Granzyme H Proteins, Antibodies, cDNA Clones Research Reagents

All Granzyme H reagents are produced in house and quality controlled, including 2 Granzyme H Antibody, 13 Granzyme H Gene, 1 Granzyme H Lysate, 1 Granzyme H Protein, 1 Granzyme H qPCR. All Granzyme H reagents are ready to use.

Granzyme H Protein (1)

    Granzyme H Antibody (2)

      Granzyme H cDNA Clone (13)


      Granzyme H qPCR Primer (1)

      Granzyme H Lysate (1)

        Granzyme H Background

        Granzymes are key components of the immune response that play important roles in eliminating host cells infected by intracellular pathogens. Several granzymes are potent inducers of cell death. A total of eight granzymes (A-G and M) have been identified in the mouse, but only five are known in humans (A, B, H, M and granzyme 3), and granzyme H appears to be specifically human. Human granzyme H is a neutral serine protease that is expressed predominantly in the lymphokine-activated killer (LAK)/natural?killer (NK) compartment of the immune system. In adenovirus-infected cells in which granzyme B (gzmB) and downstream apoptosis pathways are inhibited, granzyme H directly cleaves the adenovirus DNA-binding protein (DBP), a viral component absolutely required for viral DNA replication. This virus demonstrated that gzmH directly induces an important decay in viral DNA replication. Interestingly, gzmH also cleaves the adenovirus 1K assembly protein, a major inhibitor of gzmB, and relieves gzmB inhibition. Granzyme H has a very high amino acid identity (>9%) with many portions of the granzyme B sequence, particularly near the amino terminus of the molecule despite performing a distinct enzymic function.

        Granzyme H References

        • Meier M., et al.,(1990), Cloning of a gene that encodes a new member of the human cytotoxic cell protease family. Biochemistry 29:4042-4049.
        • Haddad P., et al., (1991), Structure and evolutionary origin of the human granzyme H gene.Int. Immunol. 3:57-66.
        • Klein J.L., et al.,(1990), Characterization of a novel, human cytotoxic lymphocyte-specific serine protease cDNA clone (CSP-C).Tissue Antigens 35:220-228.

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