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SAE0045

Sigma-Aldrich

HRV-3C Protease.

N-Terminal His tagged recombinant protein, aqueous solution, 0.8-1.2 mg/mL

Synonym(s):

Human Rhinovirus 3C Protease, Levlfqgp site protease, PreScission Protease

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About This Item

UNSPSC Code:
12352204
NACRES:
NA.54

biological source

human (human Rhinovirus Type 14)

Quality Level

200

Assay

≥90% (SDS-PAGE)

form

aqueous solution

specific activity

≥5000 U/mg

mol wt

21 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.
Proteolytic cleavage occurs between the Gln and Gly residues.
HRV-3C protease is a useful tool to cleave recombinant proteins that are expressed as a fusion protein with this sequence, between the carrier domain and the protein of interest.
This recombinant version contains a six-histidine tag and can be easily removed by IMAC chromatography.

Application

HRV-3C Protease has been used to remove the GST tag from the DsCystatin protein.

Unit Definition

One unit of HRV-3C Protease is defined as the amount of enzyme needed to digest 1nmole of the substrate peptide per hour (H-Glu-Ala-Leu-Phe-Gln-pNA) at 0 °C, in a reaction buffer consisting of 25 mM HEPES (pH 7.5), 150 mM NaCl, 1 mM EDTA, and 1 mM DTT.

Physical form

Supplied in a solution containing 50 mM Tris HCl (pH 7.5), 0.15 M NaCl, 1 mM TCEP and 50% (V/V) glycerol.

Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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An immunosuppressive tick salivary gland protein DsCystatin interferes with Toll-like receptor signaling by downregulating TRAF6
Ta S et al.9
Frontiers in Immunology, 9 (2018)
Activity of the human rhinovirus 3C protease studied in various buffers, additives and detergents solutions for recombinant protein production
Raheem U et al.
PLoS ONE (2016)
Richard W Birkinshaw et al.
Molecular cell, 81(10), 2123-2134 (2021-04-02)
A body of data supports the existence of core (α2-α5) dimers of BAK and BAX in the oligomeric, membrane-perturbing conformation of these essential apoptotic effector molecules. Molecular structures for these dimers have only been captured for truncated constructs encompassing the
Zhengmao Xu et al.
Parasites & vectors, 12(1), 341-341 (2019-07-13)
Rhipicephalus haemaphysaloides is a widespread tick species in China and other South East Asian countries, where it is the vector of many pathogens. The objective of this study was to study the role of serpin (serine protease inhibitor) during the
Micah Rapp et al.
Cell reports, 35(1), 108950-108950 (2021-04-02)
Antibodies with heavy chains that derive from the VH1-2 gene constitute some of the most potent severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)-neutralizing antibodies yet identified. To provide insight into whether these genetic similarities inform common modes of recognition, we
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