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Purified Mouse Anti-Granzyme B
Purified Mouse Anti-Granzyme B
Western blot analysis of Granzyme B.   A NK-92 cell lysate (Human natural killer cells derived from malignant non-Hodgkin's lymphoma donor; ATCC CRL-2407) was probed with the mouse anti-granzyme B antibody at concentrations of 0.125 µg/mL (lane 1), 0.0625 µg/mL (lane 2), and 0.03125 µg/mL (lane 3). Granzyme B is identified at ~32 kDa.
Western blot analysis of Granzyme B.   A NK-92 cell lysate (Human natural killer cells derived from malignant non-Hodgkin's lymphoma donor; ATCC CRL-2407) was probed with the mouse anti-granzyme B antibody at concentrations of 0.125 µg/mL (lane 1), 0.0625 µg/mL (lane 2), and 0.03125 µg/mL (lane 3). Granzyme B is identified at ~32 kDa.
Product Details
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BD Pharmingen™
Human (QC Testing), Rat (Tested in Development)
Mouse IgG2a
Western blot (Routinely Tested)
32 kDa
0.5 mg/ml
AB_393751
Aqueous buffered solution containing ≤0.09% sodium azide.
RUO


Preparation And Storage

Store undiluted at 4°C. The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.

Recommended Assay Procedures

Western blot:  Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml

Product Notices

  1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  2. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
  3. Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
550558 Rev. 5
Antibody Details
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2C5/F5

The primary mechanism by which cytotoxic T cells eliminate virally infected cells is by granule exocytosis. The release of cytotoxic granule contents by cytotoxic T lymphocytes (CTL) triggers apoptotic target cell death. CTL granules contain a poreforming protein, perforin, and a group of serine proteases called granzymes. In the classic model, perforins create holes in the target cell membrane, allowing entrance of the granzymes. Granzyme A and B are the predominant granzymes activated after CTL activation, but each act via an independent apoptotic pathway; granzyme B is activated immediately, while granzyme A acts hours later. The physiological substrates for granzyme A in the apoptotic pathway  have not been identified. Studies involving mice which are deficient in both granzyme A and B suggest a model whereby the granzyme B pathway may have evolved as the major apoptotic pathway with the granzyme A pathway acting as a backup. Granzyme B has been shown to induce apoptosis and to cleave a number of substrates which are similar in specificity to those of the caspase family of proteinases. Granzyme B can cleave substrates, such as DNA-PKcs, and nuclear mitotic apparatus protein (NuMA). Furthermore, Granzyme B can also cleave substrates such as Bid and DFF45 in a caspase-independent fashion. However, further research is needed to delineate the exact role of caspases in cytotoxic T lymphocyte-induced apoptosis involving Granzyme B. Granzyme B migrates at approximately 32 kDa in SDS/PAGE. Clone 2C5/F5 recognizes human and rat granzyme B.

550558 Rev. 5
Format Details
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Purified
Tissue culture supernatant is purified by either protein A/G or affinity purification methods. Both methods yield antibody in solution that is free of most other soluble proteins, lipids, etc. This format provides pure antibody that is suitable for a number of downstream applications including: secondary labeling for flow cytometry or microscopy, ELISA, Western blot, etc.
Purified
550558 Rev.5
Citations & References
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Development References (8)

  1. Andrade F, Roy S, Nicholson D, Thornberry N, Rosen A, Casciola-Rosen L. Granzyme B directly and efficiently cleaves several downstream caspase substrates: implications for CTL-induced apoptosis. Immunity. 1998; 8(4):451-460. (Biology). View Reference
  2. Barry M, Heibein JA, Pinkoski MJ, et al. Granzyme B short-circuits the need for caspase 8 activity during granule-mediated cytotoxic T-lymphocyte killing by directly cleaving Bid. Mol Cell Biol. 2000; 20(11):3781-3794. (Biology). View Reference
  3. Beresford PJ, Xia Z, Greenberg AH, Lieberman J. Granzyme A loading induces rapid cytolysis and a novel form of DNA damage independently of caspase activation. Immunity. 1999; 10(5):585-594. (Biology). View Reference
  4. Pinkoski MJ, Waterhouse NJ, Heibein JA, et al. Granzyme B-mediated apoptosis proceeds predominantly through a Bcl-2-inhibitable mitochondrial pathway. J Biol Chem. 2001; 276(15):12060-12067. (Biology). View Reference
  5. Rotonda J, Garcia-Calvo M, Bull HG, et al. The three-dimensional structure of human granzyme B compared to caspase-3, key mediators of cell death with cleavage specificity for aspartic acid in P1. Chem Biol. 2001; 8(4):357-368. (Biology). View Reference
  6. Sharif-Askari E, Alam A, Rheaume E, et al. Direct cleavage of the human DNA fragmentation factor-45 by granzyme B induces caspase-activated DNase release and DNA fragmentation. EMBO J. 2001; 20(12):3101-3113. (Biology). View Reference
  7. Shresta S, Graubert TA, Thomas DA, Raptis SZ, Ley TJ. Granzyme A initiates an alternative pathway for granule-mediated apoptosis. Immunity. 1999; 10(5):595-605. (Biology). View Reference
  8. Trapani JA, Smyth MJ, Apostolidis VA, Dawson M, and Browne KA. Granule serine proteases are normal nuclear constituents of natural killer cells. J Biol Chem. 1994; 269:18359-18365. (Biology). View Reference
View All (8) View Less
550558 Rev. 5

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Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described


Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims.  Comparisons are not made against non-BD technologies, unless otherwise noted.

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

Refer to manufacturer's instructions for use and related User Manuals and Technical Data Sheets before using this product as described.

Comparisons, where applicable, are made against older BD technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.