Reaction conditions will need to be optimized for each specific application. We recommend an initial PLPro concentration of 20-100 nM when using Ubiquitin-AMC (U-550) or Ubiquitin-Rhodamine 110 (U-555) as a subtrate.
Source
E. coli-derived viral Papain-like Protease protein Glu1541 - Lys1855 with a N-terminal 6-His tag
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
37 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publications using E-610 in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
6 months from date of receipt, -70 °C as supplied.
3 months, -70 °C under sterile conditions after opening.
Buffer
Supplied as a solution in HEPES, NaCl and TCEP.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant His6-SARS Virus Papain-like Protease Protein, CF
Papain-like Protease
PLpro
PL-PRO
pp1a
Replicase polyprotein 1a
Background
The Papain-like protease ("PLPro") from the human SARS coronavirus (Severe Acute Respiratory Syndrome coronavirus) is a cysteine protease located within the non-structural protein 3 (NS3) section of the viral polypeptide. PLPro activity is required to process the viral polyprotein into functional, mature subunits; specifically, PLPro cleaves a site at the amino-terminus of the viral replicase region. In addition to its role in viral protein maturation, PLPro possesses a deubiquitinating and deISGylating activity. In vivo, this protease antagonizes innate immunity by inhibiting IRF3-induced production of type I interferons. PLPro has been reported to hydrolyze both K48- and K63 linked poly-Ubiquitin chains in vitro. When used at low concentrations, the enzyme demonstrates a strong preference for K48-linked tetra-Ubiquitin chains which are primarily converted to di-Ubiquitin species.
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