The ability to produce enzymes through recombinant DNA technology has expanded the availability and versatility of enzymes, enabling their use in diverse applications for improved efficiency and sustainability
Source | Escherichia Coli (E. Coli) |
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Description | Enterokinase is a human-produced enzyme, meticulously synthesized within E. Coli cells. This enzyme plays a critical role in various scientific and industrial applications. |
Structure & Composition | Enterokinase is composed of a single, non-glycosylated polypeptide chain, containing 237 amino acids (residues 785-1019aa). It boasts a molecular mass of 26.4kDa, indicative of its refined structural integrity. |
Physical Appearance | liquid solution form, ready for immediate use |
Applications | The enzyme is ideal for research, development, and industrial processes requiring the unique catalytic properties of Enterokinase. |
Source | Escherichia Coli (E. Coli) |
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Description | Benzonase Nuclease is an enzyme derived from Serratia marcescens, known for its robust ability to degrade all forms of DNA and RNA, essential for numerous applications in molecular biology. |
Structure & Composition | A single, non-glycosylated polypeptide chain containing 245 amino acids with a molecular mass of 30 kDa and 2 essential disulfide bonds. |
Physical Appearance | Sterile Filtered colorless solution |
Applications | Effective removal of nucleic acids, Viscosity reduction from protein solutions., Enhanced protein purification. Increased gel resolution and Prevention of cell clumping. |
Source | Escherichia Coli (E. Coli) |
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Description | L-Asparaginase, derived from E.coli, is a hydrolytic enzyme known for its ability to break down the non-essential amino acid L-asparagine into L-aspartic acid and ammonia. Within the food industry, it plays a vital role in preventing the formation of acrylamide, a potential neurotoxin and carcinogen. |
Structure & Composition | The enzyme is a tetrameric polypeptide chain with a molecular mass of 34,564 Dalton. It functions by catalyzing the conversion of L-asparagine. |
Physical Appearance | Sterile Filtered White lyophilized (freeze-dried) powder. |
Applications | L-Asparaginase's unique ability to break down asparagine has made it an essential tool in the food industry, ensuring the reduction of acrylamide levels in various food products and thereby contributing to food safety. |
SDIAGNOSTIC | Taq Polymerase | Reverse Transcriptase | PFU DNA Polymerase |
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Source | E. Coli | E. Coli | E. Coli |
Description | Taq DNA Polymerase is a thermostable enzyme of approximately 95 kDa, isolated from Thermus aquaticus. It replicates DNA at 74°C and has a half-life of 40 minutes at 95°C. This enzyme catalyses the polymerization of nucleotides into duplex DNA in the 5´3´ direction and possesses 5´3´ exonuclease activity. | Enzyme of 71 kDa, Reverse Transcriptase (RT), or RNA-dependent DNA polymerase, is an enzyme that transcribes single-stranded RNA into DNA. It synthesizes a double-helix DNA after initially converting the RNA into single-strand DNA. RT plays a vital role in the life cycle of RNA viruses like retroviruses, where it helps convert their RNA genomes into DNA for integration into the host genome. | Pfu DNA Polymerase is a thermo-stable enzyme with a molecular weight of about 90kDa. Derived from E. coli and cloned from Pyrococcus furiosus strain Vc1 DSM3638, it replicates DNA at 75°C and catalyses the polymerization of nucleotides in the 5´ to 3´ directions with the presence of magnesium. It also possesses 3´ to 5´ exonuclease (proofreading) activity, making it suitable for PCR and primer extension reactions that require high-fidelity synthesis. |
Usage | The enzyme is a tetrameric polypeptide chain with a molecular mass of 34,564 Dalton. It functions by catalyzing the conversion of L-asparagine. | The enzyme is a tetrameric polypeptide chain with a molecular mass of 34,564 Dalton. It functions by catalyzing the conversion of L-asparagine. | The enzyme is a tetrameric polypeptide chain with a molecular mass of 34,564 Dalton. It functions by catalyzing the conversion of L-asparagine. |