Detects mouse Granzyme B in ELISAs and Western blots. In sandwich immunoassays, less than 1% cross-reactivity with recombinant human (rh) Granzyme A, rhGranzyme B, recombinant mouse (rm) Granzyme D, rmGranzyme G, and rhGranzyme H is observed.
Polyclonal Goat IgG
Mouse myeloma cell line NS0-derived recombinant mouse Granzyme B Lys17-Ser247 Accession # P04187
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Granzyme B in Mouse Spleen. Granzyme B was detected in immersion fixed frozen sections of mouse spleen using Goat Anti-Mouse Granzyme B Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF1865) at 15 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). View our protocol for Chromogenic IHC Staining of Frozen Tissue Sections.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
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 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). Mouse Granzyme B is synthesized as a precursor (247 residues) with a signal and a pro peptide (residues 1-20) and a mature chain (residues 21‑247) (4, 5). The recombinant mouse Granzyme B consisting of residues 17 to 247 was expressed and purified. After activation with cathepsin C, it cleaves a thioester substrate.
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. p. 1549.
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but also provides information about sample types, species, and experimental conditions.
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