ProteOn™ XPR36 Protein Interaction Array System

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Overview

ProteOn™ Technology and Applications
Analysis of Lipid-Protein Interactions
Analysis of Integral Membrane Protein–Antibody and Lipid-Protein Interactions Using the ProteOn XPR36 Protein Interaction Array System

Introduction
The interplay of interactions between membranes, membrane proteins, and antibodies is of great interest in the field of drug discovery and development. Membrane proteins and membrane-associated proteins and peptides have been shown to be important in many biological processes and are involved in key pathways in diseases such as cancer. Membrane proteins are fast becoming the next big class of drug targets.

This poster describes the use of a ProteOn XPR36 protein interaction array system, which uses surface plasmon resonance to measure 36 biomolecular interactions simultaneously, to study the interaction of artificial membranes and two significant peptides.

PDF Bulletin 5922 To read more click here

ProteOn XPR36 Protein Interaction Array System Bibliography

PDF Bulletin 5952 Download Bulletin 5952 (bibliography in PDF format).

Abdiche Y et al. (2008). Determining kinetics and affinities of protein interactions using a parallel real-time label-free biosensor, the Octet. Anal Biochem 377, 209–217.
Abdiche YN et al. (2008). Probing the binding mechanism and affinity of tanezumab, a recombinant humanized anti-NGF monoclonal antibody, using a repertoire of biosensors. Protein Sci 17, 1326–1335.
Abdiche YN et al. (2009). Exploring blocking assays using Octet, ProteOn, and Biacore biosensors. Anal Biochem 386, 172–180.
Abu-Hamad, S., et al., (2009), The VDAC1 N-terminus is essential both for apoptosis and the protective effect of anti-apoptotic proteins, Journal of Cell Science 122, 1906–1916.
Appleton BA et al. (2007). Structural studies of neuropilin/antibody complexes provide insights into semaphorin and VEGF binding. EMBO J 26, 4902–4912.
Artzy-Schnirman A, et al. (2008). A two-state electronic antigen and an antibody selected to discriminate between these states, Nano Letters, Vol. 8, No. 10, 3398–3403.
Arzoine, L., (2009). Voltage-dependent anion channel-1-based peptides interact with hexokinase to prevent its anit-apoptotic activity, Journal of Biol Chem 284, 3946–3955.
Balducci C et al. Synthetic amyloid-b oligomers impair long-term memory independently of cellular prion protein. Proc Natl Acad Sci U S A 107, 2295–2300.
Biasini E et al. (2009). Immunopurification of pathological prion protein aggregates. PLoS One 4, e7816.
Blow, N., (2009). Proteins and proteomics: life on the surface, Nature Methods, 6, 389–393.
Bravman T et al. (2006). Exploring “One-shot” Kinetics and small molecule analysis using the ProteOn XPR36 array biosensor. Anal Biochem 358, 281–288.
Bravman, T., et. al. (2008), The ProteOn XPR36 array system—high throughput kinetic binding analysis of biomolecular interactions, DOI: 10.1007/s12195-008-0036-4.
Brehin AC et al. (2008). Production and characterization of mouse monoclonal antibodies reactive to chikungunya envelope E2 glycoprotein. Virology 371, 185–195.
Brod E, Nimri S, Turner B, Sivan U. (2008). Electrical control over antibody-antigen binding. Sensors and Actuators B: Chemical 128, 560–565.
Bronner V et al. (2008). Evaluating candidate lead compounds by rapid analysis of drug interactions with human serum albumin. Am Biotechnol Lab 26, 14–16.
Cohen-Ben-Lulu GN et al. (2008). The bacterial flagellar switch complex is getting more complex. EMBO J 27, 1134–1144.
Colombo, G and Gobbi, M., et al (2010). Non-peptidic thrombospondin-1-mimics as fibroblast growth factor-2 inhibitors: An integrated strategy for the development of new antiangiogenic compounds, January 2010.
Di Fede G., eta al. (2009). A recessive mutation in the APP gene with dominant-negative effect on Amyloidogenesis, Science 323, 1473.
