1. A Guide to Necroptosis Inhibitors

    There is extensive evidence that necrosis plays a prominent role in a wide range of human pathological conditions, such as myocardial infarct, ischemic injury and neurodegeneration. Therefore, development of necrosis inhibitors is of high interest.
  2. Guide to Necrosis Signaling Pathway Inhibitors

    Necrosis is the premature death of cells in living tissue and can be caused by external factors to the cell or tissue, such as infection, toxins, cancer, infarction, poisons, ROS (Reactive Oxygen Species), inflammation or trauma. Necrosis inhibitors can counteract the effects that may normally cause cell death.   Historically, cell death has been subdivided into regulated (apoptosis, AKA programmed...
  3. Chymostatin (Protease Inhibitor) - Frequently Asked Questions

    Microbial product, chymostatin was discovered by H. Umezawaet al.v in 1970 by testing the anti-chymotrypsin activity of culture filtrates. Since the amino acid analysis of different samples gave variable ratios of phenylalanine, leucine, valine and isoleucine, chymostatin was considered to be a mixture of similar peptides with minor differences. Attempts to separate the components were unsuccessful.
  4. 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.
  5. E-64, Cysteine Protease Inhibitor: Frequently Asked Questions

    E-64, Cysteine Protease Inhibitor: Frequently Asked Questions
    Irreversible, potent and highly selective inhibitor of cysteine proteases. Does not affect cysteine residues in other enzymes. Acts by forming a thioether bond with thiol of the active cysteine. E-64 will not inhibit serine proteases (except trypsin) inhibits activation-induced programmed cell death and restores defective immune responses in HIV+ donors. Specific active site titrant.
  6. Phosphatase Inhibitor Cocktails, Ready Made Formulations

    Invasive phosphatases can contaminate research samples and slow or halt research progress, rendering time-consuming and expensive work useless.

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