Purification of a recombinant polyhistidine-tagged glucosyltransferase using immobilized metal-affinity chromatography (IMAC)

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DOIResolve DOI: http://doi.org/10.1007/978-1-4939-3393-8_9
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EditorSearch for: Arthur Germano, Fett-Neto
TypeArticle
Journal titleBiotechnology of Plant Secondary Metabolism: Methods and Protocols
Series titleMethods in Molecular Biology; no. 1405
ISSN1064-3745
ISBN978-1-4939-3391-4
978-1-4939-3393-8
Pages9107
SubjectIMAC; His-tagged protein; Glucosyltransferase; Recombinant; Purification
AbstractShort peptide tags genetically fused to recombinant proteins have been widely used to facilitate detection or purification without the need to develop specific procedures. In general, an ideal affinity tag would allow the efficient purification of tagged proteins in high yield, without affecting its function. Here, we describe the purification steps to purify a recombinant polyhistidine-tagged glucosyltransferase from Centella asiatica using immobilized metal affinity chromatography.
Publication date
PublisherSpringer
LanguageEnglish
AffiliationAquatic and Crop Resource Development; National Research Council Canada
Peer reviewedYes
NPARC number23000699
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Record identifier5b0c1e70-e25c-4cb5-9cc9-1a18db65e5e5
Record created2016-08-25
Record modified2016-08-25
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