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由来生物
microbial (Tobacco Etch virus)
リコンビナント
expressed in E. coli
アッセイ
≥90%
形状
liquid
比活性
≥10 U/μL
テクニック
protein purification: suitable
適合性
suitable for additive or modifier in the separation of proteins or peptides
アプリケーション
life science and biopharma
輸送温度
wet ice
保管温度
−20°C
詳細
TEV protease is a highly sequence specific serine protease from Tobacco Etch Virus. Due to its high specificity, TEV protease is popular for cleavage of recombinant fusion proteins. The optimal sequence for TEV protease cleavage is ENLYFQ\S is, however, TEV protease is active on a range of substrates with a consensus sequence of EXLYFΦQ\ϕ where X is any residue, Φ is any large or medium hydrophobic residue and ϕ is any small hydrophobic or polar residue (i.e. glycine, serine, alanine, valine, cysteine). Fusion tag removal in-vitro is the most popular usage of TEV protease.
This biotin-tagged TEV protease is expressed in E.coli. Our Biotin-tagged TEV protease does not carry any purification tag other than biotin and is designed to be used for on-column cleavage of fusion proteins containing a TEV protease recognition sequence. This method specifically cleaves the protein of interest from a column-bound fusion protein, leaving the purification domain or tag bound to the affinity column (e.g. Ni-NTA column) and eluting only the protein of interest.
This method is advantageous to post-elution cleavage for several reasons:
After cleavage, the biotinylated TEV protease can be removed with any avidin-conjugated or streptavidin-conjugated beads.
Biotinylation of this product is done enzymatically with no effect on its proteolytic activity. It has no other protein purification tags. The product is supplied at a concentration of =10 U/μl in an aqueous buffer containing 20 mM Tris HCl, pH 7.5, 50 mM Sodium Chloride, 1 mM TCEP, 1 mM EDTA and 50% (V/V) glycerol.
This biotin-tagged TEV protease is expressed in E.coli. Our Biotin-tagged TEV protease does not carry any purification tag other than biotin and is designed to be used for on-column cleavage of fusion proteins containing a TEV protease recognition sequence. This method specifically cleaves the protein of interest from a column-bound fusion protein, leaving the purification domain or tag bound to the affinity column (e.g. Ni-NTA column) and eluting only the protein of interest.
This method is advantageous to post-elution cleavage for several reasons:
- It eliminates most of the impurities normally associated with affinity purification.
- It allows much gentler elution conditions, with an added flexibility in the composition of the elution buffer. This can help to prevent protein aggregation and inactivation.
After cleavage, the biotinylated TEV protease can be removed with any avidin-conjugated or streptavidin-conjugated beads.
Biotinylation of this product is done enzymatically with no effect on its proteolytic activity. It has no other protein purification tags. The product is supplied at a concentration of =10 U/μl in an aqueous buffer containing 20 mM Tris HCl, pH 7.5, 50 mM Sodium Chloride, 1 mM TCEP, 1 mM EDTA and 50% (V/V) glycerol.
単位の定義
One unit of TEV protease cleaves >85% of 3 μg of control substrate in one hour at pH 8.0 at 30 °C
保管分類コード
10 - Combustible liquids
WGK
WGK 2
引火点(°F)
Not applicable
引火点(℃)
Not applicable
適用法令
試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。
Jan Code
SAE0118-5KU:
SAE0118A-BULK:
SAE0118-BULK:
SAE0118-VAR:
SAE0118-5KU-PW:
試験成績書（COA）
製品のロット番号・バッチ番号を入力して、試験成績書（COA） を検索できます。ロット番号・バッチ番号は、製品ラベルに「Lot」または「Batch」に続いて記載されています。
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