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生物源
human (human Rhinovirus Type 14)
重組細胞
expressed in E. coli
化驗
≥90%
形狀
aqueous solution
比活性
≥5000 U/mg
分子量
22 kDa
濃度
0.8-1.2 mg/mL
技術
protein purification: suitable
適合性
suitable for protein modification
應用
life science and biopharma
運輸包裝
dry ice
儲存溫度
−20°C
一般說明
HRV-3C protease from human rhinovirus type 14 is a protease that specifically cleaves within an eight-residue recognition sequence.This sequence is: Leu-Glu-Val-Leu-Phe-Gln-Gly-Pro.Proteolytic cleavage occurs between the Gln and Gly residues. The HRV-3C protease is useful for cleaving recombinant proteins that are expressed as fusion proteins with this sequence between the carrier domain and the protein of interest.
This biotinylated HRV-3C protease is intended for on-column cleavage of fusion proteins with an HRV-3C cleavage site. It specifically cleaves the protein of interest from a column-bound fusion protein, leaving the fusion domain or tag bound to the affinity column (e.g. Ni-NTA column) and eluting only the protein of interest. This method is advantageous over post-elution cleavage for several reasons:
After cleavage, the protease can be removed with any avidin-conjugated or streptavidin-conjugated beads. This product has been enzymatically biotinylated with no effect on its proteolytic activity. It has no additional protein purification tags. The product is supplied in aqueous buffer (0.8–1.2 mg/mL) with 20 mM Trizma®-HCl, pH 8.0, 200 mM NaCl, 1 mM TCEP, and 50% (v/v) glycerol.
This biotinylated HRV-3C protease is intended for on-column cleavage of fusion proteins with an HRV-3C cleavage site. It specifically cleaves the protein of interest from a column-bound fusion protein, leaving the fusion domain or tag bound to the affinity column (e.g. Ni-NTA column) and eluting only the protein of interest. This method is advantageous over post-elution cleavage for several reasons:
- It eliminates most impurities normally associated with purification on Ni-chelating columns.
- It allows gentler elution conditions, with added flexibility in the elution buffer composition. This can mitigate protein aggregation and inactivation.
After cleavage, the protease can be removed with any avidin-conjugated or streptavidin-conjugated beads. This product has been enzymatically biotinylated with no effect on its proteolytic activity. It has no additional protein purification tags. The product is supplied in aqueous buffer (0.8–1.2 mg/mL) with 20 mM Trizma®-HCl, pH 8.0, 200 mM NaCl, 1 mM TCEP, and 50% (v/v) glycerol.
準備報告
The product is supplied in aqueous buffer (0.8–1.2 mg/mL) containing 20 mM Trizma®-HCl, pH 8.0, 200 mM NaCl, 1 mM TCEP, and 50% (v/v) glycerol.
法律資訊
Trizma is a registered trademark of Merck KGaA, Darmstadt, Germany
儲存類別代碼
10 - Combustible liquids
水污染物質分類（WGK）
WGK 2
閃點（°F）
Not applicable
閃點（°C）
Not applicable
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商品
Proteases for biotinylated tag removal for protein purification workflows with related reagents and technical resources.
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