Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/59165

TitleExpression, purification and bioactivity of recombinant human bone morphogenetic protein-4,-9,-10,-11 and-14 produced in Escherichia coli for tissue engineering applications
Author(s)Bessa, P. C.
Cerqueira, M. T.
Rada, Tommaso
Gomes, M. E.
Neves, N. M.
Casal, Margarida
Reis, R. L.
Issue date2008
PublisherMary Ann Liebert Inc.
JournalTissue Engineering. Part A
Abstract(s)[Excerpt] Bone morphogenetic proteins (BMPs) are cytokines from the TGFb superfamily, with important roles during embryonic development and in inducing bone and cartilage in the adult body. In this contribution, we report the expression of recombinant human BMP-4, BMP-9, BMP-10, BMP-11 (or growth differentiation factor-11, GDF-11) and BMP-14 (GDF-5), using Escherichia coli pET-25b expression system. The BMPs were purified by affinity chromatography and its bioactivity accessed in C2C12 cell line, by screening the expression of osteogenic markers with RT-PCR. [...]
TypeAbstract
URIhttp://hdl.handle.net/1822/59165
ISSN1937-3341
Peer-Reviewedyes
AccessOpen access
Appears in Collections:3B’s - Resumos em livros de atas de conferências - indexados no ISI Web of Science

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