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SARS-CoV-2 NSP13 Recombinant Protein (RPES7054)

SKU:
RPES7054
Product Type:
Recombinant Protein
Species:
Virus
€729

Description

Product Name:SARS-CoV-2 NSP13 Recombinant Protein
Product Code:RPES7054
Size:50µg
Species:SARS-CoV-2
Expression Host:E.coli
Synonyms:SARS-CoV 2 nsp13,Helicase
Mol Mass:69.15kDa
Tag:N-His
Purity:> 90 % as determined by reducing SDS-PAGE.
Endotoxin Level:Please contact us for more information.
Bio Activity:Testing in progress
Sequence:Ala5325-Gln5925
Accession:QHD43415.1
Storage:Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
Shipping:This product is provided as lyophilized powder which is shipped with ice packs.
Formulation:Lyopilized from PBS pH7. 4,0.02%NLS, 1mM EDTA, 4%trehalose,1% mannitol. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual.
Reconstitution:Please refer to the printed manual for detailed information.
Background:NSP13 is a 67 kDa protein that belongs to the helicase superfamily 1B, it utilizes the energy of nucleotide triphosphate hydrolysis to catalyze the unwinding of double-stranded DNA or RNA in a 5′ to 3′ direction. Although NSP13 is believed to act on RNA in vivo enzymatic characterization shows a significantly more robust activity on DNA in in vitro assays with relatively weak non processive helicase activity when compared to other superfamily 1B enzymes. NSP13 has been shown to interact with the viral RNA-dependent RNA polymerase NSP1210,11, and acts in concert with the replication-transcription complex (NSP7/NSP8/NSP12). This interaction has been found to significantly stimulate the helicase activity of NSP13 possibly by means of mechano-regulation. In addition to its helicase activity, NSP13 also possesses RNA 5′ triphosphatase activity within the same active site, suggesting a further essential role for NSP13 in the formation of the viral 5′ mRNA cap.

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