SDS-PAGE gel of SARS PLpro/papain-like protease Protein 4372

SARS PLpro/papain-like protease Protein 8372

$150.00 – $500.00

Summary

Expression: E.coli
Pure: Yes (SDS-PAGE)
Amino Acid Range: Glu1-Ile314

available size

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SKU: 8372parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	P0C6U8
express system	E.coli
product tag	N-His-Avi
purity	> 95% as determined by Tris-Bis PAGE
background	The coronaviral proteases, papain-like protease (PLpro) and 3C-like protease (3CLpro), are attractive antiviral drug targets because they are essential for coronaviral replication. Although the primary function of PLpro and 3CLpro are to process the viral polyprotein in a coordinated manner, PLpro has the additional function of stripping ubiquitin and ISG15 from host-cell proteins to aid coronaviruses in their evasion of the host innate immune responses.
molecular weight	The protein has a predicted MW of 38.6 kDa same as Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

SARS PLpro/papain-like protease Protein 8372

protein

Size and concentration 100, 500µg and liquid
Form Liquid
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped with dry ice.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
The coronaviral proteases, papain-like protease (PLpro) and 3C-like protease (3CLpro), are attractive antiviral drug targets because they are essential for coronaviral replication. Although the primary function of PLpro and 3CLpro are to process the viral polyprotein in a coordinated manner, PLpro has the additional function of stripping ubiquitin and ISG15 from host-cell proteins to aid coronaviruses in their evasion of the host innate immune responses.
Protein names Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Host translation inhibitor nsp1 (Leader protein) (Non-structural protein 1) (nsp1); Non-structural protein 2 (nsp2) (p65 homolog); Papain-like protease nsp3 (PL-PRO) (EC 3.4.19.12) (EC 3.4.22.-) (Non-structural protein 3) (nsp3) (PL2-PRO); Non-structural protein 4 (nsp4);
Protein family Coronaviruses polyprotein 1ab family
Mass 486373Da
Function [Isoform Replicase polyprotein 1a]: Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein. {ECO:0000305}.; [Host translation inhibitor nsp1]: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response (PubMed:23035226). May disrupt nuclear pore function by binding and displacing host NUP93 (PubMed:30943371). {ECO:0000269\|PubMed:23035226, ECO:0000269\|PubMed:30943371}.; [Non-structural protein 2]: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2 (PubMed:19640993). Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses (PubMed:19640993). {ECO:0000269\|PubMed:19640993}.; [Papain-like protease nsp3]: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates (PubMed:17692280). Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:23943763, PubMed:24410069). Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3 (PubMed:19369340, PubMed:24622840). Prevents also host NF-kappa-B signaling (PubMed:19369340, PubMed:24622840). {ECO:0000269\|PubMed:16271890, ECO:0000269\|PubMed:17692280, ECO:0000269\|PubMed:19369340, ECO:0000269\|PubMed:23943763, ECO:0000269\|PubMed:24622840, ECO:0000303\|PubMed:24410069}.; [Non-structural protein 4]: Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763, PubMed:24410069). Alone appears incapable to induce membrane curvature, but together with nsp3 is able to induce paired membranes (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:23943763, PubMed:24410069). {ECO:0000269\|PubMed:23943763, ECO:0000303\|PubMed:24410069}.; [3C-like proteinase nsp5]: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-\|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP). May cleave host ATP6V1G1 thereby modifying host vacuoles intracellular pH. {ECO:0000255\|PROSITE-ProRule:PRU00772, ECO:0000269\|PubMed:16226257}.; [Non-structural protein 6]: Plays a role in host membrane rearrangement that leads to creation of cytoplasmic double-membrane vesicles (DMV) necessary for viral replication (PubMed:23943763). Nsp3, nsp4 and nsp6 together are sufficient to form DMV (PubMed:23943763, PubMed:24410069). Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes (PubMed:24991833). {ECO:0000269\|PubMed:23943763, ECO:0000269\|PubMed:24991833, ECO:0000303\|PubMed:24410069}.; [Non-structural protein 7]: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000269\|PubMed:22039154}.; [Non-structural protein 8]: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers. {ECO:0000269\|PubMed:22039154}.; [RNA-capping enzyme subunit nsp9]: Catalytic subunit of viral RNA capping enzyme which catalyzes the RNA guanylyltransferase reaction for genomic and sub-genomic RNAs. The kinase-like NiRAN domain of NSP12 transfers RNA to the amino terminus of NSP9, forming a covalent RNA-protein intermediate. Subsequently, the NiRAN domain transfers RNA to GDP, forming the core cap structure GpppA-RNA. The NSP14 and NSP16 methyltransferases then add methyl groups to form functional cap structures. {ECO:0000250\|UniProtKB:P0DTC1, ECO:0000269\|PubMed:19153232}.; [Non-structural protein 10]: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation. {ECO:0000269\|PubMed:22635272}.
