추천 제품
생물학적 소스
microbial (Tobacco Etch virus)
재조합
expressed in E. coli
분석
≥90%
형태
liquid
특이 활성도
≥10 U/μL
기술
protein purification: suitable
적합성
suitable for additive or modifier in the separation of proteins or peptides
응용 분야
life science and biopharma
배송 상태
wet ice
저장 온도
−20°C
일반 설명
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.
단위 정의
One unit of TEV protease cleaves >85% of 3 μg of control substrate in one hour at pH 8.0 at 30 °C
Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
문서
Proteases for biotinylated tag removal for protein purification workflows with related reagents and technical resources.
자사의 과학자팀은 생명 과학, 재료 과학, 화학 합성, 크로마토그래피, 분석 및 기타 많은 영역을 포함한 모든 과학 분야에 경험이 있습니다..
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