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Relevant bibliographies by topics / Binding assay

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Academic literature on the topic 'Binding assay'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 February 2022

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Journal articles on the topic "Binding assay"

1

Rozwandowicz-Jansen, Anita, Jonne Laurila, Eija Martikkala, et al. "Homogeneous GTP Binding Assay Employing QRET Technology." Journal of Biomolecular Screening 15, no. 3 (2010): 261–67. http://dx.doi.org/10.1177/1087057109358921.

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Functional cell signaling assays have become important tools for measuring ligand-induced receptor activation in cell-based biomolecular screening. Guanosine-5′-triphosphate (GTP) is a generic signaling marker responsible for the first intracellular signaling event of the G-protein-coupled receptors (GPCRs). [35S]GTPγS binding assay is the classical well-established method for measuring agonist-induced G-protein activation requiring a separation of free and bound fractions prior to measurement. Here a novel, separation-free, time-resolved fluorescence GTP binding assay has been developed based on a non–fluorescence resonance energy transfer (FRET) single-label approach and quenching of a nonbound europium-labeled, nonhydrolyzable GTP analog (Eu-GTP). The quenching resonance energy transfer (QRET) method relies on the use of Eu-GTP, providing a time-resolved fluorescent detection as an alternative to the radiolabel [35S]GTPγS assay. Upon activation of recombinant human α2A-adrenoceptors (α2A-AR) expressed in Chinese hamster ovary cells, guanosine-5′-diphosphate is released from the α-subunit of Gi-proteins, enabling the subsequent binding of Eu-GTP. Activation of α2A-AR with 5 different α2-AR agonists was measured quantitatively using the developed QRET GTP assay and compared to [35S]GTPγS and heterogeneous Eu-GTP filtration assays. Equal potencies and efficacy rank orders were observed in all 3 assays but with a lower signal-to-background ratio and increased assay variation in the QRET assay compared to the Eu-GTP filtration and the nonhomogeneous [35S]GTPγS binding assays.

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Kim, Jeong-Ho. "Immobilized DNA-binding assay, an approach for in vitro DNA-binding assay." Analytical Biochemistry 334, no. 2 (2004): 401–2. http://dx.doi.org/10.1016/j.ab.2004.06.045.

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3

Bylund, D. B., and M. L. Toews. "Radioligand binding methods: practical guide and tips." American Journal of Physiology-Lung Cellular and Molecular Physiology 265, no. 5 (1993): L421—L429. http://dx.doi.org/10.1152/ajplung.1993.265.5.l421.

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Radioligand binding assays are a relatively simple but extremely powerful tool for studying receptors. They allow an analysis of the interactions of hormones, neurotransmitters, growth factors, and related drugs with the receptors, studies of receptor interactions with second messenger systems, and characterization of regulatory changes in receptor number, subcellular distribution, and physiological function. As a result, these assays are widely used (and often misused) by investigators in a variety of disciplines, including pharmacology, physiology, biochemistry, immunology, and cell biology. This article presents a broad overview of the radioligand binding assay technique, primarily for the investigator who has limited experience with this technique. Practical guidelines for setting up a new assay are presented, including the receptor preparation to be used, choice of appropriate radioligand, optimizing assay conditions, and appropriate methods for data analysis. Tips for avoiding some of the common pitfalls in application of these assays are also included. The primary focus is on radioligand binding assays of membrane-bound receptors studied in membrane preparations. However, similar assay techniques can be used to study receptors on intact cells. The unique advantages and disadvantages of these intact cell binding assays are also discussed. In particular, the occurrence of regulatory changes in receptors during the course of intact cell binding assays is considered, with approaches for circumventing these complications and for using intact cell assays to advantage in studying these regulatory changes.

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Zhu, Zhengrong, Sean Kim, Taosheng Chen, et al. "Correlation of High-Throughput Pregnane X Receptor (PXR) Transactivation and Binding Assays." Journal of Biomolecular Screening 9, no. 6 (2004): 533–40. http://dx.doi.org/10.1177/1087057104264902.

