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Native Human Tryptase
Cat No.
NATE-0725
Description
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 > 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.
Abbr
Tryptase, Native (Human)
Alias
tryptase
Source
Human lung
Species
Human
Applications
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.
Product Overview
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 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.
Form
buffered aqueous solution, solution in 1 M NaCl, 50 mM sodium acetate, pH 5.0, containing 0.01% sodium azide
Enzyme Commission Number
EC 3.4.21.59
Activity
> 5 units/mg protein
CAS No.
97501-93-4
Molecular Weight
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-benzoyl DL-arginine p-nitroanilide per minute at pH 7.8 at 37°C.
Storage
−20°C
Pathway
Activation of Matrix Metalloproteinases, organism-specific biosystem; Degradation of the extracellular matrix, organism-specific biosystem; Extracellular matrix organization, organism-specific biosystem
Function
peptidase activity; protein binding; serine-type endopeptidase activity; serine-type peptidase activity; peptidase activity; serine-type endopeptidase activity; serine-type peptidase activity; serine-type endopeptidase activity; serine-type peptidase activity; peptidase activity; serine-type endopeptidase activity; serine-type peptidase activity
Synonyms
tryptase; mast cell tryptase; mast cell protease II; skin tryptase; lung tryptase; pituitary tryptase; mast cell neutral proteinase; mast cell tryptase; mast cell neutral proteinase; mast cell serine proteinase II; mast cell proteinase II; mast cell serine proteinase tryptase; rat mast cell protease II; tryptase M; EC 3.4.21.59
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