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RIPK1 Antibody (N-term) Blocking peptide

Synthetic peptide

     
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Product Information
Primary Accession Q13546
Clone Names 100430226
Additional Information
Gene ID 8737
Other Names Receptor-interacting serine/threonine-protein kinase 1, Cell death protein RIP, Receptor-interacting protein 1, RIP-1, Serine/threonine-protein kinase RIP, RIPK1, RIP, RIP1
Target/Specificity The synthetic peptide sequence used to generate the antibody AP13893a was selected from the N-term region of RIPK1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Format Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name RIPK1 (HGNC:10019)
Function Serine-threonine kinase which is a key regulator of TNF- mediated apoptosis, necroptosis and inflammatory pathways (PubMed:32657447, PubMed:31827280, PubMed:31827281, PubMed:17703191, PubMed:24144979). Exhibits kinase activity-dependent functions that regulate cell death and kinase-independent scaffold functions regulating inflammatory signaling and cell survival (PubMed:11101870, PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Has kinase-independent scaffold functions: upon binding of TNF to TNFR1, RIPK1 is recruited to the TNF-R1 signaling complex (TNF-RSC also known as complex I) where it acts as a scaffold protein promoting cell survival, in part, by activating the canonical NF-kappa-B pathway (By similarity). Kinase activity is essential to regulate necroptosis and apoptosis, two parallel forms of cell death: upon activation of its protein kinase activity, regulates assembly of two death-inducing complexes, namely complex IIa (RIPK1-FADD-CASP8), which drives apoptosis, and the complex IIb (RIPK1-RIPK3-MLKL), which drives necroptosis (By similarity). RIPK1 is required to limit CASP8-dependent TNFR1-induced apoptosis (By similarity). In normal conditions, RIPK1 acts as an inhibitor of RIPK3-dependent necroptosis, a process mediated by RIPK3 component of complex IIb, which catalyzes phosphorylation of MLKL upon induction by ZBP1 (PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Inhibits RIPK3-mediated necroptosis via FADD-mediated recruitment of CASP8, which cleaves RIPK1 and limits TNF-induced necroptosis (PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Required to inhibit apoptosis and necroptosis during embryonic development: acts by preventing the interaction of TRADD with FADD thereby limiting aberrant activation of CASP8 (By similarity). In addition to apoptosis and necroptosis, also involved in inflammatory response by promoting transcriptional production of pro-inflammatory cytokines, such as interleukin-6 (IL6) (PubMed:31827280, PubMed:31827281). Phosphorylates RIPK3: RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation (PubMed:19524513). Phosphorylates DAB2IP at 'Ser-728' in a TNF-alpha- dependent manner, and thereby activates the MAP3K5-JNK apoptotic cascade (PubMed:17389591, PubMed:15310755). Required for ZBP1-induced NF-kappa-B activation in response to DNA damage (By similarity).
Cellular Location Cytoplasm {ECO:0000250|UniProtKB:Q60855}. Cell membrane {ECO:0000250|UniProtKB:Q9ZUF4}
Research Areas
Citations (0)
citation

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Background

Essential adapter molecule for the activation of NF-kappa-B. Following different upstream signals (binding of inflammatory cytokines, stimulation of pathogen recognition receptors, or DNA damage), particular RIPK1-containing complexes are formed, initiating a limited number of cellular responses. Upon TNFA stimulation RIPK1 is recruited to a TRADD-TRAF complex initiated by TNFR1 trimerization. There, it is ubiquitinated via 'Lys-63'-link chains, inducing its association with the IKK complex, and its activation through NEMO binding of polyubiquitin chains.

References

Kim, S., et al. Cancer Sci. 101(11):2425-2429(2010)Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)Chae, Y.S., et al. J. Cancer Res. Clin. Oncol. (2010) In press :Couch, F.J., et al. Cancer Epidemiol. Biomarkers Prev. 19(1):251-257(2010)Vandenabeele, P., et al. Sci Signal 3 (115), RE4 (2010) :

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$ 277.78
Cat# BP13893a
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