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SAE0110

Sigma-Aldrich

HRV-3C Protease, Biotin tagged

Recombinant protein, 0.8-1.2 mg/mL, aqueous solution

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Synonym(s):
Human Rhinovirus 3C Protease, Levlfqgp site protease, PreScission Protease

recombinant

expressed in E. coli

form

aqueous solution

mol wt

22 kDa

concentration

0.8-1.2 mg/mL

shipped in

dry ice

storage temp.

−20°C

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This Item
SAE0045SAB5700598SAE0118
HRV-3C Protease. N-Terminal His tagged recombinant protein, aqueous solution, 0.8-1.2 mg/mL

Sigma-Aldrich

SAE0045

HRV-3C Protease.

form

aqueous solution

form

aqueous solution

form

liquid

form

-

mol wt

22 kDa

mol wt

21 kDa

mol wt

36.9 kDa

mol wt

-

concentration

0.8-1.2 mg/mL

concentration

0.8-1.2 mg/mL

concentration

-

concentration

-

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

shipped in

wet ice

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−70°C

storage temp.

−20°C

General description

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:
  • 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.

Preparation Note

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.

Legal Information

Trizma is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Michael D Scholle et al.
SLAS discovery : advancing life sciences R & D, 26(8), 974-983 (2021-06-22)
Affinity selection mass spectrometry (ASMS) has emerged as a powerful high-throughput screening tool used in drug discovery to identify novel ligands against therapeutic targets. This report describes the first high-throughput screen using a novel self-assembled monolayer desorption ionization (SAMDI)-ASMS methodology
Cheng Liu et al.
Antiviral research, 187, 105020-105020 (2021-01-31)
The 3-chymotrypsin-like cysteine protease (3CLpro) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is considered a major target for the discovery of direct antiviral agents. We previously reported the evaluation of SARS-CoV-2 3CLpro inhibitors in a novel self-assembled monolayer desorption
Margot A Cousin et al.
Nature genetics, 53(7), 1006-1021 (2021-07-03)
SPTBN1 encodes βII-spectrin, the ubiquitously expressed β-spectrin that forms micrometer-scale networks associated with plasma membranes. Mice deficient in neuronal βII-spectrin have defects in cortical organization, developmental delay and behavioral deficiencies. These phenotypes, while less severe, are observed in haploinsufficient animals
Alon Wellner et al.
Nature chemical biology, 17(10), 1057-1064 (2021-06-26)
The predominant approach for antibody generation remains animal immunization, which can yield exceptionally selective and potent antibody clones owing to the powerful evolutionary process of somatic hypermutation. However, animal immunization is inherently slow, not always accessible and poorly compatible with
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The initiation of DNA replication involves cell cycle-dependent assembly and disassembly of protein complexes, including the origin recognition complex (ORC) and CDC6 AAA+ ATPases. We report that multiple short linear protein motifs (SLiMs) within intrinsically disordered regions (IDRs) in ORC1

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