Dubin-Bar D et al. (2008). The Drosophila IKK-related kinase (Ik2) and spindle-F proteins are part of a complex that regulates cytoskeleton organization during oogenesis. BMC Cell Biol 9, 51.
Ezerzer, C., et al., (2009) Chemokine receptor-derived peptides as multi-target drug leads for the treatment of inflammatory diseases, Peptides 30 (2009) 1296–1305.
Gasparian ME, et al, (2009), Generation of new TRAIL mutants DR5-A and DR5-B with improved selectivity to death receptor 5, Apoptosis (2009) 14:778–787.
Gesuete R et al. (2009). Recombinant C1 inhibitor in brain ischemic injury. Ann Neurol 66, 332–342.
Gevorkyan-Airapetov L et al. (2009). Interaction of Tim23 with Tim50 is essential for protein translocation by the mitochondrial TIM23 complex. J Biol Chem 284, 4865–4872.
Goldin N et al. (2008). Methyl jasmonate binds to and detaches mitochondria-bound hexokinase. Oncogene 27, 4636–4643.
Hosse RJ et al. (2009). Kinetic screening of antibody-Im7 conjugates by capture on a colicin E7 DNase domain using optical biosensors. Anal Biochem 385, 346–357.
Kalie E et al. (2007). An interferon alpha2 mutant optimized by phage display for IFNAR1 binding confers specifically enhanced antitumor activities. J Biol Chem 282, 11602–11611.
Kalie E et al. (2008). The stability of the ternary interferon-receptor complex rather than the affinity to the individual subunits dictates differential biological activities. J Biol Chem 283, 32925–32936.
Katz, C., et al. (2008). Molecular basis of the interaction between the antiapoptotic Bcl-2 family proteins and the proapoptotic protein ASPP2, PNAS, vol. 105, no. 34.
LeMaire-Adkins R (2007). One-shot deal. Drug Discovery & Dev 10 (9).
Lu, J., et al., (2009), Functional characterization of a promoter polymorphism in APE1/Ref-1 that contributes to reduced lung cancer susceptibility, The FASEB Journal article fj.09-136549.
Nahshol O, et al. (2008). Parallel kinetic analysis and affinity determination of hundreds of monoclonal antibodies using the ProteOn XPR36, Anal Biochem 383, 52–60.
Pan M et al. (2008). Mutation of the IFNAR-1 receptor binding site of human IFN-alpha2 generates type I IFN competitive antagonists. Biochemistry 47, 12018–12027.
Podoly E et al. (2009). The butyrylcholinesterase k variant confers structurally derived risks for Alzheimer pathology. J Biol Chem 284, 17170–17179.
Podoly, E., et al. (2009), The Butyrylcholinesterase K variant confers structurally derived risks for Alzheimer pathology, The Journal of Biol Chem, vol. 284, no. 25.
Potapov V et al. (2008). Computational redesign of a protein-protein interface for high affinity and binding specificity using modular architecture and naturally occurring template fragments. J Mol Biol 384, 109–119.
Reichmann D et al. (2005). The modular architecture of protein-protein binding interfaces. Proc Natl Acad Sci U S A 102, 57–62.
Reichmann D et al. (2005). The modular architecture of protein-protein binding interfaces. Proc Natl Acad Sci U S A 102, 57–62.
Reichmann D et al. (2007). Binding hot spots in the TEM1-BLIP interface in light of its modular architecture. J Mol Biol 365, 663–679.
Reichmann D et al. (2008). On the contribution of water-mediated interactions to protein-complex stability. Biochemistry 47, 1051–1060.
Rich RL and Myszka DG (2007). Higher-throughput, label-free, real-time molecular interaction analysis. Anal Biochem 361, 1–6.
Rich RL and Myszka DG (2007). Survey of the year 2006 commercial optical biosensor literature. J Mol Recognition 20, 300–366.
Rich RL and Myszka DG (2008). Survey of the year 2007 commercial optical biosensor literature, J Mol Recognition, (www.interscience.wiley.com) DOI:10.1002/jmr.928
Slutzki M et al. (2006). Variations in the unstructured C-terminal tail of interferons contribute to differential receptor binding and biological activity. J Mol Biol 360, 1019–1030.