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Pregnane X receptor (PXR) transactivation and binding assays have been developed into high-throughput assays, which are robust and reproducible (Z′ > 0.5). For most compounds, there was a good correlation between the results of the transactivation and binding assays. EC50 values of compounds in the transactivation assay correlated reasonably well with their IC50 values in the binding assay. However, there were discrepancies with some compounds showing high binding affinity in the binding assay translated into low transactivation. The most likely cause for these discrepancies was an agonist-dependent relationship between binding affinity and transactivation response. In general, compounds that bound to human PXR and transactivated PXR tended to be large hydrophobic molecules.

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FERRARA, PASCUAL, та CHOH HAO LI. "β-ENDORPHIN: RADIORECEPTOR BINDING ASSAY". International Journal of Peptide and Protein Research 16, № 1 (2009): 66–69. http://dx.doi.org/10.1111/j.1399-3011.1980.tb02936.x.

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Duensing, Thomas D., and Susan R. Watson. "Simple Multiplexed Antibody-Binding Assay." Cold Spring Harbor Protocols 2018, no. 1 (2018): pdb.prot093781. http://dx.doi.org/10.1101/pdb.prot093781.

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Lee, Jennifer Y., Sheri Miraglia, Xiongwei Yan, et al. "Oncology Drug Discovery Applications Using the FMAT™ 8100 HTS System." Journal of Biomolecular Screening 8, no. 1 (2003): 81–88. http://dx.doi.org/10.1177/1087057102239668.

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High-throughput screening (HTS) for potential anticancer agents requires a broad portfolio of assay platforms that may include kinase enzyme assays, protein-protein binding assays, and functional cell-based apoptosis assays. The authors have explored the use of fluorometric microvolume assay technology (the FMAT™ 8100 HTS System) in three distinct homogeneous HTS assays: (1) a Src tyrosine kinase enzyme assay, (2) a Grb2-SH2 protein-peptide interaction assay, and (3) an annexin V binding apoptosis assay. Data obtained from all three assays suggest that the FMAT system should facilitate the implementation of homogeneous assays for a wide variety of molecular targeted and cell-based screens. ( Journal of Biomolecular Screening 2003:81-88)

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Vainshtein, Inna, Scott Silveria, Poonam Kaul, Riaz Rouhani, Richard M. Eglen, and John Wang. "A High-Throughput, Nonisotopic, Competitive Binding Assay for Kinases Using Nonselective Inhibitor Probes (ED-NSIP™)." Journal of Biomolecular Screening 7, no. 6 (2002): 507–14. http://dx.doi.org/10.1177/1087057102238624.

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A novel competitive binding assay for protein kinase inhibitors has been developed for high-throughput screening (HTS). Unlike functional kinase assays, which are based on detection of substrate phosphorylation by the enzyme, this novel method directly measures the binding potency of compounds to the kinase ATP binding site through competition with a conjugated binding probe. The binding interaction is coupled to a signal amplification system based on complementation of β-galactosidase enzyme fragments, a homogeneous, nonisotopic assay technology platform developed by DiscoveRx Corp. In the present study, staurosporine, a potent, nonselective kinase inhibitor, was chemically conjugated to a small fragment of β-galactosidase (termed ED-SS). This was used as the binding probe to the kinase ATP binding pocket. The binding potencies of several inhibitors with diverse structures were assessed by displacement of ED-SS from the kinase. The assay format was specifically evaluated with GSK3α, an enzyme previously screened in a radio-active kinase assay (i.e., measurement of [33P]-γ-ATP incorporation into the kinase peptide substrate). Under optimized assay conditions, nonconjugated staurosporine inhibited ED-SS binding in a concentration-dependent manner with an apparent potency (IC50) of 11 nM, which was similar to the IC50 value determined in a radioactive assay. Furthermore, 9 kinase inhibitors with diverse structures, previously identified from chemical compound library screening, were screened using the competitive binding assay. The potencies in the binding assay were in very good agreement with those obtained previously in the isotopic functional activity assay. The binding assay was adapted for automated HTS using selected compound libraries in a 384-well microtiter plate format. The HTS assay was observed to be highly robust and reproducible (Z factors > 0.7) with high interassay precision ( R2 > 0.96). Interference of compounds with the β-galactosidase signal readout was negligible. In conclusion, the DiscoveRx competitive kinase binding assay, termed ED-NSIP™, provides a novel method for screening kinase inhibitors. The format is homogeneous, robust, and amenable to automation. Because there is no requirement for substrate-specific antibodies, the assay is particularly applicable to Ser/Thr kinase assay, in which difficulties in identifying a suitable substrate and antibody preclude development of nonisotopic assays. Although the nonselective kinase inhibitor, staurosporine, was used here, chemically conjugating the ED fragment to other small molecule enzyme inhibitors is also feasible, suggesting that the format is generally applicable to other enzyme systems.

