SAE0110
HRV-3C Protease, Biotin tagged
Recombinant protein, 0.8-1.2 mg/mL, aqueous solution
Synonym(s):
Human Rhinovirus 3C Protease, Levlfqgp site protease, PreScission Protease
Sign In to View Organizational & Contract Pricing.
Select a Size
About This Item
NACRES:
NA.54
UNSPSC Code:
12352202
Specific activity:
≥5000 U/mg
Assay:
≥90%
Biological source:
human (human Rhinovirus Type 14)
Recombinant:
expressed in E. coli
Concentration:
0.8-1.2 mg/mL
biological source
human (human Rhinovirus Type 14)
recombinant
expressed in E. coli
assay
≥90%
form
aqueous solution
specific activity
≥5000 U/mg
mol wt
22 kDa
concentration
0.8-1.2 mg/mL
technique(s)
protein purification: suitable
suitability
suitable for protein modification
application(s)
life science and biopharma
shipped in
dry ice
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:
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.
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
10 - Combustible liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Dual inhibition of SARS-CoV-2 and human rhinovirus with protease inhibitors in clinical development.
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
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
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
Manzar Hossain et al.
Molecular cell, 81(9), 1951-1969 (2021-03-25)
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
Articles
Proteases for biotinylated tag removal for protein purification workflows with related reagents and technical resources.
Related Content
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service