Catalytic activity CATALYTIC ACTIVITY: [3C-like proteinase nsp5]: Reaction=TSAVLQ-\|-SGFRK-NH2 and SGVTFQ-\|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.; EC=3.4.22.69; Evidence={ECO:0000269\|PubMed:12917450, ECO:0000269\|PubMed:14561748}; CATALYTIC ACTIVITY: [Papain-like protease nsp3]: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269\|PubMed:12917450, ECO:0000269\|PubMed:17692280}; CATALYTIC ACTIVITY: [RNA-capping enzyme subunit nsp9]: Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate; Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50; Evidence={ECO:0000250\|UniProtKB:P0DTC1}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67014; Evidence={ECO:0000250\|UniProtKB:P0DTC1};
Subellular location [Non-structural protein 2]: Host cytoplasm {ECO:0000250\|UniProtKB:P0DTD1}. Host endosome {ECO:0000250\|UniProtKB:P0DTD1}.; [Papain-like protease nsp3]: Host membrane {ECO:0000305}; Multi-pass membrane protein. Host cytoplasm {ECO:0000269\|PubMed:23943763}.; [Non-structural protein 4]: Host membrane; Multi-pass membrane protein. Host cytoplasm {ECO:0000269\|PubMed:23943763}. Note=Localizes in virally-induced cytoplasmic double-membrane vesicles. {ECO:0000269\|PubMed:21345958, ECO:0000269\|PubMed:23943763}.; [3C-like proteinase nsp5]: Host cytoplasm {ECO:0000250\|UniProtKB:P0DTD1}. Host Golgi apparatus {ECO:0000250\|UniProtKB:P0DTD1}.; [Non-structural protein 6]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; [Non-structural protein 7]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250\|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250\|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.; [Non-structural protein 8]: Host cytoplasm, host perinuclear region {ECO:0000269\|PubMed:17532020}. Host cytoplasm {ECO:0000250\|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250\|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.; [RNA-capping enzyme subunit nsp9]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250\|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250\|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.; [Non-structural protein 10]: Host cytoplasm, host perinuclear region {ECO:0000250}. Host cytoplasm {ECO:0000250\|UniProtKB:P0DTD1}. Host endoplasmic reticulum {ECO:0000250\|UniProtKB:P0DTD1}. Note=nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes.
Structure [Non-structural protein 2]: Interacts with host PHB and PHB2. {ECO:0000269\|PubMed:19640993}.; [Non-structural protein 4]: Interacts with papain-like protease and non-structural protein 6. {ECO:0000269\|PubMed:21345958}.; [3C-like proteinase nsp5]: Exists as monomer and homodimer. Only the homodimer shows catalytic activity. {ECO:0000269\|PubMed:14561748, ECO:0000269\|PubMed:15507456}.; [Non-structural protein 7]: Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure. {ECO:0000269\|PubMed:16228002}.; [Non-structural protein 8]: Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure (PubMed:16228002). Interacts with ORF6 protein (PubMed:17532020). {ECO:0000269\|PubMed:16228002, ECO:0000269\|PubMed:17532020}.; [RNA-capping enzyme subunit nsp9]: Homodimer. {ECO:0000269\|PubMed:19153232}.; [Non-structural protein 10]: Homododecamer. {ECO:0000269\|PubMed:16873247}.
Post-translational modification [Isoform Replicase polyprotein 1a]: Specific enzymatic cleavages in vivo by its own proteases yield mature proteins (PubMed:12917450, PubMed:15331731, PubMed:15564471, PubMed:16306590, PubMed:32083638). 3C-like proteinase nsp5 liberates nsps 6-11 from the polyprotein (PubMed:32083638). Papain-like and 3C-like proteinases are autocatalytically processed. {ECO:0000269\|PubMed:12917450, ECO:0000269\|PubMed:15331731, ECO:0000269\|PubMed:15564471, ECO:0000269\|PubMed:16306590, ECO:0000269\|PubMed:32083638}.
Domain [Papain-like protease nsp3]: The hydrophobic region HD1 probably mediates the membrane assoc
Target Relevance information above includes information from UniProt accession: P0C6U8
The UniProt Consortium

Data

SDS-PAGE gel of SARS PLpro/papain-like protease Protein

SARS-CoV-2 PLpro on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

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Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.