R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
RIP (D94C12) XP® Rabbit mAb (Biotinylated) #45726
Filter:
- WB
Supporting Data
| REACTIVITY | H M R Hm Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 78 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Hm-Hamster
- Mk-Monkey
Product Information
Product Description
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated RIP (D94C12) XP® Rabbit mAb #3493.
| MW (kDa) | 78 |
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Supplied in 136 mM NaCl, 2.6 mM KCI, 12 mM sodium phosphate (pH 7.4) dibasic, 2 mg/ml BSA, and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
RIP (D94C12) XP® Rabbit mAb (Biotinylated) detects endogenous levels of total RIP (RIP1) protein. It has not been shown to cross-react with other RIP family members.
Species Reactivity:
Human, Mouse, Rat, Hamster, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu190 of human RIP.
Background
The receptor-interacting protein (RIP) family of serine-threonine kinases (RIP, RIP2, RIP3, and RIP4) are important regulators of cellular stress that 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 recruitment to TNF-R1 through interaction with TRADD (2,3). RIP-deficient cells show a failure in TNF-mediated NF-κB activation, making the cells more sensitive to apoptosis (4,5). RIP also interacts with TNF-receptor-associated factors (TRAFs) and can recruit IKKs to the TNF-R1 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 RIP death domain can trigger the apoptotic activity of RIP (8).
- 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.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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