CARD-containing interleukin-1 beta-converting enzyme-associated kinase RIP-like-interacting CLARP kinase Receptor-interacting protein 2 Tyrosine-protein kinase RIPK2 EC=220.127.116.11 RIPK2 CARDIAK, RICK, RIP2 UNQ277/PRO314/PRO34092
Recombinant human Receptor-interacting serine/threo nine-protein kinase 2 protein (1-540AA)
ELISA;Not yet tested in other applications.
Background / Function
Serine/threonine/tyrosine kinase that plays an essential role in modulation of innate and adaptive immune responses. Upon stimulation by bacterial peptidoglycans, NOD1 and NOD2 are activated, oligomerize and recruit RIPK2 through CARD-CARD domains. Contributes to the tyrosine phosphorylation of the guanine exchange factor ARHGEF2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. Once recruited, RIPK2 autophosphorylates and undergoes ‘Lys-63’-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3. The polyubiquitinated protein mediates the recruitment of MAP3K7/TAK1 to IKBKG/NEMO and induces ‘Lys-63’-linked polyubiquitination of IKBKG/NEMO and subsequent activation of IKBKB/IKKB. In turn, NF-kappa-B is released from NF-kappa-B inhibitors and translocates into the nucleus where it activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. Plays also a role during engagement of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation.
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze.
Caprylic Acid Ammonium Sulfate Precipitation purified
LiteratureRICK, a novel protein kinase containing a caspase recruitment domain, interacts with CLARP and regulates CD95-mediated apoptosis.Inohara N., del Peso L., Koseki T., Chen S., Nunez G.J. Biol. Chem. 273:12296-12300(1998) RIP2 is a novel NF-kappaB-ac