|Detection of Human Granzyme B by Western Blot. Western blot shows lysate of NK‑92 human natural killer lymphoma cell line. PVDF membrane was probed with 0.5 µg/mL of Mouse Anti-Human Granzyme B Monoclonal Antibody (Catalog # MAB2906) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018). A specific band was detected for Granzyme B at approximately 32-35 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
|Granzyme B in Human PBMCs. Granzyme B was detected in immersion fixed human peripheral blood mononuclear cells (PBMCs) using Mouse Anti-Human Granzyme B Monoclonal Antibody (Catalog # MAB2906) at 8 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Mouse IgG Secondary Antibody (red; Catalog # NL007) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm. View our protocol for Fluorescent ICC Staining of Non-adherent Cells.|
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).
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