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- KLSW
- 美国 addgene
- KL-ZL-0028
- 2025年10月11日
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- 详细信息
- 技术资料
- 保存条件：
负20度
- 保质期：
2年
- 英文名：
pMal-c5X
- 库存：
100
- 供应商：
kelei-bio
- 规格：
20μl
基本信息
启动子: Tac
复制子: ColE1 ori
终止子: rrnB T1 terminator
质粒分类: 大肠杆菌载体；pMal系列表达质粒
质粒大小: 5677bp
原核抗性: 氨苄青霉素Amp
克隆菌株: DH5α
培养条件: 37℃，有氧，LB
表达宿主: BL21(DE3)
诱导方式: IPTG或乳糖及其类似物
质粒简介
The vector pMAL-c5X is designed to produce maltose-binding protein (MBP) fusions, where the protein of interest can be cleaved from MBP with the specific protease Factor Xa . MBP fusions made with this vector are expressed cytoplasmically. The MBP has been engineered for tighter binding to amylose resin. A gene or open reading frame is inserted into a restriction site of the vector polylinker, in the same translational reading frame as the malE gene (encoding maltose-binding protein). The fusion protein thus produced can be purified by amylose affinity chromatography. The sequence coding for the four amino acids Ile-Glu-Gly-Arg is present just upstream of the XmnI site. This allows the protein of interest to be cleaved from maltose-binding protein with the specific protease Factor Xa. Fragments inserted in the XmnI site (cleaves GAAGG↓ATTTC) will produce a fusion protein that, after Factor Xa cleavage, contains no vector-derived residues on the protein of interest.
启动子: Tac
复制子: ColE1 ori
终止子: rrnB T1 terminator
质粒分类: 大肠杆菌载体；pMal系列表达质粒
质粒大小: 5677bp
原核抗性: 氨苄青霉素Amp
克隆菌株: DH5α
培养条件: 37℃，有氧，LB
表达宿主: BL21(DE3)
诱导方式: IPTG或乳糖及其类似物
质粒简介
The vector pMAL-c5X is designed to produce maltose-binding protein (MBP) fusions, where the protein of interest can be cleaved from MBP with the specific protease Factor Xa . MBP fusions made with this vector are expressed cytoplasmically. The MBP has been engineered for tighter binding to amylose resin. A gene or open reading frame is inserted into a restriction site of the vector polylinker, in the same translational reading frame as the malE gene (encoding maltose-binding protein). The fusion protein thus produced can be purified by amylose affinity chromatography. The sequence coding for the four amino acids Ile-Glu-Gly-Arg is present just upstream of the XmnI site. This allows the protein of interest to be cleaved from maltose-binding protein with the specific protease Factor Xa. Fragments inserted in the XmnI site (cleaves GAAGG↓ATTTC) will produce a fusion protein that, after Factor Xa cleavage, contains no vector-derived residues on the protein of interest.
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pMal-c5X质粒
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