Detects both the pro and active forms of human Granzyme H in direct ELISAs and Western blots. In direct ELISAs, approximately 25% cross‑reactivity with recombinant human Granzyme B is observed and approximately 5% cross-reactivity with recombinant mouse (rm) Granzyme C, rmGranzyme D, and rmGranzyme G is observed.
Polyclonal Goat IgG
Mouse myeloma cell line NS0-derived recombinant human Granzyme H Glu19-Leu246 Accession # P20718
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Granzyme H in Human PBMCs.
Granzyme H was detected in immersion fixed human peripheral blood mononuclear cells (PBMCs) using Goat Anti-Human Granzyme H Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF1377) at 5 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Streptavidin (red; Catalog # NL999) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm. View our protocol for Fluorescent ICC Staining of Non-adherent Cells.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Granzyme H
Granzyme H is a member of the granzyme family of serine proteases found specifically in the cytotoxic granules of cytotoxic T lymphocytes (CTL) and natural killer (NK) cells (1, 2). Granzyme H’s functions are largely unknown. The more abundant expression of Granzyme H than Granzyme B in NK cells suggests that Granzyme H may complement the pro-apoptotic function of Granzyme B in this cell type (3). Human Granzyme H shows the highest amino acid identity (71%) to mouse Granzyme C (4). Human Granzyme H is synthesized as a precursor (246 residues) with a signal peptide (residues 1‑18), a propeptide (residues 19‑20) and a mature chain (residues 21‑246) (5‑7). The pro-enzyme is expressed and purified. After being activated by active cathepsin C, rhGranzyme H cleaves a thioester substrate, which was described previously (8).
Kam, C.-M. et al. (2000) Biochim. Biophys. Acta 1477:307.
Smyth, M.J. et al. (1996) J. Leukoc. Biol. 60:555.
Sedelies, K.A. et al. (2004) J. Biol. Chem. 279:26581.
Sattar, R. et al. (2003) Biochem. Biophys. Res. Comm. 308:726.
Meier, M. et al. (1990) Biochemistry 29:4042.
Haddad, P. et al. (1991) Int. Immunol. 3:57.
Klein, J.L. et al. (1990) Tissue Antigens 35:220.
Edwards, K.M. et al. (1999) J. Biol. Chem. 274:30468.
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