Reference - Detail
RRC ID | 51638 |
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Author | Fujiwara Y, Yang L, Takaiwa F, Sekikawa K. |
Title | Expression and Purification of Recombinant Mouse Interleukin-4 and -6 from Transgenic Rice Seeds. |
Journal | Mol Biotechnol |
Abstract |
Transgenic rice seed can be utilized as a bioreactor to produce high-value recombinant proteins. Mouse interleukin 4 (mIL-4) and mIL-6 were specifically expressed as secretory proteins in rice endosperm by ligating the N-terminal glutelin B-1 (GluB-1) signal peptide and the C-terminal KDEL endoplasmic reticulum retention signal under control of the endosperm-specific GluB-1 promoter. In the transgenic rice seed, mIL-4 and mIL-6 accumulated in levels up to 0.43 mg/g grain and 0.16 mg/g grain, respectively. The reducing agents and detergents required for extraction from the transgenic rice seeds differed between the two proteins, indicating differences in their intracellular localization within the endosperm cell. Purified mIL-4 and mIL-6 exhibited high activity and very low endotoxin contamination. |
Volume | 58(4) |
Pages | 223-31 |
Published | 2016-4-1 |
DOI | 10.1007/s12033-016-9920-7 |
PII | 10.1007/s12033-016-9920-7 |
PMID | 26876890 |
MeSH | Animals Detergents Interleukin-4 / genetics* Interleukin-4 / isolation & purification* Interleukin-4 / metabolism Interleukin-6 / genetics* Interleukin-6 / isolation & purification* Interleukin-6 / metabolism Mice Oryza / genetics* Oryza / growth & development Plants, Genetically Modified / growth & development Recombinant Proteins / genetics Recombinant Proteins / isolation & purification Recombinant Proteins / metabolism Seeds / genetics* Seeds / metabolism |
IF | 2.022 |
Times Cited | 5 |
Resource | |
Human and Animal Cells | 7-TD-1(RCB1190) |