|Application ||IHC-P, E|
|Other Accession||NP_003795, 57242761|
|Calculated MW||Predicted: 74 kDa|
|Application Notes||RIP1 antibody can be used for detection of RIP1 by immunohistochemistry at 5 - 10 µg/mL.|
|Other Names||RIP1 Antibody: RIP, RIP1, RIP, Cell death protein RIP, RIP-1, receptor (TNFRSF)-interacting serine-threonine kinase 1|
|Reconstitution & Storage||RIP1 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year.|
|Precautions||RIP1 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.
RIP1 Antibody: RIP1 (Receptor Interacting Protein), also known as RIPK1, is a crucial 74 kD adaptor kinase in several of stress-induced signaling pathways and on the crossroad of a cell’s decision to live or die. RIP1 contains an N-terminal region with homology to protein kinases, an intermediate domain capable of association with MAPKKK and a C-terminal region containing a death domain motif present in the Fas and TNFR1 intracellular domains. Full length RIP1 is important for signallling to NF-kappa-B, MAPKs and necrosis, whereas caspase-8 generates a C-terminal RIP1 cleavage fragment, promoting TNF-induced apoptosis. It is required for TNFRSF1A-mediated and TLR3-induced NF-kappa-B activation. RIP1-deficient mice fail to thrive, displaying extensive apoptosis in both lymphoid and adipose tissues and dying at 1-3 days of age.
Stanger BZ, Leder P, Lee TH, et al. RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death. Cell 1995; 81:513-23.
Hsu H, Huang J, Shu HB, et al. TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity 1996; 4:387-96.
Meylan E, Burns K, Hofmann K, et al. RIP1 is an essential mediator of Toll-like receptor 3-induced NF-kappa B activation. Nat. Immunol.; 2004; 5:503-7.
Festjens N, Vanden Bergh T, Cornelis S, et al. RIP1, a kinase on the crossroads of a cell's decision to live or die. Cell Death Differ. 2007;14:400-10.
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