Binds to human α-, βI-, βII-, βIII-tryptase isoforms.
Inhibits the catalytic activity of βI-, βII-, and βIII-tryptases (noncompetitive inhibitor).
Isotype: IgG4
Various conjugated forms available upon request.
Summary
Specifications
Antibody Isotype
IgG4
Clone
31A.v11
Species Reactivity
Human
Immunogen
Recombinant human monomeric and tetrameric βI-tryptase
Conjugate
Unconjugated
Applications
Application Notes
ELISA, Inhib, WB, Crystallization Each laboratory should determine an optimum working titer for use in its particular application. Other applications have not been tested but use in such assays should not necessarily be excluded.
General Notes
Clone 31A.v11 is a noncompetitive inhibitory antibody that against human β-tryptase and dissociates active tetramers into inactive monomers. This anti-tryptase antibody potently blocks tryptase enzymatic activity in a humanized mouse model, reducing IgE-mediated systemic anaphylaxis, and inhibits airway tryptase in Ascaris-sensitized cynomolgus monkeys with favorable pharmacokinetics.
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References
An Allosteric Anti-tryptase Antibody for the Treatment of Mast Cell-Mediated Severe Asthma.
Severe asthma patients with low type 2 inflammation derive less clinical benefit from therapies targeting type 2 cytokines and represent an unmet need. We show that mast cell tryptase is elevated in severe asthma patients independent of type 2 biomarker status. Active β-tryptase allele count correlates with blood tryptase levels, and asthma patients carrying more active alleles benefit less from anti-IgE treatment. We generated a noncompetitive inhibitory antibody against human β-tryptase, which dissociates active tetramers into inactive monomers. A 2.15 ? crystal structure of a β-tryptase/antibody complex coupled with biochemical studies reveal the molecular basis for allosteric destabilization of small and large interfaces required for tetramerization. This anti-tryptase antibody potently blocks tryptase enzymatic activity in a humanized mouse model, reducing IgE-mediated systemic anaphylaxis, and inhibits airway tryptase in Ascaris-sensitized cynomolgus monkeys with favorable pharmacokinetics. These data provide a foundation for developing anti-tryptase as a clinical therapy for severe asthma.
COA
Publication 
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