Ezpression of recombinant mouse yhymine DNA glycosylase (TDG) and production of its polyclonal antiserum
The wild-type mouse thymine DNA glycosylase (mTDG) protein was expressed as a His-tag fusion protein in Escherichia coli. Expressional protein was purified by Ni2+ affinity and molecular sieve columns. Purified TDG exhibited as a homogenous band corresponding to the molecular weight of 64 kDa. Immunization of rabbits against the purified TDG protein was allowed the production of high titre polyclonal antiserum. This new polyclonal antibody could recognize recombinant TDG protein in Western blot.
TDG his-tag fusion protein polyclonal antibody
Li Shi-Ying Tang Bo Lan Yan Hua Zi-Chun
The State Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, Nanjing, 210093, China
国际会议
International Symposium on Medical and Pharmaceutical Biotechnology(医药生物技术国际研讨会)
南京
英文
87-89
2009-04-27（万方平台首次上网日期，不代表论文的发表时间）