Stadtmueller B and Myszka DG (2010). Structural models for interactions between the 20S proteasome and its PAN/19S activators, J Biol Chem 285, 13–17.
Sun, B., et al. (2008). Molecular basis of the interaction of Saccharomyces cerevisiae Eaf3 chromo domain with methylated H3K36. http://www.jbc.org/cgi/doi/10.1074/jbc.M806564200.
Tenhumberg S et al. (2008). Structure guided optimization of the interleukin-6 trans-signaling antagonist sgp130. J. Biol. Chem. 283: 27200–27207.
Trinh DV et al. (2008). The nuclear I kappaB protein I kappaB zeta specifically binds NF-kappab p50 homodimers and forms a ternary complex on kappab DNA. J Mol Biol 379, 122–135.
Tubbs, J. L., (2009). Alkylated DNA damage flipping bridges base and nucleotide excision repair, Nature manuscript.
Xin F et al. (2008). Molecular identification and characterization of peptide: N-glycanase from Schizosaccharomyces pombe. Biochem Biophys Res Commun 368, 907–912.
Yosef, E., et al. (2008). Computational design of calmodulin mutants with up to 900-fold increase in binding specificity, doi: 10.1016/j.jmb.2008.09.053.
Yousef M (2007). Advances in rapid monoclonal antibody screening. Am Biotechnol Lab, November/December issue.
Zhang D et al. (2009). Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor. Mol Cell 36, 1018–1033.
Zhang, F., et al., (2009). VEGF-B is dispensable for blood vessel growth but critical for their survival, and VEGF-B targeting inhibits pathological angiogenesis, www.pnas.org/cgi/content/full/0813061106/DCSupplemental
Zhang. D., Bronner, V., et al., (2009). Together, Rpn10 and Dsk2 can serve as polyubiquitin chain-length sensor, Cell Press, Molecular Cell 36, 1018–1033.
Trade Journal Publications
Swinderman, A., (2009), An affinity for membrane proteins, Drug Discovery News, March 2009.
Mainini, C., (2009), Binding affinities in protein-protein interactions, sp2 Magazine (Genomics & Proteomics).
Moriarty, L., (2009), Protein interaction array system Interview, SelectScience.tv, http://www.selectscience.net/SelectScience-TV/Videos/&showID=&video_type=&videoID=207&classI=0#video.
Moriarty, L., (2009), Multiplexed SPR accelerates protein interaction studies, Bioscience Technology.
Blow, N., (2009), Proteins and proteomics: Life on the surface, Nature Methods.
Perkel, Jeffrey M., (2009), Who needs lables? Macromolecular Interaction Sans Labels, AAAS/Science.
Moriarty, L., (2009), The adoption of SPR in drug discovery and development, Pharma Magazine, Sept/Oct. Issue.
BioRadiations Publications
Cover Story (2006), Analyzing protein interactions with the ProteOn XPR36 protein interaction array system, BioRadiations 119, 16–21.
Bronner, V., et al (2006), Analysis of multiple protein-protein interactions using the ProteOn XPR36 protein interaction array system, BioRadiations 119, 22–24.
Bronner, V., et al (2006), Rapid and detailed analysis of multiple antigen-antibody pairs using the ProteOn XPR36 protein interaction array system, BioRadiations 119, 25–27.
Cover Story (2007), Accelerating research and discovery with the ProteOn XPR36 protein interaction array system, BioRadiations 122, 16–21.
Shlomit, C, et al (2007), Applications of the ProteOn NLC sensor chip: Antibody-antigen, DNA-protein, and protein-protein interactions, BioRadiations 122. 22-23.
Turner, B., et al (2008), Applications of the ProteOn GLH sensor chip: Interactions between proteins and small molecules, BioRadiations 124, 28–29.
Product Focus (2008), ProteOn XPR36 proteininteraction array system: Regulatory tools for drug development, BioRadiations 125, 9.
Bronner, V., et al (2009), Rapid assay development and optimization for small molecule drug discovery, BioRadiations 127, 30–31.
Cover Story (2009), Gette, B., Miller, S. Removing obstacles to discovery – A more than 55 year tradition, Bio-Radiations 128, 16–21.
Customer Interview with Marco Gobbi (2009), Accelerating the study of fibrillogenic peptides, BioRadiations 129, 30–31.
ProteOn™ Webinar Series