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Calvo, David, María Jesús Vázquez, Charlotte Ashby, and Juan Manuel Domínguez. "Kinetic Considerations on the Development of Binding Assays in Single-Addition Mode." Journal of Biomolecular Screening 17, no. 8 (2012): 1041–49. http://dx.doi.org/10.1177/1087057112452318.

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The development of assays in single-addition mode is of great interest for screening purposes given the multiple advantages of minimizing the number of intervention steps. Binding assays seem to be more prone to this attractive format because no functional biological activity is taking place but instead a biophysical process, whose dynamics seem easier to control without introducing significant alterations, is happening. Therefore, single-addition assays based on the displacement of prebound labeled ligands can be conceived, but careful kinetic considerations must still be taken to maximize the sensitivity of the assay and to avoid jeopardizing the identification of compounds with slow-binding kinetics. This article shows the development of a single-addition, displacement-based binding assay intended to identify modulators that act by binding to the gabapentin site of the ion channel regulatory protein α2δ1. After studying the kinetics of gabapentin binding and the influence they might have on the assay sensitivity, the best conditions were identified, and the sensitivity was compared with that of the more classical two-additions competition-based assay. Although the present study focuses on α2δ1 and its interaction with gabapentin, the rationale and the methodology followed are of broad purpose and can be applied to virtually every binding assay.

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Wilkins, T. A., J. E. Midgley, R. A. Stevens, I. Caughey, and N. Barron. "Assay performance and tracer properties for two analog-based assays of free triiodothyronine." Clinical Chemistry 32, no. 3 (1986): 465–69. http://dx.doi.org/10.1093/clinchem/32.3.465.

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Abstract We determined binding characteristics of the triiodothyronine (T3) analog tracer used in the Amerlex and Amerlex-M FT3 radioimmunoassay for the three endogenous binding proteins in serum: thyroxin-binding globulin (TBG), thyroxin binding prealbumin (PA), and albumin. Both T3 and its analog bind to the same sites on TBG and PA. However, the analog has significantly lower association constants (1.0% and 3.8%, respectively, of T3 binding affinity) and it binds to different sites on albumin. Analog binding is characterized by two (weak) specific binding sites [K = 0.46 (SD 0.03) X 10(5) L/mol]; T3 is bound at about 28 very weak, nonspecific sites [K = 0.41 (SD 0.03) X 10(4) L/mol]. Sera from healthy subjects with a wide range of concentrations of binding proteins showed no interference from analog binding in the FT3 assay. In contrast, in vitro studies of albumin binding revealed a weak dependence of both assays on albumin concentration (0.05 pmol of FT3 per gram of albumin per liter), an interference probably unimportant for most laboratory samples. Nonesterified fatty acids (NEFA) and the T3 analog apparently bind to different sites on albumin; thus the Amerlex FT3 assay is insensitive to moderately increased concentrations of NEFA in serum.

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Dissertations / Theses on the topic "Binding assay"

1

Kopanchuk, Sergei. "Regulation of ligand binding of melanocortin receptor subtypes /." Online version, 2006. http://dspace.utlib.ee/dspace/bitstream/10062/950/5/kopanchuk.pdf.

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Nguyen, Loc Tien. "BIV TAR RNA binding glycine mutant Tat peptides| An integrated modeling and binding assay approach." Thesis, San Jose State University, 2015. http://pqdtopen.proquest.com/#viewpdf?dispub=1602943.

