1. Recombinant Proteins
  2. Enzymes & Regulators
  3. Serpins (Protease Inhibitors)

Serpins (Protease Inhibitors)

Serpins (serine proteinase inhibitors) are a superfamily of evolutionarily conserved, structurally homologous proteins that antagonize the activity of serine proteases and involved in many critical biological processes like blood coagulation, fibrinolysis, programmed cell death, development and inflammation. Serpins are found across the kingdoms Eukarya, Bacteria, Archaea and some viruses. So far, About 37 serpins have been identified in the human body. Thirty of these are functional protease inhibitors. Serpins generally consist of ~350-400 amino acid residues and molecular weight varies between 40 and 100 kDa due to differences in their glycosylation profile. In general, they fold into 7-9 α helices and 3 β-sheets. The core structure of serpins is highly conserved, which is important for their function that uses a conformational change to inhibit target enzymes.

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