l General Information |
Product Name | Tryptase from human lung |
General deion | Tryptase is a glycoprotein released from mast cells during anaphylaxis, which performs a number of functions including catalyzing the activation of complement C3, converting prostromelysin to stromelysin (MMP-3), and cleaving fibrinogen resulting in a loss of clotting potential. Human tryptase is a major secretory protease of human lung mast cells. |
Assay | ≥5 units/mg protein |
Molecular Weight | ~135 kDa (Human) | MDL number | MFCD00272854 |
Suitability | BioReagent |
l Physical and Chemical Information |
Appearance | Colorless Clear to Faint Yellow buffered aqueous solution |
Physical form | Solution in 1 M NaCl, 50 mM sodium acetate, pH 5.0, containing 0.01% sodium azide |
l Biological Information |
Biochem/Physiol Actions | Tryptase is a member of the serine protease S1 family. It is the predominant neutral protease of the mast cell granules. Within the mast cell granule it exists as a heparin-stabilized active tetramer. Stabilization is a result of the high negative charge density of the glycosaminoglycan. This stabilization activity is observed with heparins with a MW greater than 6 kDa as well as other glycosaminoglycans such as dextran sulfate or chondroitin sulfates. Removal of heparin results in dissociation of the tetramer and inactivation of the enzyme. High concentrations of NaCl will result in the dissociation of heparin. Tryptase is released from the mast cell as a result of the degranulation response during anaphylaxis. In addition, several tryptase genes and alleles (α, β, γ & δ) have been identified in various tissues and circulating in blood. Pro-β-tryptase is thought to be the constituative circulating form in blood. The biological function of tryptase is unknown. However it has been reported to catalyze the activation of complement C3, convert prostromelysin to stromelysin (MMP-3), and cleave fibrinogen resulting in a loss of clottting potential. Tryptase also degrades fibronectin, calcitonin gene-related peptide, vasoactive intestinal peptide, and kininogen. |
Application | Tryptase has been used in a study that purified and characterized recombinant rat mast cell protease 7 expressed in Pichia pastoris. Tryptase has also been used in a study to investigate drug allergies in mast cell disease. |
Preparation Note | Solution in 1 M NaCl, 50 mM sodium acetate, pH 5.0, containing 0.01% sodium azide |
Unit Definition | One unit will hydrolyze 1.0 μmole of N-benzyl-DL-Arg-pNA per minute at pH 8 at 25 °C. |
l Storage |
Storage temp. | -20°C |
l Precautions and Disclaimer |
This product is for R&D use only, not for drug, household, or other uses. |
l References |
1. http://www.drugbank.ca 2. https://ncit.nci.nih.gov 3. https://www.ncbi.nlm.nih.gov |