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<p> Interactions between viral encoded regulatory proteins and RNA target sequences control gene expression of Lentiviruses, including human immunodeficiency virus (HIV).  Bovine immunodeficiency virus (BIV) provides a simpler model of interaction between the viral trans-activating protein (Tat) and trans-activation response RNA element (TAR), using Tat peptides binding to TAR RNA fragments. The resulting characterization of the hinge region of native BIV TAR-Tat complex was confirmed by more comprehensive calculations, involving an exhaustive generation of lattice chains. This modeled 2-residues per move of the native 11-mer Tat peptide and a 28-nucleotides TAR fragment. But these sorts of coarse-grained calculations, upon substitution of Gly at key hinge region positions, are not fully sensitive to the local flexibility of amino acid side chains optimized for packing and possible interaction with relevant all-atom RNA structure. An overall binding destabilization effect is indicated for the single substitution at 78 and double substitution of Gly at positions 75 and 78. Destabilization effects were further examined, and model data showed that it included both potential and flexibility effects. Future studies require 1-residue per move approach and building all-atom models to fully examine molecular interactions of TAR-Tat complexes.</p>

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Meddins, Anna Kathryn. "Isolating candidate cyclin-binding proteins using the Yeast Two-Hybrid assay." Thesis, University of Cambridge, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.627268.

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Pueblo, Hanna Elizabeth. "APPLICATIONS OF DYNAMIC ISOELECTRIC/ANISOTROPY BINDING LIGAND ASSAY FOR PROTEOMIC RESEARCH." OpenSIUC, 2012. https://opensiuc.lib.siu.edu/dissertations/494.

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The work presented in this dissertation centers around the development of analytical tools for the study of advanced proteomics. Section 1 of this work reviews the need for high efficiency protein separation techniques. Dynamic isoelectric focusing (DIEF) is new technique similar to capillary isoelectric focusing (CIEF) invented by Dr. Luke Tolley at Southern Illinois University Carbondale. Using DIEF, the electric field inside the separation capillary can be modified using high voltage electrodes, additional to the anode and cathode, to control the depth and shape of the resulting pH gradient. By changing the pH gradient, the location and width of focused protein bands can be controlled. As a new analytical technique, the development of DIEF required the design and fabrication of special holders which allow for electrical connections to be made at lengths along the separation capillary. These holders were also designed to have a removable section of capillary to extract very specific pH range proteins from high-resolution separations. Higher throughput DIEF systems were investigated, as well as multiplexed DIEF systems. Section 2 covers the topic of dynamic isoelectric/anisotropy ligand binding assay (DIABLA). DIABLA is a new method used to identify proteins in a complex sample that bind to a known molecule. DIABLA has the potential to be used in two complimentary ways, discovery mode and scanning mode. Both modes are accomplished by using DIEF, followed by fluorescence anisotropy as a sensitive detection method. This allows the entire length of capillary to be scanned to identify areas of non-zero anisotropy, which indicate binding interactions between the protein and target molecule. The binding protein(s) can then be extracted using the removable section of capillary from the DIEF holder, and can be identified by using a second dimension analysis, such as LC/MS/MS. DIABLA was verified in a series of proof-of-concept experiments in both discovery and scanning modes. These experiments involved fluorescently tagging proteins that were focused in the presence of a ligand tagged with a different fluorophore. The usefulness of DIABLA as a separation technique was demonstrated in four specific analyses of complex protein samples in Chapter 10.

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Sudlow, James. "Design, synthesis and high-throughput assay of inhibitors for p97-cofactor binding." Thesis, Imperial College London, 2014. http://hdl.handle.net/10044/1/24875.

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p97 is an abundant protein in human cells and is essential for many forms of life. Its putative mechanism of action is the binding of adaptor proteins, which mediate its functions, and subsequent transfer of energy from ATP hydrolysis through the adaptor to substrate proteins. The unfolding or degradation of these substrates is known to regulate a diverse number of processes and the malfunction of p97 in many of these has been linked to a range of diseases. Developing inhibitors for p97-cofactor binding may help uncover further functions, as well as potentially providing a treatment for a number of the diseases in which p97 is implicated. A high-throughput assay based on Förster Resonance Energy Transfer (FRET) was developed, which allowed the high-throughput analysis of candidate compounds. Using this assay, the affinity of p97 for several of its partner proteins was measured. The results were found to be similar to literature values and the assay was measured to have a high Z' factor. Analysis of the hot-spot interactions between p97 and the adaptor protein, p47, enabled the design of novel peptide inhibitors of p97-Cofactor binding. A range of small molecules were also identified through a computer modelling approach known as scaffold hopping. A peptide that was designed to closely mimic the S3/S4 loop within p47 was found to bind to p97 and inhibit its interaction with p47. No inhibition, however, was detected from a second generation of peptides. Two molecules from the virtual ligand screen were found to inhibit p97 binding. Of these, one of the compounds was an unnatural tripeptide, amenable to the rapid synthesis of multiple variations. A second generation of compounds based on this original hit was analysed and another compound was identified with an improved level of inhibition.