The ProteOn webinars feature presentations from leaders in the field of label-free biomolecular interaction analysis using surface plasmon resonance (SPR) technology. Since 2009 this webinar series has covered a wide range of novel SPR applications spanning protein characterization, antibody and small molecule drug discovery, and structural biology research topics.

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The ProteOn™ XPR36 protein interaction array system is an SPR optical biosensor that provides real-time data on the affinity, specificity, and interaction kinetics of protein interactions. Using XPR technology*, a unique approach to multiplexing, this system generates a 6 x 6 interaction array for the simultaneous analysis of up to six ligands with up to six analytes. The ProteOn XPR36 system increases the throughput, flexibility, and versatility of experiment design, enabling the completion of more experiments in less time:

  • Analyze up to 36 different protein interactions in a single run, on a single chip
  • Perform a complete kinetic analysis in a single run
  • Measure a variety of experimental conditions simultaneously in parallel
  • Screen multiple panels of analytes

See the ProteOn Technology and Applications videos for more information about how the ProteOn system works and how it can be applied to drug discovery and to address important experimental questions.

The ProteOn XPR36 protein interaction analysis system includes all of the components required for interaction analysis: instrumentation, ProteOn Manager™ software, ProteOn sensor chips, buffer and reagent kits, and protocol development kits.

User-friendly ProteOn Manager software uses a flexible, guided approach to coordinate instrument control, experiment setup, and data analysis.

Key Features and Benefits

  • Novel 6 x 6 array design
  • Real-time data acquisition
  • Analysis of interaction kinetics, binding affinity, and analyte concentration
  • No radiochemical or fluorescent labels needed
  • Integrated system

Applications and Uses

  • Antibody characterization and development
  • Large and small molecule drug development
  • Protein interface analysis
  • Protein complex and cascade analysis

*The ProteOn XPR36 protein interaction array system is covered by Bio-Rad patents, including United States patent numbers 8,111,400, 8,105,845, 7,999,942, and 7,443,507.

This product or portions thereof is manufactured and sold under license from GE Healthcare under United States patent numbers 5,554,541, 7,736,587, and 8,021,626, and any international patents and patent applications claiming priority.

Number of interaction spots 36
Number of interspot references 42
Response uniformity <2% CV
Refractive index range 1.33–1.37 refractive index units
Dynamic range, RU 1–40,000
Baseline noise <1 RU, 1–20,000 RU
<1.5 RU, 20,000–40,000 RU
Baseline drift <1 RU/min (15–40°C)*
Operating temperature range 15–40°C*
Autosampler temperature range 2–35°C
Sample configuration 72 x 1.5 ml vials or 2 x 96-well microplates
CCD 12-bit digital camera
Acquisition rate 3 Hz (3 images/sec), average 3 images/data point
Weight, kg 85
Dimensions (W x H x D), cm 95 x 58 x 50
Controller with 19" flat panel monitor (1,280 x 1,024 pixels) supplied with instrument  
* Not lower than 15°C below room temperature.  
ProteOn XPR36 Protein Interaction Array System #176-0100
ProteOn XPR36 Protein Interaction Array System

176-0100
100–240 V, includes ProteOn XPR36 instrument, ProteOn Manager™ software, controller/display, maintenance kit (#176-4100), One-shot Kinetics™ kit (#176-1010), buffers, and accessories

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ProteOn Controller and Display #176-0300
ProteOn Controller and Display

176-0300
PC and 19 in. flat-panel monitor (1,280 x 1,024 pixels), for use with the ProteOn XPR36 protein interaction array system

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ProteOn Manager Software #176-0200
ProteOn Manager™ Software

176-0200
Software for ProteOn XPR36 instrument control, experiment design, data collection, and analysis, CD-ROM, includes HASP key

