Anti-RIP/RIPK1 Antibody Picoband® Fluoro488 Conjugated

RIPK1 (Regulator of G Protein Signaling 3), also called RIP, is an enzyme that in humans is encoded by the RIPK1 gene. Members of the TRAF protein family have been implicated in the activation of NF-kappa-B by the TNF superfamily. By yeast 2-hybrid and coimmunoprecipitation studies using mammalian cell extracts, Hsu et al. (1996) showed that RIP interacts with TRADD, TRAF1, TRAF2, and TRAF3. Hartz (2012) mapped the RIPK1 gene to chromosome 6p25.2 based on an alignment of the RIPK1 sequence with the genomic sequence. Stanger et al. (1995) found that overexpression of Rip in mammalian cells induced morphologic changes characteristic of apoptosis. They suggested that RIP may be an important element in the signal transduction machinery that mediates programmed cell death.

Receptor-interacting serine/threonine-protein kinase 1;2.7.11.1; Cell death protein RIP; Receptor-interacting protein 1; RIP-1; Serine/threonine-protein kinase RIP; RIPK1; RIP, RIP1

Detected in embryos from E8.5-16.5 in cortical ventricular zone, dorsal root ganglia and cerebellar primordia. Isoform 3 is detected in testis and in spermatocytes from newborn mice. Levels increase and reach a maximum after 21 days; after this they decrease again. Long isoforms are widely expressed. .

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. .

1. Hartz, P. A. Personal Communication. Baltimore, Md. 10/26/2012. 2. Hsu, H., Huang, J., Shu, H.-B., Baichwal, V., Goeddel, D. V. TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity 4: 387-396, 1996. 3. Stanger, B. Z., Leder, P., Lee, T.-H., 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 81: 513-523, 1995.