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Published on: October 16, 2014
[Prokaryotic expression and purification of recombinant rat HMGB1-A]
Linquan He1, Jiayun Liu2, Yuanli Qu3
1Department of Traditional Chinese Medicine, Military Health Team, Kelamayi Detachment, Xinjiang Corps of Armed Police Force, Kelamayi 834000, China.
Abstract:
Objective To obtain the recombinant A-domain of high mobility group box 1 (HMGB1-A) protein. Methods Using genetic engineering techniques, we cloned and recombined rat HMGB1-A gene. Using prokaryotic expression technique, we expressed and purified the recombinant rat HMGB1-A protein, which was verified by Western blotting. Results Agarose gel electrophoresis analysis showed that HMGB1-A cassette gene size was about 250 bp; double digestion for identifying the recombinant clone pUC-A showed that the product size was about 3000 bp, 250 bp; PCR for identifying the recombinant clone pGEX-A showed that the product size was about 250 bp. SDS-PAGE revealed that the product size was about 36 000, which was consistent with the expectation. Conclusion The recombinant rat HMGB1-A was successfully expressed and purified.
