Product Pathways - NF-kappaB Signaling
RIP Antibody #4926
| Applications | Reactivity | Sensitivity | MW (kDa) | Source |
|---|---|---|---|---|
| W IP IF-IC F | H M R | Endogenous | 78 | Rabbit |
Applications Key:
W=Western Blotting
IP=Immunoprecipitation
IF-IC=Immunofluorescence (Immunocytochemistry)
F=Flow Cytometry
Reactivity Key:
H=Human
M=Mouse
R=Rat
Species cross-reactivity is determined by Western blot.
Specificity / Sensitivity
RIP Antibody detects endogenous levels of RIP protein. No cross-reactivity was detected with other family members. This antibody also detects a carboxy-terminal fragment of RIP (45 kDa) produced by caspase-8 dependent cleavage.
Source / Purification
Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to residues surrounding arginine 413 of human RIP. Antibodies were purified by protein A and peptide affinity chromatography.
Western Blotting
Western blot analysis of extracts from HL-60, MOLT-4 and Raji cell lines, using RIP Antibody.
Flow Cytometry
Flow cytometric analysis of Jurkat cells, using RIP antibody (blue) compared to a nonspecific negative control antibody (red).
IF-IC
Immunofluorescent staining of HeLa cells transfected with RIP showing punctate cytoplasmic staining, using RIP Antibody.
Background
The RIP (receptor-interacting protein) family of serine-threonine kinases (RIP, RIP2, RIP3 and RIP4) are important regulators of cellular stress that can trigger pro-survival and inflammatory responses through the activation of NF-κB as well as pro-apoptotic pathways (1). In addition to the kinase domain, RIP contains a death domain responsible for interaction with the death domain receptor Fas and for the recruitment to TNFR1 through interaction with TRADD (2,3). RIP also interacts with TNF-receptor-associated factors (TRAFs) and can recruit IKKs to the TNFR1 signaling complex via interaction with NEMO leading to IκB phosphorylation and degradation (6,7). Overexpression of RIP induces both NF-κB activation and apoptosis (2,3). Caspase-8 dependent cleavage of the death domain on RIP can trigger the apoptotic activity of RIP (8). RIP-deficient cells show a failure in TNF-mediated NF-κB activation making the cells more sensitive to apoptosis (4,5).
- Meylan, E. and Tschopp, J. (2005) Trends Biochem Sci 30, 151-9.
- Hsu, H. et al. (1996) Immunity 4, 387-96.
- Stanger, B.Z. et al. (1995) Cell 81, 513-23.
- Ting, A.T. et al. (1996) EMBO J 15, 6189-96.
- Kelliher, M.A. et al. (1998) Immunity 8, 297-303.
- Devin, A. et al. (2000) Immunity 12, 419-29.
- Zhang, S.Q. et al. (2000) Immunity 12, 301-11.
- Lin, Y. et al. (1999) Genes Dev 13, 2514-26.
Application References
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This product is for in vitro research use only and is not intended for use in humans or animals. This product is not intended for use as therapeutic or in diagnostic procedures.