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Bourns, Brenda. "Development and characterization of a new assay to examine telomere-protein interactions in vivo /." Thesis, Connect to this title online; UW restricted, 1997. http://hdl.handle.net/1773/6336.

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Engqvist, Martin. "A generic capture assay for immunogenicity, using Biacore." Thesis, Uppsala universitet, Institutionen för biologisk grundutbildning, 2013. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-198767.

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The purpose of this investigation was to create and optimise a capture assay for the detectionof anti-drug antibodies (ADA) in human plasma, using Biacore. We also dealt with the nonspecificplasma binding to mouse-derived anti-biotin which may occur in the capture assay.By paying attention to these things we aimed at reaching as high sensitivity as possible for theADA detection. The capture assay also benefited and gained flexibility from using the same regenerationsolution irrespective of drug and from having a composition that minimises the risk ofdamaging drug epitopes.

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Mahatnirunkul, Thanisorn. "One-step gold nanoparticle size-shift assay using synthetic binding proteins and dynamic light scattering." Thesis, University of Leeds, 2017. http://etheses.whiterose.ac.uk/19216/.

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Gold nanoparticles (AuNPs) have attracted significant interest for biosensing applications because of their distinctive optical properties including light scattering. Dynamic light scattering (DLS) is an analytical tool used routinely for measuring the hydrodynamic size of colloids and nanoparticles in liquid environment. By combining the light scattering properties of AuNPs with DLS, a label-free, facile and sensitive assay has been developed. There have been several reports showing that NPcoupled DLS size shift assays are capable of quantitative analysis for target analytes ranging from metal ions to proteins as well as being a tool for biomolecular interaction studies. The principle of the assay developed is to immobilise bioreceptors (antibodies, oligonucleotides or synthetic binding proteins) specific to the target analyte onto AuNPs to produce nanobiosensors. When the analyte is added to the system, binding of the target protein to the immobilised bioreceptors leads to a size increase of the functionalised AuNPs. The hydrodynamic diameter (DH) can then be measured by DLS for complete quantitation. However, the ability to use synthetic binding proteins (Affimers) in optical sensing has not been investigated. Here, antimyoglobin (Mb) Affimers were selected by biopanning of a phage display library and subcloned into a bacterial plasmid for expression in a prokaryotic system. These Affimers were then expressed and characterised before being used as bioreceptors in the NP-coupled DLS size shift assay. The Affimer functionalised AuNPs were compared to those using polyclonal antibodies (IgG) as bioreceptors. The Affimer nanobiosensors could selectively detect Mb with a limit of detection of 554 fM when multiple Affimer clones were immobilized onto the AuNPs, which was comparable to IgG based nanobiosensors (LOD = 148 fM). These findings suggest that in general a polyclonal reagent is optimum for the assay. In addition, other factors, such as AuNP size and concentration, related to the assay were investigated. The detection range of the size shift assay could be tailored to each analyte by selecting the appropriate AuNP size and concentration. This fundamental data will serve as a base for future studies of using Affimers in DLS based sensing applications.

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Xie, Tian. "Scintillation proximity assay (SPA) measuring p53 DNA binding and total p53 level in human thyroid cancer cell line ARO." Diss., Online access via UMI:, 2007.

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10

Wan, Jonathan. "Development of a Pulse Proteolysis Assay to Investigate Stability in the Measles Polymerase Nucleocapsid Binding Domain." Thesis, The University of Arizona, 2013. http://hdl.handle.net/10150/297801.