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Number Description Options
6550 Building New Anti-HIV Molecules with Bio-Rad’s ProteOn™ XPR36 System, Rev A Click to download
6132 The ProteOn HTG Sensor Chip: Novel Surface for Stable Capture of Histidine-Tagged Proteins for Protein-Protein Interaction Analysis, Rev A Click to download
6299 Guide to SPR Data Processing on the ProteOn XPR36 Protein Interaction Assay System, Rev A Click to download
6300 Guide to SPR Data Analysis on the ProteOn XPR36 System, Rev A Click to download
6295 ProteOn Sensor Chips, Tips and Techniques, Rev A Click to download
5948 Attachment of Membrane Protein Interactions Using Lipoparticles Bound to the Surface of the ProteOn XPR36 Sensor Chips, Rev A Click to download [ Add to Cart (Free) ]
5968 Screening and Characterization of Human Immunoglobulin G Binding Peptides Using the ProteOn XPR36 Protein Interaction Array System, Rev A Click to download [ Add to Cart (Free) ]
6044 Analyte Interaction and Kinetics Guide, Rev A Click to download
5960 High-Throughput Profiling of Kinase Inhibitors Selectivity Using the ProteOn™ XPR36 Protein Interaction Array System, Rev A Click to download
5390 ProteOn XPR36 Protein Interaction Array System Brochure, Rev D Click to download [ Add to Cart (Free) ]
5538 Analyzing Protein Interactions With the ProteOn XPR36 Protein Interaction Array System, Rev D Click to download [ Add to Cart (Free) ]
5413 ProteOn XPR36 Hardware Product Information Sheet, Rev B Click to download
5627 ProteOn Manager Software Product Information Sheet, Rev C Click to download [ Add to Cart (Free) ]
5404 ProteOn Sensor Chips Product Information Sheet, Rev E Click to download [ Add to Cart (Free) ]
5410 ProteOn Protocol Development Kits Product Information Sheet, Rev B Click to download [ Add to Cart (Free) ]
5409 Protein Interaction Analysis Ordering Information Sheet, Rev E Click to download [ Add to Cart (Free) ]
5819 ProteOn XPR36 Protein Interaction Array System: Regulatory Tools for Drug Development Product Focus, Rev A Click to download
5965 Rapid, High-Throughput Screening of Protein Kinase Inhibitors Using the ProteOn XPR36 Protein Interaction Array System, Rev B Click to download
5846 Determining the Binding Kinetics of HIV-1 Nucleocapsid Protein to Six Densities of Oligonucleotide Using the ProteOn XPR36 Protein Interaction Array System, Rev A Click to download
5412 Antibody Characterization and Development: ProteOn XPR36 Protein Interaction Array System Application Guide, Rev C Click to download
5540 Screening, Ranking, and Epitope Mapping of Anti-Human IL-9 Supernatants, Rev A Click to download
5820 Rapid Screening and Selection of Optimal Antibody Capturing Agents Using the ProteOn XPR36 Protein Interaction Array System, Rev A Click to download [ Add to Cart (Free) ]
3172 Rapid and Efficient Determination of Kinetic Rate Constants Using the ProteOn XPR36 Protein Interaction Array System, Rev B Click to download
5360 Rapid and Detailed Analysis of Multiple Antigen-Antibody Pairs Using the ProteOn XPR36 Protein Interaction Array System, Rev A Click to download
5367 Rapid Optimization of Immobilization and Binding Conditions for Kinetic Analysis of Protein-Protein Interactions Using the ProteOn XPR36 Protein Interaction Array System, Rev A Click to download
5368 Anaylsis of Multiple Protein-Protein Interactions Using the ProteOn XPR36 Protein Interaction Array System, Rev B Click to download
5358 Mechanisms of Protein-Protein Binding: Double-Mutant Cycle Analysis Using the ProteOn XPR36 System, Rev A Click to download
5821 Guide to Ligand Immobilization Protocol Guide, Rev A Click to download
5822 How to Perform Excluded Volume Correction on the ProteOn XPR36 Protein Interaction System Protocol Guide, Rev C Click to download
5797 Rapid Assay Development and Optimization for Small Molecule Drug Discovery, Rev B Click to download [ Add to Cart (Free) ]
5679 Applications of the ProteOn GLH Sensor Chip: Interactions Between Proteins and Small Molecules, Rev A Click to download [ Add to Cart (Free) ]
5449 Applications of the ProteOn NLC Sensor Chip: Antibody-Antigen, DNA-Protein, and Protein-Protein Interactions, Rev B Click to download [ Add to Cart (Free) ]
5434A ProteOn XPR36 Protein Interaction Array System Folder. (Contains bulletins 3172, 5358, 5360, 5367, 5368, 5390, 5404, 5409, 5410, 5413, 5538, and 5465 DVD, depending on availability) [ Add to Cart (Free) ]
6161 Highly Efficient Lipoparticle Capture and SPR Binding Kinetics of a Membrane Protein Using the ProteOn XPR36 Protein Interaction Array System, Rev A Click to download [ Add to Cart (Free) ]
6254 The ProteOn HTE Sensor Chip: Novel Surface for Stable Capture of Histidine-Tagged Proteins for Protein-Small Molecule Interaction Analysis, Rev A Click to download [ Add to Cart (Free) ]
6449 Novel Liposome-Capture Surface Chemistries to Analyze Drug-Lipid Interaction using the ProteOn XPR36 System, Rev A Click to download
6414 ProteOn XPR36 Experimental Design and Application Guide, Rev A Click to download