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T7063 Sigma-Aldrich

Tryptase from human lung

buffered aqueous solution, ≥5 units/mg protein



Related Categories 3.4.x.x Peptidases, 3.x.x.x Hydrolases, Application Index, Biochemicals and Reagents, Enzyme Class Index,
form   buffered aqueous solution
shipped in   dry ice
storage temp.   −20°C
Gene Information   human ... TPSAB1(7177), TPSB2(64499), TPSD1(23430), TPSG1(25823)


General description

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.

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.


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.

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.


Highly purified

Physical properties

Molecular Weight: ~135 kDa (Human)(Non-covalently linked tetramer with two sets of dissimilar subunits possibly resulting from heterogeneity in N-linked glycosylation and existence of a & b isoforms sequences in human lung). 31-33 kDa (Monomer MW)

Unit Definition

One unit will hydrolyze 1.0 μmole of N-benzyl-DL-Arg-pNA per minute at pH 8 at 25 °C.

Physical form

Solution in 1 M NaCl, 50 mM sodium acetate, pH 5.0, containing 0.01% sodium azide

Safety & Documentation

Safety Information

NONH for all modes of transport
WGK Germany 


Certificate of Analysis


Certificate of Origin


Frequently Asked Questions

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Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product.
What is the extinction coefficient (E1%)of product T7063, Tryptase from human lung?
The extinction coefficient (E1%) of product T7063, Tryptase from human lung, is 30.3 when measured at 280 nm wavelength.
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