Human Granzyme B DuoSet ELISA, 5 Plate

As one of the five Granzymes (A, B, H, K and M) identified in the human genome, Granzyme B (32kDa) (5) is the most widely researched in terms of its biological function and its utility in health and disease (4). It is synthesized as a precursor (247 residues) with a signal peptide (residues 1-18), a pro-peptide (residues 19-20), and a mature chain (residues 21-247) (6-8). Once inside granules, Granzyme B is fully processed into the mature chain and becomes an active protease when the pro-peptide, Gly-Glu is removed from the N-terminus by cleavage with Cathepsin C (9). The protease activity of Granzyme B is tightly controlled by Serpin B9/ Protease Inhibitor 9 (9). The amino acid sequence of human Granzyme B is 71%, 69%, and 68% identical to its canine, rat, and mouse counterparts, respectively. 

Granzymes have been shown to modulate inflammation, and Granzyme B plasma levels have been found higher with atopic dermatitis and psoriasis when compared to healthy controls. This is in contrast to Granzyme A plasma levels which remain unchanged (10). Serum from patients with Crohn's disease have significantly higher Granzyme B levels than controls (11).