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Western blot analysis of Caspase-2 on Jurkat cell lysate. Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of anti-Caspase-2.
Immunofluorescent staining of FHS cells.
BD Transduction Laboratories™ Purified Mouse Anti-Caspase-2
BD Transduction Laboratories™ Purified Mouse Anti-Caspase-2
Regulatory Statusの凡例
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
推奨アッセイ手順
Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml.
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.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Caspase-2/ICH-1 is related to the C. elegans cell death gene product CED-3 and its mammalian homologue interleukin-1β-converting enzyme (ICE). Caspase-2 /ICH-1 was identified from a mouse cDNA library and originally termed NEDD-2. The NEDD-2 mRNA was found to be expressed during early mouse embryonic brain development and subsequently down-regulated in adult neuronal tissue. With the identification of the human NEDD-2 gene, the murine gene was renamed Ich-1 to symbolize Ice and ced-3 homology. Caspase-2/ICH-1 mRNA is alternatively spliced. The larger mRNA species encoding a product of 435 amino acids is known as Caspase-2 long, or ICH-1L. The smaller mRNA species encoding a protein of 312 amino acids is named Caspase-2 short, or ICH-1S. Overexpression of ICH-1L induces apoptosis, while over-expression of Ich-1S suppresses Rat-1 cell death induced by serum deprivation. Thus, it appears that Caspase-2/ICH-1 plays an important dual role in programmed cell death.
Development References (5)
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Guo Y, Srinivasula SM, Druilhe A, Fernandes-Alnemri T, Alnemri ES. Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria. J Biol Chem. 2002; 277(16):13430-13437. (Clone-specific: Western blot). View Reference
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Li J, Chen P, Sinogeeva N, et al. Arsenic trioxide promotes histone H3 phosphoacetylation at the chromatin of CASPASE-10 in acute promyelocytic leukemia cells. J Biol Chem. 2002; 277(51):49504-49510. (Clone-specific: Flow cytometry, Western blot). View Reference
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Mancini M, Machamer CE, Roy S. Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during apoptosis. J Cell Biol. 2000; 149(3):603-612. (Clone-specific: Immunofluorescence). View Reference
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Shibata M, Hisahara S, Hara H. Caspases determine the vulnerability of oligodendrocytes in the ischemic brain. J Clin Invest. 2000; 106(5):643-653. (Clone-specific: Western blot). View Reference
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Wang L, Miura M, Bergeron L, Zhu H, Yuan J. Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death. Cell. 1994; 78(5):739-750. (Biology). View Reference
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