Different grades and packaging are available.

BenzoNuclease® is a recombinant endonuclease derived from Serratia marcescensa. The protein is expressed in Escherichia coli (E. coli). BenzoNuclease® has been shown to exert a broad spectrum of substrate specificity to degrade both DNA and RNA—whether single-stranded, double-stranded, linear, circular or supercoiled. No base preference is observed. As with all endonucleases, BenzoNuclease® hydrolyzes internal phosphodiester bonds present between the nucleotides. Upon complete digestion, all free nucleic acids present in solution are reduced to 5’-monophosphate-terminated oligonucleotides, which are three to five bases in length. In scientific research, BenzoNuclease® can be used as the preferred enzyme preparation for supernatant of cultured cells and viscosity removal of cell lysate, which can remove nucleic acid interference and improve the subsequent protein purification or functional research. At the same time in the vaccine industry, protein and polysaccharide pharmaceutical industry, used to remove the host residual nucleic acid, greatly reduce the vaccine and protein products of nucleic acid pollution, reduce the processing steps, improve the yield of products. This product is expressed by large-scale fermentation of E. coli, and is produced with raw materials of medicinal specifications. The host protein residue, nucleic acid residue and common pathogens are strictly controlled, and the production and quality management procedures of the product comply with GMP regulations to ensure the traceability of the production process and all raw materials.

Enterokinase (light chain), highly specifically recognizes the Asp-Asp-Asp-Asp-Lys sequence and hydrolyzes the polypeptides at the C-terminus of Lys. It can convert trypsinogen to trypsin in vivo, and fusion proteins with this recognition sequence can also be cleaved. This product, enterokinase, produced by recombinant yeast secretion and expression system, is of a high purity, high bio-activity, and an excellent stability, which allows a wide range of working condition (4-45℃, pH 4.5-9.5) even keeps a part of bio-activity in the presence of various detergent and denatured agents. This product is from a large scale GMP leveled recombinant enterokinase production via Pichia pastoris expression. Applying pharmaceutical leveled adjuvant and material for production, strictly controlling host protein residues, nucleic acid residues and other impurities, we guarantee manufacture and quality control practice complying to GMP regulation, as well as all the materials traceable.

E. coli Poly (A) Polymerase does not depend on the presence of template, and can catalyze the sequential incorporation of ATP in the form of AMP into the 3´ terminal of RNA, i.e., the addition of polyA tail to the 3´ terminal of RNA. Poly (A) polymerase has A high tail adding efficiency and can add 20 to 200 A bases to the 3´ terminal of RNA. Polyadenylation improves the stability of RNA in cells and enhances the expression efficiency of RNA after transfection or microinjection. Poly(A) tails can be used as primer binding sites for first-strand cDNA synthesis in some applications and can be used for end-labeling or quantification of miRNA. The original enzymes of T7 RNA Transcription Enzyme Mix produced in E. coli. Our manufacturing processes are strictly controlled to ensure the end products free from host protein or nucleic acid contaminations and other impurities following the Pharmaceutical Manufacturing Guidelines. We guarantee the manufacturing and quality control comply with GMP regulation for tracking each and every step of the manufacturing process, including raw material sourcing.