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The protein encoded by GZMH is a member of the granzyme family. Additionally we are shipping Granzyme H (Cathepsin G-Like 2, Protein H-CCPX) Antibodies (31) and Granzyme H (Cathepsin G-Like 2, Protein H-CCPX) Kits (8) and many more products for this protein.
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Granzyme H did directly process DFF45 (show DFFA Proteins), potentially leading to DNA damage.
Upon reactive center loop cleavage at Phe-343,SERPINB1 (show SERPINB1 Proteins) covalently complexes with GzmH. SERPINB1 (show SERPINB1 Proteins) overexpression suppresses GzmH- or LAK (show ARL4C Proteins) cell-mediated cytotoxicity. Crystal structures show possible conformational changes in GzmH for the suicide inhibition.
An unusual RKR (show CACNA1A Proteins) motif (Arg39-Lys40-Arg41), conserved only in GzmH, helps define the S3' and S4' binding regions, indicating the preference for acidic residues at the P3' and P4' sites.
GzmH suppresses viral replication through association with the hepatitis B virus x protein.
Granzyme C rapidly induces target cell death by attacking nuclear and mitochondrial targets and that these targets are distinct from those used by granzyme B to cause classical apoptosis.
granzyme H complements the pro-apoptotic function of granzyme B in human NK cells
Granzyme H destroys the function of critical adenoviral proteins required for viral DNA replication and granzyme B inhibition.
Expression levels of GzmH in naive natural killer cells and its killing ability support the role of the protease in triggering an alternative cell-death pathway in innate immunity.
GzmH may play an essential role in caspase-dependent pathogen clearance in the innate immunity that may complement the proapoptotic function of GzmB in human NK cells.
Granzyme H could have evolved a proteolytic specificity that both interferes directly with adenovirus replication and prevents the virus from blocking the potent pro-apoptotic activity of granzyme B.
The protein encoded by this gene is a member of the granzyme family. Members of this family are highly conserved serine proteases that eliminate transformed cells and virus-infected cells. This protein, which has chymotrypsin-like activity, has a preference for bulky aromatic amino acids at the P1 position and for acidic residues at the P3' and P4' positions. This protein is reported to be constitutively expressed in NK cells and may play a role in the cytotoxic arm of the innate immune response by inducing target cell death and by directly cleaving substrates in pathogen-infected cells. Alternative splicing results in multiple transcript variants that encode different protein isoforms.
, cytotoxic T-lymphocyte proteinase
, cytotoxic T-lymphocyte-associated serine esterase 1
, cytotoxin serine protease-C