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Western blot analysis of Caspase-4 (TX). Lysates from 293 adenovirus-transformed human kidney cells were probed with anti-Caspase-4 (clone B25-1). The B25-1 antibody identifies Caspase-4 as an ~43 kDa band.


BD Pharmingen™ Purified Mouse Anti-Human Caspase-4

Regulatory Status Legend
Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
Preparation And Storage
Recommended Assay Procedures
Applications include western blot analysis (1-2 µg/ml). Jurkat T cells (ATCC TIB- 152) and 293 adenovirus-transformed human kidney cells (ATCC CRL-1573) are suggested as positive controls.
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- 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.
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Caspase-4 (ICErelII, TX, ICH-2) is a 43 kDa cytosolic protein with homology to the ICE/Ced-3 family of cysteine proteases. Functional similarity with ICE proteases include the ability of Caspase-4 to induce apoptosis when overexpressed. Caspase-4 exhibits protease activity, cleaving both itself and the p30 ICE/caspase-1 proenzyme. However, unlike ICE/caspase-1, caspase-4 displays no IL-1β processing activity. Caspase-4 mRNA is expressed in most adult human tissues, suggesting a broad tissue distribution.
The B25-1 antibody recognizes an ~43 kDa band corresponding to human Caspase-4 (TX). A recombinant human Caspase-4 protein fragment corresponding to amino acids 334-377 was used as immunogen.
Development References (2)
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Faucheu C, Diu A, Chan AW. A novel human protease similar to the interleukin-1 beta converting enzyme induces apoptosis in transfected cells. EMBO J. 1995; 14(9):1914-1922. (Biology). View Reference
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Munday NA, Vaillancourt JP, Ali A. Molecular cloning and pro-apoptotic activity of ICErelII and ICErelIII, members of the ICE/CED-3 family of cysteine proteases. J Biol Chem. 1995; 270(26):15870-15876. (Biology). View Reference
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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.
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