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231223s2010 xx |||||o 00| ||eng c |
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|a 10.1021/la904829y
|2 doi
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|a pubmed25n0657.xml
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|a (DE-627)NLM197139094
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|a (NLM)20369837
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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1 |
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|a Engin, Sinem
|e verfasserin
|4 aut
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|a Benzylguanine thiol self-assembled monolayers for the immobilization of SNAP-tag proteins on microcontact-printed surface structures
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|c 2010
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 02.08.2010
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|a Date Revised 27.04.2010
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|a published: Print
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|a Citation Status MEDLINE
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|a The site-selective, oriented, covalent immobilization of proteins on surfaces is an important issue in the establishment of microarrays, biosensors, biocatalysts, and cell assays. Here we describe the preparation of self-assembled monolayers consisting of benzylguanine thiols (BGT) to which SNAP-tag fusion proteins can be covalently linked. The SNAP-tag, a modified O(6)-alkylguanine-DNA alkyltransferase (AGT), reacts with the headgroup of BGT and becomes covalently bound upon the release of guanine. Bacterially produced recombinant His-tag-SNAP-tag-GFP was used to demonstrate the site-specific immobilization on BGT surface patterns created by microcontact printing (microCP). With this versatile method, any SNAP-tag protein can be coupled to a surface
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Enzymes, Immobilized
|2 NLM
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|a Guanidines
|2 NLM
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|a Recombinant Fusion Proteins
|2 NLM
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|a O(6)-Methylguanine-DNA Methyltransferase
|2 NLM
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|a EC 2.1.1.63
|2 NLM
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1 |
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|a Trouillet, Vanessa
|e verfasserin
|4 aut
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|a Franz, Clemens M
|e verfasserin
|4 aut
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1 |
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|a Welle, Alexander
|e verfasserin
|4 aut
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|a Bruns, Michael
|e verfasserin
|4 aut
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|a Wedlich, Doris
|e verfasserin
|4 aut
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1991
|g 26(2010), 9 vom: 04. Mai, Seite 6097-101
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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|g volume:26
|g year:2010
|g number:9
|g day:04
|g month:05
|g pages:6097-101
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|u http://dx.doi.org/10.1021/la904829y
|3 Volltext
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