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|Title:||Expression, 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.
Gomes, M. E.
Neves, N. M.
Reis, R. L.
|Publisher:||Mary Ann Liebert Inc.|
|Journal:||Tissue 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. [...]|
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