SAE0118
TEV Protease, Biotin tagged
recombinant protein, aqueous solution
Synonyma:
TEVp, Tobacco Etch Virus protease
About This Item
Doporučené produkty
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
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
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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