Western blot analysis of RIP on a human endothelial cell lysate. Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of the mouse anti-RIP antibody.
Immunofluorescence staining of WI-38 cells (Human lung fibroblasts; ATCC CCL-75).
Western blot analysis of RIP on a human endothelial cell lysate. Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of the mouse anti-RIP antibody.
Immunofluorescence staining of WI-38 cells (Human lung fibroblasts; ATCC CCL-75).
Preparation And Storage
Recommended Assay Procedures
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.
Companion Products
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Binding or cross linking of the Fas antigen (also known as APO-1 and CD95) is known to elicit apoptosis in susceptible cells. Fas is a member of a family of cell surface receptors which includes tumor necrosis factor receptors (TNF-R, and TNF-R2) and nerve growth factor receptors (NGF-R), CD40, OX40, CD30, CD27, and 4-1BB. Several members of this family have been shown to regulate or induce cell death (TNF-R1 and TNF-R2). A 74 kDa member of this family protein named RIP (Receptor Interacting Protein) contains an N-terminal region with homology to protein kinases and a C-terminal region containing a cytoplasmic "death domain" present in both Fas and TNF-R1. Both Fas and RIP have been shown to require this death domain to induce apoptosis and overexpression of RIP has been shown to induce cell death in transfected cells.
Development References (5)
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Devin A, Lin Y, Yamaoka S, Li Z, Karin M, Liu Zg. The alpha and beta subunits of IkappaB kinase (IKK) mediate TRAF2-dependent IKK recruitment to tumor necrosis factor (TNF) receptor 1 in response to TNF. Mol Cell Biol. 2002; 21(12):3986-3994. (Biology: Western blot). View Reference
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Fulda S, Meyer E, Debatin KM. Metabolic inhibitors sensitize for CD95 (APO-1/Fas)-induced apoptosis by down-regulating Fas-associated death domain-like interleukin 1-converting enzyme inhibitory protein expression. Cancer Res. 2000; 60(14):3947-3956. (Biology: Western blot). View Reference
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Lewis J, Devin A, Miller A, et al. Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation. J Biol Chem. 2000; 275(14):10519-10526. (Biology: Immunoprecipitation, Western blot). View Reference
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Stanger BZ, Leder P, Lee TH, Kim E, Seed B. RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death. Cell. 1995; 81(4):513-523. (Biology). View Reference
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Takahashi T, Tanaka M, Brannan CI, et al. Generalized lymphoproliferative disease in mice, caused by a point mutation in the Fas ligand. Cell. 1994; 76(6):969-976. (Biology). View Reference
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