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Key Documents

SAE0118

Sigma-Aldrich

TEV Protease, Biotin tagged

recombinant protein, aqueous solution

Synonyma:

TEVp, Tobacco Etch Virus protease

Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen


About This Item

UNSPSC Code:
12352202
NACRES:
NA.54

biological source

microbial (Tobacco Etch virus)

recombinant

expressed in E. coli

assay

≥90%

form

liquid

specific activity

≥10 U/μL

technique(s)

protein purification: suitable

suitability

suitable for additive or modifier in the separation of proteins or peptides

application(s)

life science and biopharma

shipped in

wet ice

storage temp.

−20°C

General description

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:
  • 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.

Unit Definition

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

10 - Combustible liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Sortimentní položky

Proteases for biotinylated tag removal for protein purification workflows with related reagents and technical resources.

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