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Purified Mouse Anti-Human Caspase-9
Purified Mouse Anti-Human Caspase-9

Western blot analysis of caspase-9. Lysates from control (lanes 1-3) and amptothecin treated Jurkat cells (lanes 4-6) were probed with anti-human caspase-9 (clone 2-22, Cat. No. 551247) at concentrations of: 1.0 (lane 1), 0.5 (lane 2), and 0.25 µg/ml (lane 3). Caspase-9 is identified as a band of 47 kDa (proform), and 37 kDa (intermediate) in treated cells, and the 47 kDa band in control cells.

Purified Mouse Anti-Human Caspase-9

(+) = positive, (-) = negative, (NT) = not tested

Western blot analysis of caspase-9. Lysates from control (lanes 1-3) and amptothecin treated Jurkat cells (lanes 4-6) were probed with anti-human caspase-9 (clone 2-22, Cat. No. 551247) at concentrations of: 1.0 (lane 1), 0.5 (lane 2), and 0.25 µg/ml (lane 3). Caspase-9 is identified as a band of 47 kDa (proform), and 37 kDa (intermediate) in treated cells, and the 47 kDa band in control cells.

(+) = positive, (-) = negative, (NT) = not tested

Product Details
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BD Pharmingen™
ICE-LAP-6, Mch6, Apaf-3
Human (QC Testing)
Mouse IgG1, κ
Human caspase-9 N-terminal fragment aa 1-134
Western blot (Routinely Tested)
47, 37 kDa
0.5 mg/ml
AB_394119
Aqueous buffered solution containing ≤0.09% sodium azide.
RUO


Preparation And Storage

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

Recommended Assay Procedures

Applications include western blot analysis (0.5 - 1.0 µg/ml). Jurkat cells (ATCC TIB-152) are suggested as a positive control. BD Biosciences Pharmingen offers several caspase-9 antibodies. A Jurkat model cell system was used to evaluate these antibodies; these results are summarized in the following table. However, actual bands observed could vary according to the cell model system or treatment used.

Product Notices

  1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  2. Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
  3. 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.
551247 Rev. 3
Antibody Details
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2-22

The caspase family of cysteine proteases plays a key role in apoptosis and inflammation. Caspases are synthesized as inactive proenzymes containing three domains, that are processed into large and small subunits that associate to form the active enzyme. Processing can occur in apoptotic cells by either transactivation, self-proteolysis or cleavage by another protease. While caspases share a common structure, there are some differences, such as the preferred substrate specificity. These sequence differences in specificity, as well as the size of the NH2 -terminal prodomain, can be used to catagorize the caspases into functional groups including apoptotic initiators (long prodomains), apoptotic executioners (short prodomains), and cytokine processors.  Caspase-9 is a member of the apoptotic initiator group of caspases which include caspases-2, -8, and -10. Activation of caspase-9 occurs in the presence of cytochrome c, following an interaction between caspase-9 and APAF-1. Activation may also be triggered directly by the cytotoxic T-cell protease, granzyme B. Active caspase-9 cleaves and thus activates caspase-3, and is also a relevant target of active caspase-3. Caspase-9 can also cleave the nuclear protein PARP. Northern blot analysis suggests that high expression of caspase-9 is found in the heart, testis, and ovary. The antibody recognizes  the 47 kDa proform and 37 kDa cleaved form of human caspase-9. The N-terminal fragment (amino acids 1-134) of human caspase-9 was used as an immunogen.

551247 Rev. 3
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
551247 Rev.3
Citations & References
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Development References (6)

  1. Cohen GM. Caspases: the executioners of apoptosis. Biochem J. 1997; 326(1):1-16. (Biology). View Reference
  2. Duan H, Chinnaiyan AM, Hudson PL, Wing JP, He WW, Dixit VM. ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis. J Biol Chem. 1996; 271(3):1621-1625. (Biology). View Reference
  3. Li P, Nijhawan D, Budihardjo I, et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell. 1997; 91(4):479-489. (Biology). View Reference
  4. Srinivasula SM, Fernandes-Alnemri T, et al. The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32. J Biol Chem. 1996; 271(43):27099-27106. (Biology). View Reference
  5. Thornberry NA, Rano TA, Peterson EP, et al. A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis. J Biol Chem. 1997; 272(29):17907-17911. (Biology). View Reference
  6. Wolf BB, Green DR. Suicidal tendencies: apoptotic cell death by caspase family proteinases. J Biol Chem. 1999; 274(29):20049-20052. (Biology). View Reference
View All (6) View Less
551247 Rev. 3

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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.