ProTEV Buffer, 20X【子货号:V602A,包装:1 x 1ml,,运保温度:–20°C】
ProTEV Plus【子货号:V610A,包装:1 x 1,000u,,运保温度:–20°C】
描述:
说明
ProTEV Plus 是基因工程改造的 TEV 蛋白酶,是一个高度特异的蛋白水解酶,在一个七氨基酸序列内部进行切割,可在理想的切割位点对含有七氨基酸序列的融合蛋白进行切割。 ProTEV Plus 蛋白的 N 末端还具有 1 个 HQ 标签,可固定在亲和树脂上,从切割反应中去除。
特点
• 在宽广的pH和温度范围内都有活性:用最适条件切割每个融合蛋白,从而使其保持活力和正确构型。
• HQ标签:切割反应后,可使用基于镍的亲和树脂来方便地去除 ProTEV Plus 。
• 在溶液中直接切割融合蛋白或用亲和树脂固定:ProTEV Plus 在多种实验中都很方便易用。
应用
• 在蛋白纯化后,从融合蛋白中切除亲和标签。
原厂资料:
ProTEV Plus is an improved 48kDa version of the Nla protease from tobacco etch virus (TEV) that has been engineered to be more stable than native TEV protease for prolonged enzymatic activity. It is a highly specific proteolytic enzyme that cleaves within a seven-amino-acid sequence (ENLYFQ(G/S)). ProTEV Plus is active over a wide range of pH values (5.5–8.5) and temperatures (4–30°C). It can be used to cleave protein fusions that have been engineered with the above amino acid sequence at the desired cleavage site. The enzyme is compatible for both in-solution and on-column cleavage reactions. ProTEV Plus also contains an HQ tag (analogous to His tag) located at the N-terminus of the protein, which allows it to be immobilized on Ni-based affinity resins and removed from the cleavage reaction.
Active Over a Wide Range of pH and Temperatures:Cleave individual fusion proteins using optimal conditions to maintain activity and correct conformation.
HQ-Tagged:Convenient removal of ProTEV Plus using Ni-based affinity resins after cleavage.
Specific:Highly specific and active for its seven-amino acid sequence with minimal off-target effects.
Cleaves Fusion Proteins Directly in Solution or Immobilized on Affinity Resins:ProTEV Plus is easy to use in multiple experimental formats.
Applications
Cleavage of affinity tags from fusion proteins after protein purification.
Removal of HaloTag® protein during protein purification/expression of fused proteins of interest.
References
Du, Y., Cai, Y., Hou, S. and Xu, X. (2012) Identification of the hetR recognition sequence upstream ofhetZinAnabaenasp. strain PCC 7120.J. Bacteriol.194, 2297–2306.
Morrow, B.J.et al.(2011) Antistaphylococcal activities of the new fluoroquinolone JNJ-Q2.Antimicrob. Agents Chemother.55, 5512–21.
Ruepp, M.-D.et al.(2010) The 68 kDa subunit of mammalian cleavage factor I interacts with the U7 small nuclear ribonucleoprotein and participates in 3´-end processing of animal histone mRNAs.Nucleic Acids Res.38, 7637–50.
Chen, Y.-C.et al.(2010) Protein arginine methylation facilitates cotranscriptional recruitment of pre-mRNA splicing factors.Mol. Cell. Biol.30, 5245–56.