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The nucleocapsid-binding domains (NBDs) form part of the paramyxovirus replication complex and mediate attachment to the nucleocapsid, a nucleoprotein complex containing the viral RNA genome. NBDs form a very simple helical bundle, and vary between intrinsically unstructured and highly stable in the case of mumps and measles respectively. Despite the differences in properties, these domains show similar sequence and structure. The differences between mumps and measles NBDs provide a point of comparison to investigate differences in structural stability. Using the measles protein as a starting point, we created variants of different stabilities and devised a convenient assay based on pulse proteolysis to rank the variants. A library of NBD variants fused to the SUMO protein were generated by random mutagenesis, and used as a test case for assay development. Three variants of different stabilities were sequenced and their apparent stability differences rationalized based on the mutations present. Pulse proteolysis was then used to screen for the stability and it was concluded to be an effective tool in screening the library for appropriate mutations to be analyzed.

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Books on the topic "Binding assay"

1

Receptor binding techniques. 3rd ed. Humana Press, 2012.

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Moyse, Emmanuel. Visualization of receptors in situ: Applications of radioligand binding. CRC Press, 2001.

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Munson, Peter J. A user's guide to LIGAND: Data analysis and curve-fitting for ligand binding experiments. 2nd ed. Laboratory of Theoretical and Physical Biology, National Institute of Child Health and Human Development, National Institutes of Health, 1987.

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Smiljanic-Georgijev, Natasha. Evaluation of the hydrophobic and oligosaccharide binding functions of the G[subscript]Mb2s activator protein by fluorescence dequenching assay. National Library of Canada = Bibliothèque nationale du Canada, 1999.

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Khan, Masood N., and John W. A. Findlay, eds. Ligand-Binding Assays. John Wiley & Sons, Inc., 2009. http://dx.doi.org/10.1002/9780470541517.

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Cell surface receptors: A short course on theory & methods. 3rd ed. Springer, 2004.

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Cell surface receptors: A short course on theory and methods. Nijhoff, 1986.

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Limbird, Lee E. Cell surface receptors: A short course on theory and methods. 2nd ed. Kluwer Academic Publishers, 1996.

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9

I, Yamamura Henry, Enna S. J, and Kuhar Michael J, eds. Neurotransmitter receptor binding. 2nd ed. Raven Press, 1985.

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Davenport, Anthony P. Receptor Binding Techniques. 2nd ed. Humana Press, 2005.

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Book chapters on the topic "Binding assay"

1

Harvath, Liana, Robert R. Aksamit, and Robert E. Cunningham. "Assay for Chemoattractant Binding." In Immunocytochemical Methods and Protocols. Humana Press, 1994. http://dx.doi.org/10.1385/0-89603285-x:269.

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Catani, Valeria M., and Valeria Gasperi. "Assay of CB1 Receptor Binding." In Methods in Molecular Biology. Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3539-0_5.

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Sakuma, Keiichiro, and Reiji Kannagi. "Selectin-Binding Assay by Flow Cytometry." In Methods in Molecular Biology. Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-0430-4_11.

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Gabaglio, Marina, Pamela Prini, Erica Zamberletti, Tiziana Rubino, and Daniela Parolaro. "Assay of GTPγS Binding in Autoradiography." In Methods in Molecular Biology. Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3539-0_10.

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Miller, Katherine R., and David P. Cistola. "Titration calorimetry as a binding assay for lipid-binding proteins." In Cellular Fatty Acid-Binding Proteins II. Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-3096-1_5.

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Makkar, Harinder P. S. "Protein-Binding Capacity by Filter Paper Assay." In Quantification of Tannins in Tree and Shrub Foliage. Springer Netherlands, 2003. http://dx.doi.org/10.1007/978-94-017-0273-7_9.

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Pucci, Michael J., and Thomas J. Dougherty. "A Method to Assay Penicillin-Binding Proteins." In Methods In Molecular Medicine™. Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-246-5_11.

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Christensen, P. "Receptor Assay Based on 3H-Imipramine Binding." In Clinical Pharmacology in Psychiatry. Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-71288-3_23.

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Finlayson, Keith, and John Sharkey. "A High-Throughput Binding Assay for HERG." In Optimization in Drug Discovery. Humana Press, 2004. http://dx.doi.org/10.1385/1-59259-800-5:353.

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Munnik, Teun, and Magdalena Wierzchowiecka. "Lipid-Binding Analysis Using a Fat Blot Assay." In Methods in Molecular Biology. Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-401-2_23.

