EXPRESSION AND PURIFICATION OF RECOMBINANT T4 DNA LIGASE IN E. COLI | Zendy

Duong Long Duy | Zendy; Duc Van Luong | Zendy; Hieu Thi Phuong Nguyen | Zendy; Thanh Hoa Tran | Zendy; Thao Thi Phuong Dang | Zendy; Thuoc Linh Tran | Zendy

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EXPRESSION AND PURIFICATION OF RECOMBINANT T4 DNA LIGASE IN E. COLI

Author(s) -

Duong Long Duy,

Duc Van Luong,

Hieu Thi Phuong Nguyen,

Thanh Hoa Tran,

Thao Thi Phuong Dang,

Thuoc Linh Tran

Publication year - 2011

Publication title -

science and technology development journal

Language(s) - English

Resource type - Journals

ISSN - 1859-0128

DOI - 10.32508/stdj.v14i3.1991

Subject(s) - dna ligase , recombinant dna , microbiology and biotechnology , lac operon , plasmid , dna , biology , western blot , escherichia coli , dna ligases , myc tag , affinity chromatography , chemistry , gene , biochemistry , enzyme , fusion protein

In this study, we report results on the expression and purification of recombinant T4 DNA ligase. Plasmid pET16b-T4Dnl contains the gp30 gene which encodes for T4 DNA ligase. The target protein is fused with 10xHis tag to facilitate the purification and recovery. pET16b-T4Dnl was transformed into E. coli BL21(DE3) and then induced the expression of 10xHis-T4Dnl by IPTG. The recombinant protein was purified by Ni-NTA chromatography and confirmed by SDS-PAGE and Western blot. The activity of purified protein was tested by joining DNA λ/HindIII.

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