1. Protease Enzymes - Common Applications

    Protease Enzymes - Common Applications
    Introduction to Protease Enzymes There are five families of proteases in which serine (eg: proteinase K/protease K/endopeptidase K), threonine, cysteine, aspartic or metallic groups play a primary catalytic role. Protease enzymes break the long chain-like molecules of proteins into shorter fragments. They are ubiquitous, found in all living organisms, and are essential for cell growth and differentiation. While protease enzymes...
  2. Part 2: Solving Mysteries with Trypsin and Proteinase K

    Part 2: Solving Mysteries with Trypsin and Proteinase K
    In Part 1, we discussed using trypsin on bone specimens as a cleaning alternative to sanding in preparation for DNA extraction. In this second part of the series, we cover the details of attaining a higher yield of DNA using proteinase K. Proteinase K for Higher DNA Yield from Bone Specimens DNA in bone is located in the osteocytes (Hochmeister et...
  3. Part 1: Solving Mysteries with Trypsin and Proteinase K

    Part 1: Solving Mysteries with Trypsin and Proteinase K
    Identifying Human Remains Human remains are fascinating. They have many properties that can be used to identify a person: distinct scars, special features, dental x-rays, fingerprint comparisons, or physical facial characteristics. Forensic scientists attempt to identify human skeletal remains in situations like mass fatality incidents involving military personnel or others recovered from war, fires, explosions, and in criminal matters. However...
  4. Attaining High DNA Yield from Sperm Cells using Proteinase K

    Attaining High DNA Yield from Sperm Cells using Proteinase K
    There are many techniques that can be used to isolate high quality and high molecular weight DNA from mammalian somatic cells. However, these techniques are ineffective for mammalian sperm. Unlike somatic cells, nearly all histones in sperm cells are replaced by protamines held together by disulfide bonds, which compacts the sperm nucleus, rendering it resistant to conventional lysis procedures. Sperm...
  5. Cathepsins - FAQs

    Cathepsins - FAQs
    What are Cathepsins? Cathepsins are proteases, which degrade proteins, found in all animals and other organisms. There are about a dozen members of this family distinguished by their structure, catalytic mechanism, and which proteins they cleave. When do most members become activated? They are activated at low pH found in lysosomes. Where does Cathepsin activity take place? Almost entirely within...
  6. Protease Inhibitors: Killing Viral Replication

    Protease Inhibitors: Killing Viral Replication
    What Is a Protease Inhibitor? To best explain what a protease inhibitor is, let's start with a basic review of the biology of viruses, such as HIV. Firstly, HIV is a virus that attacks the immune system by infecting cells of the immune system. The infection does not kill the cell immediately, but HIV forces the infected cell to make...
  7. Top 4 Scientific Articles on Protease Activity

    Top 4 Scientific Articles on Protease Activity
    Listed below are some articles that are of great reference for those interested in examining protease activity and their relationships to carbon and nitrogen, as well as their characterization. Click on the titles to follow the article. 1. Proteolytic activity in soil: A review WHAT:This article reviews current knowledge on inputs, sources and regulation of protease activities in soils from...
  8. Why should it be AG Scientific's HRV3C Protease?

    Why should it be AG Scientific's HRV3C Protease? Human rhinovirus 3C protease (HRV 3C Protease) is a cysteine protease that recognizes the cleavage site of Leu-Glu-Val-Leu-Phe-Gln-Gly-Pro, commonly referred to as the PreScission Site. It cleaves between Gln and Gly. The recombinant form of the HRV3C protease is a restriction grade protease that has robust activity at 4°C and high specific...
  9. How to Use Proteases for Protein Proteolysis

    How to Use Protease/s for Protein Proteolysis Protein Proteolysis refers to the use of hydrochloric acid to destroy peptide bonds between the amino acids that make up a protein. When carried out with proteases (also known as proteinases), which are enzymes, the process is termed proteolysis. Depending on how efficient the enzyme is or what links it breaks, the proteolysis can be limited or unlimited. Proteolysis can begin either from one end of the chain of amino acids that comprise the protein or somewhere in the middle of it. Unlimited proteolysis produces individual amino acids while limited proteolysis produces short chains of polypeptides.

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