Protein Arrays

 

Parallel functional protein analysis

 

With E.coli expressed proteins derived from cDNA libraries from four different human tissues (lungcolonT-lymphocytesfoetal brain), our sister company Source BioScience offers one of the largest collection of arrayed proteins for screening experiments.

 

Protein array handbook

 

Proteinarray 1

Search and order

 

For ordering, please contact Sales.

 

Applications

 

  • Target protein identification, using antibodies and sera
  • Functional assays, e.g. phosphorylation, ribosylation, methylation
  • Identification of DNA/RNA binding proteins
  • Identification of protein−protein interactions

 

Product range

 

Source BioScience offers the following 2 Protein Array types as standard, readily available products:

 

  • hEXselect - Human random cDNA Protein Array, redundancy reduced, 24.000 clones - hEXselect protein expression library is derived from human foetal brain and contains 24,000 clones. It comprises full-length as well as shorter cDNA clones in an E.coli expression vector. All clones have been 5' tag sequenced and are fully annotated. The size of the low redundancy collection allows a complete spotting in duplicates onto 1 Protein Array, which saves processing time and hybridisation probe volume. Note that the majority of the clones represent partial proteins including translated 5' UTR sequences, with one third matching to the human proteome (Büssow et al., 2000: A human cDNA library for high-throughput protein expression screening. Genomics. 65(1): 1−8). Protein Arrays are delivered with an accompanying annotation table and respective spotting positions.

 

  • UniPEx - Human in frame cDNA Protein Array Set, redundancy reduced, 15.300 clones / 7390 distinct human proteins - The UniPEx protein expression library consists of 2 Arrays representing clones in 2 different vectors. In total, more than 100,000 sequenced clones from different protein expression libraries (human foetal brain, T-cells, lung, colon) were analysed in depth for their coding potential. After in-frame analysis only clones with a confirmed in-frame ORF were selected and redundancy with respect to clones per gene was minimised (< 3 fold). In total, the 15,300 UniPEx clones are representing 7,390 distinct human proteins. The UniPEx set comes together with an annotation table showing cloneIDs per filter position, geneID, gene description in Excel format, with links to public databases.

 

  • Custom-made Protein Arrays can be generated from subsets of these libraries


 

 

Product details

 

Source BioScience offers a variety of protein expression clone libraries which are also employed to create Protein Arrays. Source BioScience Protein Arrays consist of up to 27,648 spots, which are printed in duplicate (total up to 55,296 protein spots) onto 22 cm x 22 cm PVDF membranes. The expression vector adds a HIS-Tag to each expressed protein. All proteins on the arrays have been verified for expression by detecting this HIS-Tag using an anti-HIS antibody. Protein expression clone collections and the respective individual cDNA clones are available for in-depth follow-up-experiments such as structural genomics.

 

Proteinarray 2

 

Fig.1 Vector Structure of Source BioScience protein expression clones

 

The fabrication of Source BioScience Protein Arrays combines reliable contact printing technology with in situ protein expression directly at the surface of PVDF membranes. Protein synthesis is based on an E. coli based expression system for recombinant proteins. Expressed proteins are extracted and immobilised under denaturing conditions, directly at the PVDF membrane surface. Resulting Source BioScience Protein Arrays mainly consist of almost linear sequence epitopes, ideally suited for epitope mapping, for auto antibody assays, and for antibody cross reactivity screenings

 

Proteinarray 3

 

Fig.2 Overview about Source BioScience's protein array production process and subsequent screening and analysis procedure

 

Reference customers

 

Dr. Derek Murphey
Associate Director 
Centre for Human Proteomics
Royal College of Surgeons in Ireland
123 St Stephen's Green
Dublin 2
Ireland
Tel.: +353 1 402 8518
Fax: +353 1 402 8514
Email
Homepage



Dr. Mark T. Bedford
University of Texas
M.D. A. Cancer Center, Dept.of Carcinogenesis
Smithville, USA
Email
Homepage

 

References proteinarrays

 

2010

 

M. Raab, H. Daxecker, R.J. Edwards, A. Treumann, D. Murphy, N. Moran.
Protein interactions with the platelet integrin alpha(IIb) regulatory motif.
Proteomics (2010) May 18. [Epub ahead of print]

 

E.W. Dervan, H. Chen, S.L. Ho, N. Brummel, J. Schmid, D. Toomey, M. Haralambova, E. Gould, D.M. Wallace, J.H. Prehn, C.J. O'Brien, D. Murphy
Protein macroarray profiling of serum autoantibodies in pseudoexfoliation glaucoma
Invest Ophthalmol Vis Sci (2010) 51(6):2968-75. Epub 2010 Jan 27.

 

D. Murphy, J. Parker, M. Zhou, F.M. Fadlelmola, C. Steidl, A. Karsan, R.D. Gascoyne, H. Chen, D. Banerjee
Constitutively overexpressed 21 kDa protein in Hodgkin lymphoma and aggressive non-Hodgkin lymphomas identified as cytochrome B5b (CYB5B).
Mol Cancer. (2010) 9:14.

