Tryptase, Beta1 Mouse Active Protein

Recombinant mouse

Mouse

Supplied in a 0.2um sterile-filtered solution of 25mM Tris, 10mM CaCl2, 0.15M sodium chloride, pH 7.5.

Highly Purified
95%, as determined by SDS-PAGE and visualized by silver stain.

Stable for up to twelve months at -70 degree C from the date of receipt. The protein can be aliquoted and stored at -20 degree to -70 degree C in a manual defrost freezer for six months without a significant loss of activity. Avoid repeated freeze-thaw cycles.
Tryptase beta-1 (Mast Cell Protease 7) is a serine protease with trypsin-like activity. It is storedin the secretory granules of mouse mast cells. It exhibits anticoagulant activity due to its ability to degrade fibrinogen in the presence of the diverse array of protease inhibitors in plasma. The deduced amino acid sequence consists of a signal peptide (residues 1-18), a pro region (residues 19-28) and the mature chain (residue 29-273). The mature chain was expressed and purified.

The purified, secreted recombinant, murineTryptase beta-1 corresponds to the mature form with the N-terminal sequence of I29VGGQEAHGN. By SDS-PAGE, the protein migrates as the doublet with apparent molecular masses of approximately 37 and 36kD.

Protein activity can be an ambiguous term. Please refer to the data sheet or inquire with Technical Support to determine the definition of activity for this product.

Measured by its ability to cleave a peptide substrate, Benzyloxcarbonyl-Lys-Thiobenzyl ester (Z-K-SBzl), in the presence of 5,5'-Dithio-bis (1-nitrobenzoic acid) (DTNB), as measured by
absorbance at 405nm and using the extinction coefficient of 13,260 M-1cm-1.2. The specific activity, measured with 100uM Z-K-SBzl and 500ng enzyme in 100ul of 50mM MES, pH 6.5 containing 0.1mM DTNB atRT, is 200pmoles/min/ug.

1EU/1ug of the protein as determined by the LAL method.

Molecular Biology; MB-Enzymes; Proteinase