Blogs about Enzymes

  1. Daptomycin: Frequently Asked Questions - Answered!

    Daptomycin: Frequently Asked Questions - Answered!
    For the last 15 years, A.G. Scientific has been a leading supplier of Daptomycin. We offer a range of catalog sizes, as well as, multi-kilogram quantities for bulk applications. Additionally, we provide a full service of bottling, sterile formulations, custom packaging, as well as, comprehensive private labeling capabilities.
  2. Beta-Lactamase and Microbial Antibiotic Resistance

    Beta-Lactamase and Microbial Antibiotic Resistance
    β-Lactamases continue to be the leading cause of resistance to β-lactam antibiotics among gram-negative bacteria. In recent years there has been an increased incidence and prevalence of extended-spectrum β-lactamases (ESBLs), enzymes that hydrolyze and cause resistance to oxyimino-cephalosporins and aztreonam.
  3. RNase A: Frequently Asked Questions

    RNase A: Frequently Asked Questions
    Introduction to RNase Ribonucleases (RNases) are a large group of hydrolytic enzymes that degrade ribonucleic acid (RNA) molecules. These are nucleases that catalyze the breakdown of RNA into smaller components. They are a superfamily of enzymes which catalyze the degradation of RNA, operating at the levels of transcription and translation. 3D conformation of ribonuclease A enzyme These enzymes are present...
  4. IPTG Triggers the Transcription of the Lac Operon

    IPTG Triggers the Transcription of the Lac Operon
    Isopropyl β-D-1-thiogalactopyranoside, abbreviated IPTG, is a molecular biology reagent. This compound is used as a molecular mimic of allolactose, a lactose metabolite that triggers transcription of the lac operon.
  5. Frequently Asked Questions About Proteinase K

    Frequently Asked Questions About Proteinase K
    In molecular biology Proteinase K (also protease K or endopeptidase K) is a broad-spectrum serine protease. The enzyme was discovered in 1974 in extracts of the fungus Engyodontium album (formerly Tritirachium album). Proteinase K is able to digest native keratin (hair), hence, the name "Proteinase K". The predominant site of cleavage is the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked alpha amino groups. It is commonly used for its broad specificity.

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