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Conference papers on the topic "Binding assay"

1

Sigurdson, M., H. Feldman, and C. D. Meinhart. "AC Electrokinetics for Assay Enhancement." In ASME 2007 International Mechanical Engineering Congress and Exposition. ASMEDC, 2007. http://dx.doi.org/10.1115/imece2007-42224.

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We have developed an AC electrokinetic microstirring technique, and have demonstrated its ability to accelerate diffusion-limited binding in a micro device by nearly an order of magnitude. Binding rates are increased by augmenting diffusive transport with microstirring generated through the application of an AC electric field. Numerical simulations suggest optimized microstirring devices may increase binding by a factor of 20.

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Chen, Jing-Yin, Joseph R. Knab, Shuji Ye, Yunfen He, and Andrea G. Markelz. "Using terahertz spectroscopy as a protein binding assay." In Biomedical Optics 2006, edited by Gerald E. Cohn, Warren S. Grundfest, David A. Benaron, and Tuan Vo-Dinh. SPIE, 2006. http://dx.doi.org/10.1117/12.664098.

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Woodroofe, Carolyn C., Matthew B. Robers, Thomas A. Kirkland, et al. "Abstract 4241: Isozyme-selective intracellular binding assay for histone deacetylases ." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-4241.

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Lee, Lim, Timo R. Bretschneider, and Peter R. Preiser. "Automatic Analysis of Cos-7 Binding Assay Imagery for Malaria Vaccination Experiments." In 2006 9th International Conference on Control, Automation, Robotics and Vision. IEEE, 2006. http://dx.doi.org/10.1109/icarcv.2006.345383.

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Khavrutskii, Lyuba, Sergey G. Tarasov, Colin Fields, Karen Stefanisko, and Nadya Tarasova. "Abstract 4029: Robust Ras inhibition assay utilizing fully synthetic Ras-binding domain." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-4029.

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6

Ingerslev, J., S. Stenbjerg, A. Bukh, NPH Møller, and J. Zeuthen. "EVIDENCE FOR AN ABNORMAL EXPRESSION OF THE COLLAGEN BINDING DOMAIN IN VON WILLEBRAND'S DISEASE TYPE II." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644644.

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A recently developed new series of monoclonal antibodies (MAbs) against the von Willebrand factor (vWf) included antibodies strongly inhibiting ( Mab vWf-41) and partly inhibiting ( Mab vWf-33) the collagen binding of vWf. We also characterized two Mabs with interacting properties against the ristocetin induced platelet aggregation (MAbs vWf-21 and vWf-39). These antibodies were conjugated with horse-radish peroxidase (HRP) and examined in different constructions forming two-site MAb ELISA's for plasma vWf:Ag and compared with polyclonal antibody ELISA. Symmetrical MAb-ELISA ( i.e. same Mab for extraction and detection) gave practical no dose-response in the standard assay, whereas any different combination of Mabs gave favourable dose-response relationships in sensitive ELISA's for vWf:Ag. Two different sandwiches were chosen using MAb vWf-33 and Mab vWf-41 at either side of the ELISA. These two assay models gave results of plasma from normal persons almost identical to those obtained with polyclonal antibody ELISA. Also in type I von Willebrand's disease these three assays performed very uniformly. In subtypes II plasma ( IIA: n=7; IIB: n=3, IIC: n=l, IID: n=i) . the assay using vWf-33 for coating and vWf-41-HRP for detection measured considerably lower than the polyclonal ELISA and the Mab-ELISA based on the opposite combination. We believe, that our results are indicative of a molecular defect in the collagen binding domain of vWf in subtype II plasma.

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Zhdanova, Nadezda, Evgeny Shirshin, Victor Fadeev, and Alexander Priezzhev. "SDS-binding assay based on tyrosine fluorescence as a tool to determine binding properties of human serum albumin in blood plasma." In Saratov Fall Meeting 2015, edited by Elina A. Genina, Valery V. Tuchin, Vladimir L. Derbov, et al. SPIE, 2016. http://dx.doi.org/10.1117/12.2229850.

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8

Kalyan, N. K., S. G. Lee, W.-T. Hum, R. Hartzell, M. Levner, and P. P. Hung. "IN VITRO STUDIES ON THE BINDING OF TISSUE-TYPE PLASMINOGEN ACTIVATOR (t-PA) AND UROKINASE (u-PA) TO LIVER MEMBRANES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643603.

