| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:2000 |
| IHC | 1:50-1:200 |
| FC | 1:50-1:200 |
Granzyme B is a serine protease that plays a central role in immune-mediated cell death, functioning as a key effector molecule released by cytotoxic T lymphocytes and natural killer cells. Upon delivery into target cells, this enzyme initiates apoptosis through both caspase-dependent and caspase-independent pathways, making it an essential marker for studying cytotoxic immune responses, tumor immunology, and inflammatory conditions.
This recombinant monoclonal antibody against human Granzyme B offers the consistency and reliability that demanding experimental workflows require. Produced using recombinant technology with a defined sequence, this antibody eliminates the lot-to-lot variability often encountered with traditional hybridoma-derived reagents, ensuring reproducible results across extended studies and multi-site collaborations.
Validation across multiple platforms demonstrates the versatility of this antibody for diverse experimental approaches. Western blot analysis of K562 whole cell lysate reveals a clean band at approximately 28 kDa, closely matching the predicted molecular weight of 27.7 kDa and confirming specific target recognition. Immunohistochemical staining in paraffin-embedded human tonsil tissue shows clear detection of Granzyme B-positive cells, providing researchers with a reliable tool for examining cytotoxic cell infiltration in tissue sections. Flow cytometry analysis using THP-1 cells demonstrates distinct positive signal separation from isotype controls, enabling quantitative assessment of intracellular Granzyme B expression in cell populations.
Whether investigating tumor-infiltrating lymphocyte activity, characterizing immune cell phenotypes, or examining cytotoxic mechanisms in disease models, this antibody provides the specificity and application flexibility needed for immunology and cell biology research focused on understanding immune effector function.
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