|Application ||WB, IHC, IP|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||75931 Da|
|Application & Usage||Western blot analysis (2-6 µg/ml), immunoprecipitation and Immunohistochemistry. However, the optimal conditions should be determined individually.|
|Other Names||RIPK1, FLJ39204, Rinp, RIPK1, Receptor interacting protein|
|Formulation||100 µg (0.5 mg/ml) affinity purified rabbit anti-RIP polyclonal antibody in phosphate buffered saline (PBS), pH 7.2, containing 30% glycerol, 0.5% BSA, 0.01% thimerosal.|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||RIP Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Serine-threonine kinase which transduces inflammatory and cell-death signals (programmed necrosis) following death receptors ligation, activation of pathogen recognition receptors (PRRs), and DNA damage. Upon activation of TNFR1 by the TNF-alpha family cytokines, TRADD and TRAF2 are recruited to the receptor. Phosphorylates DAB2IP at 'Ser-728' in a TNF-alpha-dependent manner, and thereby activates the MAP3K5-JNK apoptotic cascade. Ubiquitination by TRAF2 via 'Lys-63'-link chains acts as a critical enhancer of communication with downstream signal transducers in the mitogen-activated protein kinase pathway and the NF-kappa-B pathway, which in turn mediate downstream events including the activation of genes encoding inflammatory molecules. Polyubiquitinated protein binds to IKBKG/NEMO, the regulatory subunit of the IKK complex, a critical event for NF-kappa-B activation. Interaction with other cellular RHIM-containing adapters initiates gene activation and cell death. RIPK1 and RIPK3 association, in particular, forms a necrosis-inducing complex.|
|Cellular Location||Cytoplasm. Cell membrane.|
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Provided below are standard protocols that you may find useful for product applications.
RIP (Receptor Interacting Protein) is a 74 kDa Ser/Thr kinase which interacts with CD95 (Fas/Apo1) receptor and the tumor necrosis factor receptor (TNFR1). It is a cell death domain adapter protein which can bind to the adapter proteins TRADD, RAID, and TRAF2. RIP contains an N-terminal region with homology to protein kinase, an intermediate domain capable of association with MAPKKK and a C-terminal region containing an intracellular death domain motif. RIP activates both p38 MAP kinase and SAPK families. In vitro, RIP induces apoptosis, as well as SAPK/JNK and NF-kB activation. RIP possesses kinase activity as it autophosphorylates itself on serine and threonine residues.
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