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The plasminogen activators, t-PA and u-PA, are glycoproteins known to be involved in homeostasis of the blood clotting system, and thus are of potential clinical use in the treatment of thrombosis. Several in vivo studies have shown that both t-PA and u-PA are quickly removed from the blood circulation, predominantly by the liver. The mechanism by which the liver removes these proteins is not understood. To delineate this, we conducted in vitro studies of binding of PAs or their derivatives to isolated mouse liver membranes utilizing a functional assay developed in our laboratory. The assay consisted of initial binding of t-PA to liver membranes followed by centrifugation to pellet the membranes and the assay of the activity of the membrane-bound t-PA by a fibrin-agar plate method. The bound t-PA, which retained complete enzymic activity, could be dissociated by SDS treatment in an undegraded form as shown by SDS-PAGE. The binding of t-PA as well as u-PA was very fast and did not compete with glycoproteins or sugars containing the terminal galactose, mannose and N-acetylglucosamine residues. Furthermore, the treatment of t-PA with neuraminidase and/or periodate oxidation did not affect its binding characteristics. These data suggest that the carbohydrate moieties of t-PA and u-PA, unlike many glycoproteins, do not mediate their binding to the liver. This raised the possibility of the liver binding sequence being located in the protein backbone, especially the non-protease domains which are known to determine the biological specificities of PAs. The relative binding of u-PA and its low molecular weight (LMW) derivative containing only the protease domain, to the liver membranes was studied. Unlike u-PA and t-PA, LMW-urokinase did not bind significantly. This suggests that the protein sequence containing the non-protease domains, rather than the carbohydrate moieties of PAs contain the information necessary for binding to the liver and possibly their clearance from the blood circulation.

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Bosma, P. J., D. C. Rijken, and W. Nieuwenhuizen. "BINDING OF TISSUE-TYPE PLASMINOGEN ACTIVATOR AND PLASMINOGEN TO FIBRINOGEN AND ITS DEGRADATION PRODUCTS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644402.

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In order to localize the binding site(s) for tissue-type plasminogen activator (t-PA) in the fibrin(ogen) molecule, two-chain t-PA was immobilized onto microtitration plates and incubated with fibrinogen and various fibrinogen fragments. The extent of binding was quantified with an enzyme immunoassay. Hardly any binding to t-PA was observed with fibrinogen, fragments X, Y and E. A moderate binding was observed with fragments D(cate) and D(EGTA) and a strong binding with the cyanogen bromide fragment FCB-2 (Kd apparent = 65 nM). Results of control experiments, in which the binding of fibrinogen and its fragments to immobilized Lys-plasminogen was measured, using the same assay, were in line with literature data: hardly any binding was found with fibrinogen, fragments X and Y. A moderate binding was observed with fragments D and E and a strong binding with FCB-2 (Kd apparent = 100 nM). The stimulatory capacity of the various fragments on the Lys-plasminogen activation by t-PA, as studied in a spectrophotometric assay, was found to be absent for fragment E, low for fibrinogen, fragments X, Y and D, and high for FCB-2. It is concluded that the t-PA binding site in the fibrin (ogen) molecule resides in the distal domains from which fragments D and FCB-2 are derived. The site is apparently hidden in fibrinogen and early fibrinogen degradation products. Binding of both plasminogen and t-PA is required for stimulation of the plasminogen activation, as illustrated by fragment E which binds plasminogen and no t-PA, and has no stimulatory capacity.

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Laser, Daniel. "New Microfluidic Technologies for Accelerating and Enhancing Molecular Binding Processes in Cartridge-format Assay Systems." In CLEO: Science and Innovations. OSA, 2013. http://dx.doi.org/10.1364/cleo_si.2013.atu1n.1.

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Reports on the topic "Binding assay"

1

Chung, Arthur. Development of Novel Ligand Binding Assay for Estrogen Receptor. Defense Technical Information Center, 2000. http://dx.doi.org/10.21236/ada390487.

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2

Chung, Arthur C. Development of a Novel Ligand Binding Assay for Estrogen Receptor. Defense Technical Information Center, 2002. http://dx.doi.org/10.21236/ada421346.

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