Tryptase alpha/beta-1 is a trypsin-like serine protease. The enzyme is stored in the secretory granules of mast cells in an inactive form and is released upon the activation and degranulation of these cells . When released, it forms active tetramers stabilized by heparin proteoglycan . This unique tetrameric structure makes the enzyme resistant to all known endogenous proteinase inhibitors .
The enzyme’s active sites are arranged in such a way that they face a narrow central pore, which contributes to its resistance to inhibition . This structural arrangement is essential for its function in the extracellular matrix, where it participates in various physiological and pathological processes.
Tryptase alpha/beta-1 is involved in several critical biological processes, including:
Recombinant human tryptase alpha/beta-1 is produced using advanced biotechnological methods. The enzyme is typically expressed in a mouse myeloma cell line (NS0) and purified to high levels of purity (>95%) using techniques such as SDS-PAGE under reducing conditions . The recombinant form is often tagged with a C-terminal 10-His tag to facilitate purification and detection .
The recombinant enzyme is supplied as a carrier-free formulation, which means it does not contain bovine serum albumin (BSA). This formulation is particularly useful for applications where the presence of BSA could interfere with experimental results .