Recombinant 2019-nCoV Helicase (His Tag)

Collections: Coronaviruses, Featured viral antigens molecules, Recombinant proteins, Viral antigen

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Product Overview

Tag	His
Host Species	2019-nCoV
Accession	YP_009725308.1
Synonym	SARS-CoV 2 Helicase; SARS-CoV 2 nsp13
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.
Description	Recombinant 2019-nCoV Helicase is produced by our E.coli expression system and the target gene encoding Ala1-Gln601 is expressed with a 6His tag at the C-terminus.
Source	E.coli
AA Sequence	Ala1-Gln601
Molecular Weight	70kDa. AP Mol Mass: 70kDa, reducing conditions.
Purity	>90% as determined by reducing SDS-PAGE.
Formulation	Recombinant 2019-nCoV Helicase Supplied as a 0.2 μm filtered solution of PBS, 10% Glycerol, pH 7.4.
Sensitivity	For Research Use Only
Detection Limit	Store at < -20°C, stable for 6 months after receipt. Please Avoid repeated freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.