 

D.S. Gibson, J. Banha, D. Penque, L. Costa, T.P. Conrads, D.J. Cahill, J.K. O'Brien and M.E. Rooney
Diagnostic and prognostic biomarker discovery strategies for autoimmune disorders.
Journal of Proteomics (2010) 73, 1045-1060

 

D.J. O'Connell, M.C. Bauer, J. O'Brien, W.M. Johnson, C.A. Divizio, S.L. O'Kane, T. Berggård, A. Merino, K.S. Åkerfeldt, S. Linse and D.J. Cahill
Integrated protein array screening and high throughput validation of 70 novel neural calmodulin binding proteins.
Mol Cell Proteomics (2010) Jan 12. [Epub ahead of print]
Article

 

G. Kijanka, S. Hector, E.W. Kay, F. Murray, R. Cummins, D. Murphy, B.D. MacCraith, J.H.M. Prehn, D Kenny
Human IgG antibody profiles differentiate between symptomatic patients with and without colorectal cancer.
Gut (2010) 59: 69-78
Article

 

E. Kowenz-Leutz, O. Pless, G. Dittmar, M. Knoblich and A. Leutz
Crosstalk between C/EBPß phosphorylation, arginine methylation, and SWI/SNF/Mediator implies an indexing transcription factor code.
The EMBO Journal (2010) 29, 1105-1115

Article

 

2009

 

G. Kijanka, S. IpCho, S. Baars, H. Chen, K. Hadley, A. Beveridge, E. Gould and D. Murphy
Rapid characterisation of binding specificity and cross-reactivity of antibodies using recombinant human protein arrays.
Journal of Immunological Methods (2009) 340, 132-137
Article

 

G. Kijanka, R. Barry, H. Chen, E. Gould, S.K. Seidlits, J. Schmid, M. Morgan, D.Y. Mason, J. Cordell and D. Murphy
Defining the molecular target of an antibody derived from nuclear extract of Jurkat cells using protein arrays.
Analytical Biochemistry (2009) 395 , 119-124
Article

 

G. Kijanka and D. Murphy
Protein arrays as tools for serum autoantibody marker discovery in cancer.
Journal of Proteomics (2009) 72, 936 - 944
Article

 

 

2008

 

O. Pless, E. Kowenz-Leutz, M. Knoblich, J. Lausen, M. Beyermann, M.J. Walsh and A. Leutz
G9a-mediated Lysine Methylation Alters the Function of CCAAT/Enhancer-binding Protein-ß*.
Journal of Biological Chemistry (2008) 283 (39), 26357-26363
Article

 

2007

 

W.-H. Yang and D.B. Bloch
Probing the mRNA processing body using protein macroarrays and ''autoantigenomics''
RNA (2007), 13:704-712.
Article

 

Before 2007

 

 

Cepok S, Zhou D, Srivastava R, Nessler S, Stei S, Büssow K, Sommer N, Hemmer B
Identification of Epstein-Barr virus proteins as putative targets of the immune response in multiple sclerosis.
J Clin Invest. (2005) 115(5):1352-60
Article

 

G. Grelle, S. Kostka, A. Otto, B. Kersten, K. Genser, E. Müller, S. Wälter, A. Böddrich, U. Stelzl, C. Hänig,  R. Volkmer-Engert, C. Landgraf, S. Alberti, J. Höhfeld, M. Strödicke, and E. Wanker
Identification of VCP/p97, CHIP and amphiphysin II interaction partners using membrane-based human proteome arrays.
MCP (2005) 10.1074/mcp.M500198−MCP200
Abstract

 

K. de Graaf, P. Hekerman, O. Spelten, A. Herrmann, L. C. Packman, K. Bussow. G. Muller-Newen, W. Becker
Characterisation of cyclin L2, a novel cyclin with an arginine/serine-rich domain: phosphorylation by DYRK1A and colocalisation with splicing factors.
J Biol Chem. (2004) 279(6):4612−24
Abstract

 

K. Büssow, C. Quedenau, V. Sievert, J. Tischler, C. Scheich, H. Seitz, B. Hieke, F.H. Niesen, F. Gotz, U. Harttig, H. Lehrach
A catalog of human cDNA expression clones and its application to structural genomics.
Genome Biol. 2004 Aug; 5(9):R71
Abstract

 

U. Radelof, C.Hüls, B. Korn, J. Maurer
Proteinarrays und rekombinante Proteine für die Proteinanalyse.
Laborwelt 2004. 5: p.35
Article

 

C. Maercker
Protein-Chips in der Genomforschung.
Laborwelt 2004. 4: p.12−15
Article

 

J. Lee and M.T. Bedford
PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays.
EMBO Reports 2002. 3(3): p.268−73
Abstract

 

U. Mahlknecht, O.G. Ottmann, and D. Hoelzer
Far-Western based protein-protein interaction screening of high-density protein filter arrays.
Journal of Biotechnology 2001. 88(2): p. 89−94
Abstract

K. Büssow, E. Nordhoff, C. Lübbert, H. Lehrach, and G. Walter
A human cDNA library for high-throughput protein expression screening.
Genomics 2000.65(1): 1−8
Abstract

 

L. J. Holt, K. Büssow, G. Walter, and I. M. Tomlinson
By-passing selection: direct screening for antibodyantigen interactions using protein arrays.
Nucleic Acids Research 2000. 28(15): p. E72
Abstract

 

K. Büssow, D. Cahill, W. Nietfeld, D. Bancroft, E. Scherzinger, H. Lehrach, and G. Walter
A method for global protein expression and antibody screening on high-density filters of an arrayed cDNA library.
Nucleic Acids Research 1998. 26(21): p. 5007−5008 
Abstract

 

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