The extinction coefficient (E1%) of product T7063, Tryptase from human lung, is 30.3 when measured at 280 nm wavelength.
T7063
Tryptase from human lung
buffered aqueous solution, ≥5 units/mg protein
Synonyme(s) :
Tryptase enzyme
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About This Item
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Produits recommandés
Forme
buffered aqueous solution
Niveau de qualité
Activité spécifique
≥5 units/mg protein
Poids mol.
~135 kDa
Conditions d'expédition
dry ice
Température de stockage
−20°C
Informations sur le gène
human ... TPSAB1(7177) , TPSB2(64499) , TPSD1(23430) , TPSG1(25823)
Description générale
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. [1]
Application
Actions biochimiques/physiologiques
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.
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.
Qualité
Highly purified
Propriétés physiques
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)
Définition de l'unité
One unit will hydrolyze 1.0 μmole of N-benzyl-DL-Arg-pNA per minute at pH 8 at 25 °C.
Forme physique
Supplied as a liquid in 50mM Sodium Acetate, 1M Sodium Chloride, pH 5.0 with 0.05mM Heparin and 0.01% Sodium Azide
Code de la classe de stockage
12 - Non Combustible Liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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Les clients ont également consulté
Michele Ammendola et al.
Updates in surgery, 65(1), 53-57 (2012-11-03)
Literature data indicate that mast cells (MCs) are involved in angiogenesis through the release of several pro-angiogenetic factors among which tryptase, a serine protease stored in MC granules, is one of the most active. However, no data are available concerning
Grazyna Michalska-Krzanowska
Advances in clinical and experimental medicine : official organ Wroclaw Medical University, 21(3), 403-408 (2012-12-12)
Determination of serum mast cell tryptase (MCT) is becoming more widely used in diagnosing allergic reactions involving mast cells. It can help evaluate the allergenic effects of drugs administered during anesthesia and the perioperative period. Until now, data about the
Liang Chen et al.
Journal of cellular biochemistry, 120(6), 9799-9809 (2018-12-16)
Macrophages polarization plays essential but different roles in most diseases such as atherosclerosis, adipose tissue inflammation, and insulin resistance. Our previous study revealed that protease-activated receptor 2 (PAR2), a G-protein coupled receptor influenced macrophage function, but little is known regarding
Peter Vadas et al.
The Journal of allergy and clinical immunology, 131(1), 144-149 (2012-10-09)
Platelet-activating factor (PAF) is an important mediator and correlates with anaphylaxis severity. How well PAF correlates with severity relative to histamine or tryptase is not known. To analyze the levels of PAF, histamine, and tryptase as a function of severity
T J Smith et al.
The Journal of biological chemistry, 259(17), 11046-11051 (1984-09-10)
Human lung tryptase, a mast cell-derived trypsin-like serine protease, has been isolated from whole human lung tissue obtained at autopsy. Increased yields from this purification process have allowed extensive characterization of the enzyme. One of the critical steps in the
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What is the extinction coefficient (E1%) of product T7063, Tryptase from human lung?
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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.
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