Tryptase β11 (human), (recombinant)



BML-SE418-0020	20 µg	221.00 USD

ßII-tryptase, also known as beta-tryptase or tryptase II, is a glycosylated trypsin-like neutral serine endopeptidase. Like the closely-related tryptase-α, -ß1, and -ß3, it forms tetramers that are stored in mast cell secretory granules until release. Its physiological targets include pro-MMP-3, vasoactive intestinal peptide (VIP), and fibronectin. It is believed to be involved in tissue and wound remodeling, and inflammatory and allergic processes, making it a target for drug discovery in these areas.

Product Specification

MW:	~35kDa (under reducing conditions); ~140kDa (tetramer under non-reducing conditions).

Purity:	≥90% (SDS-PAGE)

Formulation:	This preparation does not contain heparin, a poly-negative molecule which can alter assay outcomes or interfere with inhibitors. Stabilized with 2M NaCl in the storage buffer, but dilution will reduce stability. It is recommended that enzyme inhibitor assays be done in the manner of Mecca et al. (see reference). If long incubation times are necessary, heparin (50-100μg/ml final) or dextran sulfate can be added. Also available is substrate Z-GPR-AMC (Prod. No. BML-P142).

Specific Activity:	1000 U/mg, where one unit yields an absorbance change of 1 OD/minute at 410 nm using as substrate 400μM CBZ-L-lysine thiobenzyl ester coupled with 0.5mM DTNB at 25°C.

EC:	3.4.21.59

Source/Host:	Produced in yeast.

Application:	Study enzyme kinetics, cleave target substrates and screen for inhibitors.

Long Term Storage:	-20°C

Use/Stability:	-20°C for at least six months. The enzyme is stable as supplied on ice for at least several days. However, it is recommended that dilution of the enzyme, and its stabilizer NaCl, be done within as short a time as possible before start of the assay. After initial defrost, aliquot product into individual tubes and refreeze at -20°C. It can be freeze/thawed at least 4 times, but avoid repeated freeze/defrost cycles.

Handling:	After opening, prepare aliquots and store at -20°C. Avoid freeze/thaw cycles.

Background / Technical Information:	Please click here for the comprehensive product datasheet.

General Literature References

Mast cell-restricted tryptases: structure and function in inflammation and pathogen defense: H.P. McNeil, et al.; J. Biol. Chem. 282, 20785 (2007), Abstract;

Structural requirements and mechanism for heparin-dependent activation and tetramerization of human betaI- and betaII-tryptase: J. Hallgren, et al.; J. Mol. Biol. 345, 129 (2005), Abstract;

Structure based design of 4-(3-aminomethylphenyl)piperidinyl-1-amides: novel, potent, selective, and orally bioavailable inhibitors of betaII tryptase: J. Levell, et al.; Bioorg. Med. Chem. 13, 2859 (2005), Abstract;

Designed calix[8]arene-based ligands for selective tryptase surface recognition: T. Mecca, et al.; Bioorg. Med. Chem. 12, 5057 (2004), Abstract;

Mast cell tryptase, a still enigmatic enzyme: L. Fiorucci & F. Ascoli; Cell. Mol. Life Sci. 61, 1278 (2004), Abstract;

Definition of the extended substrate specificity determinants for beta-tryptases I and II: J.L. Harris, et al.; J. Biol. Chem. 276, 34941 (2001), Abstract;