Recombinant Proteinase K For Covid-19 Nucleic Acid Extraction

Description

Proteinase K (Proteinase K), a serine protease, is named proteinase K because it can digest keratin. Proteinase K has a stable structure, extremely high enzymatic activity and broad substrate specificity, but prefers peptide chains with aliphatic and aromatic hydrocarbons, and can preferentially decompose hydrophobic amino acids, sulfur-containing amino acids, and aromatic amino acid carboxyl groups end-linked peptide bonds. Because proteinase K is active in a wide pH range (4~12.5) and high temperature (50~70℃), and will not be inhibited by denaturants such as urea, SDS and EDTA, it has high activity and stability in the buffer for DNA and RNA extraction, so it is always used for the isolation of plasmid or genomic DNA and RNA , is a key reagent for DNA and RNA extraction. Nowadays, proteinase K is mainly used in genetic diagnosis kits, genomic DNA extraction kits, and RNA extraction kits to remove nucleases and other protein contamination in the field of medical diagnosis.

Due to the high stability and strong proteolytic effect of proteinase K, with the outbreak of the Covid-19 epidemic in 2020, the demand for proteinase K has skyrocketed. For the detection of Covid-19 nucleic acid, the role of proteinase K, on ​​the one hand, is to lyse the virus to release nucleic acid, and eliminate the nucleolytic enzyme (RNase) to prevent the RNA degradation of the virus. On the other hand, the virus can be inactivated in the sample pretreatment stage, so that the virus is no longer infectious, and the safety of the transportation and detection stages can be improved. Therefore, proteinase K is an important component of virus sampling solution.

However, currently commercially available proteinase K is mainly isolated and purified from Tritirachiurn album Limber by fermentation which has some difficulties in the production process of proteinase K: 1) Low expression level: Proteinase K can degrade most proteins non-specifically, causing serious toxicity to the expressing host cells, so the expression level of proteinase K is generally very low. 2) Residues of pigments and nucleic acids: Large-scale fermentation introduces a large number of pigments and residues of host nucleic acids, which are difficult to purify and cost high. 3) Unstable and short shelf life: Proteinase K is not stable enough, it can enzymatically hydrolyze itself, and it is difficult to store it stably for a long time without protective agent. Commercially available proteinase K has a typical shelf life of 12 months at 2-8°C. These difficulties made the proteinase K market in short supply.

The recombinant proteinase K(rProK) of Healthgen Biotech is derived from recombinant expression of genetically engineered yeast, and purified by chromatography process with calcium and glycerin as protective agents, which perfect solves the problems mentioned above. rProK has high activity and high capacity, as well as other advantages, such as follows:

1. High capacity and stable supply: 80kg capacity per month can meet bulk demands.
2. High purity: greater than 95% as determined by SDS-PAGE due to Healthgen Biotech’s world-leading protein purification technology.
3. Cost-effective due to the high production capacity more than 80kg/month.
4. Easy to store: store at 2-8 degrees for more than 36 months.
5. High activity greater than 30U/mg and specific activity greater than 40 U/mgP.
6. Excellent stability within and between batches as well as excellent thermal stability, which has complete stability data of the room temperature and accelerated test.
7. DNase and RNase free
8. Can extract ultra-micro amounts of nucleic acid which has been verified by many of our customers and the results are good.

• Source: Yeast
• Other Names: Recombinant ProK, rPK, Proteinase K, rProK, PK
• Certificate: ISO9001:2015 certificate
• Molecular weight: 29kD
• Package size: 1g, 10g, 50g, 100g