Detects human Granzyme B in direct ELISAs and Western blots. Does not cross-react with recombinant human (rh) Granzyme A, rhGranzyme H, recombinant mouse (rm) Granzyme B, rmGranzyme C, rmGranzyme D, or rmGranzyme G.
Monoclonal Mouse IgG2A Clone # 351927
Protein A or G purified from hybridoma culture supernatant
Mouse myeloma cell line NS0-derived recombinant human Granzyme B Gly19-Tyr247 Accession # P10144
Supplied in a saline solution containing BSA and Sodium Azide.
Detection of Granzyme B in NK‑92 Human Cell Line by Flow Cytometry.
NK‑92 human natural killer lymphoma cell line was stained with Mouse Anti-Human Granzyme B Alexa Fluor® 488‑conjugated Monoclonal Antibody (Catalog # IC2906G, filled histogram) or isotype control antibody (Catalog # IC003G, open histogram). To facilitate intracellular staining, cells were fixed with Flow Cytometry Fixation Buffer (Catalog # FC004) and permeabilized with Flow Cytometry Permeabilization/Wash Buffer I (Catalog # FC005). View our protocol for Staining Intracellular Molecules.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze.
12 months from date of receipt, 2 to 8 °C as supplied.
Background: Granzyme B
Granzyme B is a member of the granzyme family of the serine proteases found specifically in the cytotoxic granules of cytotoxic T lymphocytes (CTL) and natural killer (NK) cells (1, 2). Granzyme B plays an essential role in granule-mediated apoptosis and may have additional roles in rheumatoid arthritis and in bacterial and viral infections (3). It activates various caspases and cleaves proteins such as aggrecan (3). Human Granzyme B 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) (4-6). The recombinant human (rh) Granzyme B consisting of residues 19-247 was expressed and purified. After being activated by active cathepsin C, rhGranzyme B cleaves a thioester substrate described previously (3).
Kam, C-M. et al. (2000) Biochim. Biophys. Acta 1477:307.
Smyth, M.J. et al. (1996) J. Leukoc. Biol. 60:555.
Froelich, C.J. (2004) in Handbook of Proteolytic Enzymes, Barrett, A.J. et al., eds., pp. 1549 - 1552.
Schmid, J. and C. Weissman (1987) J. Immunol. 139:250.
Caputo, A. et al. (1988) J. Biol. Chem. 263:6363.
Trapani, J.A. et al. (1988) Proc. Natl. Acad. Sci. USA 85:6924.
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