Soluble Expression Of Recombinant Human Interferon Alpha 2a Fusion Protein In Escherichia coli
Arizah Kusumawati, Adi Santoso, Maksum Radji
Abstract
Arizah Kusumawati, Adi Santoso, Maksum Radji
Abstract
BL21(DE3). Obtained transformant clones were cultured and induced by addition of IPTG 1 mM to produce the expression of recombinant human IFN α2a proteins. As result of isolation process, recombinant protein of human IFN α2a are collected in fused protein thus can simplify the detection and purification method. The proteins are characterized by the SDS PAGE method followed by western blot. The results show that the recombinant human IFN alpha 2a protein bands are exactly 36 kDa. The maximum expression results were obtained at 37⁰C with 5 hours incubation after induction process. Recombinant human IFN α2a fusion proteins were expressed predominantly as a soluble form in the cytoplasm cells.
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BL21(DE3). Obtained transformant clones were cultured and induced by addition of IPTG 1 mM to produce the expression of recombinant human IFN α2a proteins. As result of isolation process, recombinant protein of human IFN α2a are collected in fused protein thus can simplify the detection and purification method. The proteins are characterized by the SDS PAGE method followed by western blot. The results show that the recombinant human IFN alpha 2a protein bands are exactly 36 kDa. The maximum expression results were obtained at 37⁰C with 5 hours incubation after induction process. Recombinant human IFN α2a fusion proteins were expressed predominantly as a soluble form in the cytoplasm cells.
Key concepts: Recombinant DNA, Fusion protein, lac operon, Molecular biology, Escherichia coli, Western blot, Myc-tag, Protein A/G