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Western blot analysis of RIP2/RICK on human endothelial cell lysate. Lane 1: 1:500, lane 2: 1:1000, lane 3: 1:2000 dilution of anti-RIP2/RICK.
Immunofluorescent staining of HeLa cells.
BD Pharmingen™ Purified Mouse Anti-RIP2/RICK
BD Pharmingen™ Purified Mouse Anti-RIP2/RICK
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
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.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
- 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.
Acute promyelocytic leukemia (APL) is characterized by the translocation of the retinoic acid receptor (RAR) gene on chromosome 17q21 with the promyelocytic leukemia (PML) gene on chromosome 15q22, resulting in t(15;17). The chimeric PML-RARα receptor protein retains essential functional domains encoded by the two genes. PML-RARα blocks cellular differentiation, thereby inducing leukemogenesis. All-trans-retinoic acid (ATRA) induces differentiation of APL cells. It is thought that ATRA promotes PML-RARα degredation which allows differentiation to progress. ATRA-induced differentiation of APL cells involves the coordinated regulation of many genes. NB4, a cell line derived from an APL patient, expresses RIG-G (Retinoic acid Induced Gene G) protein following treatment with ATRA or IFN-α. RIG-G displays strong homology to the protein products of the IFN-stimulated gene (ISG) family and contains multiple sites for post-translational modification. However, these sites remain to be fully characterized. Thus, RIG-G may be a component of ATRA and IFN signaling pathways that mediate cellular differentiation and the avoidance of leukemogenesis.
Development References (4)
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Inohara N, Koseki T, Lin J. An induced proximity model for NF-kappa B activation in the Nod1/RICK and RIP signaling pathways. J Biol Chem. 2000; 275(36):27823-27831. (Biology). View Reference
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Inohara N, del Peso L, Koseki T, Chen S, Nunez G. RICK, a novel protein kinase containing a caspase recruitment domain, interacts with CLARP and regulates CD95-mediated apoptosis. J Biol Chem. 1998; 273(20):12296-12300. (Biology). View Reference
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McCarthy JV, Ni J, Dixit VM. RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase. J Biol Chem. 1998; 273(27):16968-16975. (Biology). View Reference
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Navas TA, Baldwin DT, Stewart TA. RIP2 is a Raf1-activated mitogen-activated protein kinase kinase. J Biol Chem. 1999; 274(47):33684-33690. (Biology). View Reference
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For Research Use Only. Not for use in diagnostic or therapeutic procedures.