The ProteOn XPR36™ Array System-High Throughput Kinetic Binding Analysis of Biomolecular Interactions

被引:8
作者
Bravman, Tsafrir [2 ]
Bronner, Vered [2 ]
Nahshol, Oded [2 ]
Schreiber, Gideon [1 ]
机构
[1] Weizmann Inst Sci, Dept Biol Chem, IL-76100 Rehovot, Israel
[2] Biorad Technol Inc, Technion Israel Inst Technol, IL-32000 Haifa, Israel
关键词
Protein-protein interaction; Biosensors; Kinetics;
D O I
10.1007/s12195-008-0036-4
中图分类号
Q813 [细胞工程];
学科分类号
摘要
Surface plasmon resonance (SPR) technology is a central, widely used tool for kinetic studies of interactions between unlabeled biomolecules in real time. The ProteOn XPR36 protein interaction array system possesses all the qualities of high-level SPR biosensing technology combined with high-throughput and multiplexing capabilities. This system is based on the built-in orientation controlled multi-channel module of the ProteOn XPR36 system, which allows parallel measurement of multiple binding interactions between as many as six protein pairs. This kind of multiplexing is done efficiently on the ProteOn XPR36 system using the innovative technique of One-shot Kinetics (TM), which allows simultaneous monitoring of multiple protein pair interactions. Here we demonstrate the capabilities of the ProteOn XPR36 for the measurements of a wide range of biomolecules interactions including proteins, DNA oligos, small molecules and antibodies and discuss its optimal mode of use.
引用
收藏
页码:216 / 228
页数:13
相关论文
共 31 条
  • [1] Determining kinetics and affinities of protein interactions using a parallel real-time label-free biosensor, the Octet
    Abdiche, Yasmina
    Malashock, Dan
    Pinkerton, Alanna
    Pons, Jaurne
    [J]. ANALYTICAL BIOCHEMISTRY, 2008, 377 (02) : 209 - 217
  • [2] Probing the binding mechanism and affinity of tanezumab, a recombinant humanized anti-NGF monoclonal antibody, using a repertoire of biosensors
    Abdiche, Yasmina Noubia
    Malashock, Dan Stephen
    Pons, Jaume
    [J]. PROTEIN SCIENCE, 2008, 17 (08) : 1326 - 1335
  • [3] Repressor assembly at trp binding sites is dependent on the identity of the intervening dinucleotide between the binding half sites
    BareketSamish, A
    Cohen, I
    Haran, TE
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1997, 267 (01) : 103 - 117
  • [4] Exploring "one-shot" kinetics and small molecule analysis using the ProteOn XPR36 array biosensor
    Bravman, Tsafrir
    Bronner, Vered
    Lavie, Kobi
    Notcovich, Ariel
    Papalia, Giuseppe A.
    Myszka, David G.
    [J]. ANALYTICAL BIOCHEMISTRY, 2006, 358 (02) : 281 - 288
  • [5] Production and characterization of mouse monoclonal antibodies reactive to Chikungunya envelope E2 glycoprotein
    Brehin, Anne-Claire
    Rubrecht, Laetitia
    Navarro-Sanchez, Martha Erika
    Marechal, Valerie
    Frenkiel, Marie-Pascale
    Lapalud, Priscilla
    Laurie, Daniel
    Sall, Amadou Alpha
    Despres, Philippe
    [J]. VIROLOGY, 2008, 371 (01) : 185 - 195
  • [6] Buijs Jos, 2005, Briefings in Functional Genomics & Proteomics, V4, P39, DOI 10.1093/bfgp/4.1.39
  • [7] Kinetic screening of antibodies from crude hybridoma samples using Biacore
    Canziani, GA
    Klakamp, S
    Myszka, DG
    [J]. ANALYTICAL BIOCHEMISTRY, 2004, 325 (02) : 301 - 307
  • [8] CAREY J, 1991, J BIOL CHEM, V266, P24509
  • [9] The bacterial flagellar switch complex is getting more complex
    Cohen-Ben-Lulu, Galit N.
    Francis, Noreen R.
    Shimoni, Eyal
    Noy, Dror
    Davidov, Yaacov
    Prasad, Krishna
    Sagi, Yael
    Cecchini, Gary
    Johnstone, Rose M.
    Eisenbach, Michael
    [J]. EMBO JOURNAL, 2008, 27 (07) : 1134 - 1144
  • [10] Label-free screening of bio-molecular interactions
    Cooper, MA
    [J]. ANALYTICAL AND BIOANALYTICAL CHEMISTRY, 2003, 377 (05) : 834 - 842