Receptor interacting protein kinase 2 (RIP2K) has an N-terminal dual-specificity ser/tyr kinase domain. This gene is a member of the TKL kinase family (tyrosine kinase-like). RIP2K is located on human chromosome 8q21.
Immunogen
The antiserum was produced against synthesized peptide derived from human RIPK2 around the phosphorylation site of Ser176.
Immunogen Range: 146-195
Biochem/physiol Actions
Receptor interacting protein kinase 2 (RIP2K) can act as a new target for anti-inflammatory drugs. This gene participates in multiple nuclear factor-κB (NFκB) activation pathways and human colon tumorigenesis.
Features and Benefits
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Physical form
Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Genetics of inflammasome-associated disorders: a lesson in the guiding principals of inflammasome function
Rodrigue-Gervais IG and Saleh M
European Journal of Immunology, 40(3), 643-648 (2010)
Structures of the inactive and active states of RIP2 kinase inform on the mechanism of activation
Pellegrini E, et al.
PLoS ONE, 12(5) (2017)
Receptor-interacting protein 2 (RIP2) gene polymorphisms are associated with increased risk of subclinical atherosclerosis and clinical and metabolic parameters. The Genetics of Atherosclerotic Disease (GEA) Mexican study
Posadas-Sanchez R, et al.
Experimental and Molecular Pathology, 102(1), 1-6 (2017)
Cytosolic innate immune sensing is critical for protecting barrier tissues. NOD1 and NOD2 are cytosolic sensors of small peptidoglycan fragments (muropeptides) derived from the bacterial cell wall. These muropeptides enter cells, especially epithelial cells, through unclear mechanisms. We previously implicated
The role of nucleotide-binding oligomerization domain 2 (NOD2) in foot-and-mouth disease virus (FMDV)-infected cells remains unknown. Here, we showed that FMDV infection activated NOD2-mediated beta interferon (IFN-β) and nuclear factor-κB (NF-ĸB) signaling pathways. NOD2 inhibited FMDV replication in the infected
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