is effective in most cases; however drug-resistance may arise due to prolonged treatment mainly in immunocompromised individuals. In this study, an antiherpes screening was performed with 65 cardenolide derivatives obtained from different sources, and one natural cardenolide, glucoevatromonoside, inhibited HSV-1 and HSV-2 replication at very low concentrations. This cardenolide showed viral inhibitory effects if added up to 12h p.i. and these effects appear to take place by the inhibition of viral proteins synthesis (ICP27, U(L)42, gB, gD), the blockage of virus release and the reduction of viral cell-to-cell spread. This compound also showed synergistic antiviral effects with acyclovir and anti-Na(+)K(+)ATPase activity, suggesting that cellular electrochemical gradient alterations might be involved in the mechanism of viral inhibition. These results suggest that cardenolides might be promising for future antiviral drug design.Copyright © 2011 Elsevier B.V. All rights reserved.
PMID:21763352[PubMed - in process]
Sample Type: ATPase extract
References: Hu, WW et al (2009). Digoxigenin modification of adenovirus to spatially control gene delivery from chitosan surfaces. J Control Release. 135(3):250-8
Pubmed ID: 19331850
Pubmed link: http://www.ncbi.nlm.nih.gov/pubmed?term=19331850
Abstract: To spatially control the delivery of multiple viral vectors from biomaterial scaffolds, digoxigenin (DIG) was conjugated to adenoviral capsid proteins as an antigenic determinant for antibody immobilization. The infectivity, toxicity, specificity and immobilization stability of DIG-modified adenovirus were examined to investigate the feasibility and effectiveness of this viral surface modification. Anti-DIG antibody conjugated on chitosan surfaces was able to immobilize DIG-modified adenovirus and could be stably bound on the material for at least two weeks, yet the modification was mild enough that viral infectivity was maintained. To immobilize two different adenoviruses, wax masking was applied to conjugate anti-DIG and anti-adenovirus antibodies in two discrete regions of a chitosan film. The distribution of these two viral vectors expressing different reporter genes was examined after cell culture. Fluorescent protein expression from transduced cells illustrated that the infection distribution could be controlled: one gene was delivered to the entire region of the biomaterial, and another was only delivered to defined regions. Compared to three other cardiac glycosides, ATPase inhibition was undetectable when DIG was conjugated on the adenovirus, suggesting that the method may be safe for in vivo application. This dual viral vector delivery system should be capable of generating distinct interfaces between cell signaling viruses to control tissue regeneration from a range of different biomaterials.
[PubMed - indexed for MEDLINE] PMCID: PMC2668726
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