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 Expression and Purification of Full-length CYP26 B1 and Spliced CYP26 B1
Örebro University, School of Science and Technology.
2009 (English)Independent thesis Advanced level (degree of Master (Two Years)), 20 credits / 30 HE creditsStudent thesis
Abstract [en]

The goal of this project is to express both the normal CYP26 B1 and the spliced CYP26 B1 from human in Escherichia coli (E.coli) cells for further crystallization. This will be achieved by cloning in the DNA fragments into the Champion pET SUMO vector that is later transformed into E.coli cells. The CYP26 B1 contains a hydrophobic helix at the N-terminal of the protein, making both protein expression and crystallization difficult. Two variants of both full-length CYP26 B1 and the spliced variant will therefore be made, one with the trans-membrane helix present and one without the helix. The SUMO-vector will produce a fusion protein that will make CYP26 B1 more hydrophilic and improve the purification of the two proteins.

Place, publisher, year, edition, pages
2009. , 36 p.
National Category
Cell and Molecular Biology
Identifiers
URN: urn:nbn:se:oru:diva-7394ISRN: ORU-NAT/KEM-AS-2009/0001-SEOAI: oai:DiVA.org:oru-7394DiVA: diva2:225480
Presentation
(English)
Uppsok

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Examiners
Available from: 2009-06-29 Created: 2009-06-29 Last updated: 2009-06-29Bibliographically approved

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