Author: Muhammad, Azharuddin; Toufeeq, Shahzad; Yu, Hai-Zhong; Wang, Jie; Zhang, Shang-Zhi; Li, Bing; Li, Zhen; Yang, Li-Ang; Hu, Pei; Ma, Yan; Xu, Jia-Ping
Title: Molecular Characterization of Two Mitogen-Activated Protein Kinases: p38 MAP Kinase and Ribosomal S6 Kinase From Bombyx mori (Lepidoptera: Bombycidae), and Insight Into Their Roles in Response to BmNPV Infection Document date: 2019_2_2
ID: 2s3x6sj8_31
Snippet: To analyze the physiological function of Bmp38 and BmS6K proteins, recombinant His-tagged Bmp38 and BmS6K were expressed using prokaryotic expression system. The recombinant proteins (Bmp38 and BmS6K) were successfully expressed and detected by SDS-PAGE with molecular mass of approximately 35kDa and 30kDa, respectively (Fig. 4A-C) . The recombinant proteins were purified under denaturing conditions by affinity chromatography using Ni-NTA column (.....
Document: To analyze the physiological function of Bmp38 and BmS6K proteins, recombinant His-tagged Bmp38 and BmS6K were expressed using prokaryotic expression system. The recombinant proteins (Bmp38 and BmS6K) were successfully expressed and detected by SDS-PAGE with molecular mass of approximately 35kDa and 30kDa, respectively (Fig. 4A-C) . The recombinant proteins were purified under denaturing conditions by affinity chromatography using Ni-NTA column (Fig. 4B-D) , and recombinant proteins were confirmed through western blotting (Fig. 5) . For preparation of antibody, purified proteins were utilized. The titer of antibody was 1:60,000 approximately as per ELISA determination.
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