SARS-CoV-2 Helicase Protein (His & MBP)

The non—structural protein 13 (nsp13) of SARS—CoV 2 is a helicase that separates double—stranded RNA or DNA with a 5'—3' polarity, using the energy of nucleotide hydrolysis. A basic biochemical characterization of nsp13 demonstrated that it can unwind both doublestranded DNA and RNA in a 5’-3’ direction, and it can hydrolyze all deoxyribonucleotide and ribonucleotide triphosphates. Helicases are motor proteins that utilize the energy derived from nucleotide hydrolysisto unwind double-stranded nucleic acids into two single-stranded nucleic acids. Initially, helicases were only thought to be molecular engines that unwind nucleic acids during replication, recombination, and DNA repair. Recent studies have shown that they are also involved in other biological processes, including displacement of proteins from nucleic acid, movement of Holliday junctions, chromatin remodeling, catalysis of nucleic acid conformational changes, several aspects of RNA metabolism, including transcription, mRNA splicing, mRNA export, translation, RNA stability and mitochondrial gene expression. Some human diseases, including Bloom’s syndrome, Werner’s syndrome, and Xeroderma Pigmentosum have been associated with defects in helicase function.

Pack Size	Availability	Price/USD
10 μg	5 days	$ 154.00
50 μg	5 days	$ 465.00
500 μg	5 days	$ 2,480.00
1 mg	5 days	$ 3,720.00

Pack Size

Availability

Price/USD

Quantity

10 μg

5 days

$ 154.00

50 μg

5 days

$ 465.00

500 μg

5 days

$ 2,480.00

1 mg

5 days

$ 3,720.00

Description

Species	SARS-CoV-2
Expression System	E. coli
Tag	C-6His
Accession Number	P0DTD1
Synonyms	SARS-CoV 2 nsp13, SARS-CoV 2 Helicase
Amino Acid	Ala5325-Gln5925
Construction	Recombinant 2019-nCoV Helicase is produced by our E.coli expression system and the target gene encoding Ala5325-Gln5925 is expressed with a 6His, MBP tag at the N-terminus.
Protein Purity	Greater than 80% as determined by reducing SDS-PAGE. (QC verified)
Molecular Weight	120 KDa, reducing conditions

Formulation	Supplied as a 0.2 μm filtered solution of PBS, pH 7.4.
Stability & Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Research Background	The non—structural protein 13 (nsp13) of SARS—CoV 2 is a helicase that separates double—stranded RNA or DNA with a 5'—3' polarity, using the energy of nucleotide hydrolysis. A basic biochemical characterization of nsp13 demonstrated that it can unwind both doublestranded DNA and RNA in a 5’-3’ direction, and it can hydrolyze all deoxyribonucleotide and ribonucleotide triphosphates. Helicases are motor proteins that utilize the energy derived from nucleotide hydrolysisto unwind double-stranded nucleic acids into two single-stranded nucleic acids. Initially, helicases were only thought to be molecular engines that unwind nucleic acids during replication, recombination, and DNA repair. Recent studies have shown that they are also involved in other biological processes, including displacement of proteins from nucleic acid, movement of Holliday junctions, chromatin remodeling, catalysis of nucleic acid conformational changes, several aspects of RNA metabolism, including transcription, mRNA splicing, mRNA export, translation, RNA stability and mitochondrial gene expression. Some human diseases, including Bloom’s syndrome, Werner’s syndrome, and Xeroderma Pigmentosum have been associated with defects in helicase function.

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SARS-CoV-2 Helicase Protein (His & MBP)

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