Mouse plasmin

Activity according to the lot
MW(Da) : 83 000
Extinction coef. : 17
Isoelectric point: 6.7-8.3
Structure: 2 subunits (MW 57,000 and 26,000 Da), linked by a disulfide bridge, 5 kringles domains, 22 disulfide bridges and an N-terminal lysine.

The vast majority of enzymes is pure (without additives) with > 95% purity SDS-PAGE.
Expiration date of one year from delivery.
Delivery in large quantities.
Discount according to quantities.

An enzyme is a protein that catalyzes a biochemical reaction. It converts a substrate into a product. Each enzyme has a structure adapted to its function and its activity is dependent on an optimum temperature and pH.
Plasmin is the active form of plasminogen.
Plasmin is a serine protease which catalyzes the hydrolysis of the peptide bonds located preferentially after a lysine residue or an arginine residue. Plasmin has a greater selectivity than trypsin.