Recombinant human RIP2 protein (Active) (GST tag N-Terminus)
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Recombinant human RIP2 protein (Active) (GST tag N-Terminus) is a Human Fragment protein, in the 2 to 299 aa range, expressed in Baculovirus infected Sf9 cells, with >90%, suitable for SDS-PAGE, FuncS.
View Alternative Names
CARDIAK, RICK, RIP2, UNQ277/PRO314/PRO34092, RIPK2, Receptor-interacting serine/threonine-protein kinase 2, CARD-containing interleukin-1 beta-converting enzyme-associated kinase, RIP-like-interacting CLARP kinase, Receptor-interacting protein 2, Tyrosine-protein kinase RIPK2, CARD-containing IL-1 beta ICE-kinase, RIP-2
- FuncS
Supplier Data
Functional Studies - Recombinant human RIP2 protein (Active) (GST tag N-Terminus) (AB271734)
Specific activity of ab271734 was ≥15 pmol/min/μg.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant human RIP2 protein (Active) (GST tag N-Terminus) (AB271734)
SDS-PAGE analysis of ab271734.
Complementary Products
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
RIP2 interacts with key components of the immune signaling network. It forms part of a complex with other proteins like nucleotide-binding oligomerization domain (NOD) proteins influencing immune responses. By binding to NOD1 and NOD2 RIP2 modulates inflammatory signaling pathways leading to the activation of NF-kB and the production of inflammatory cytokines. This protein helps regulate the body's defense against bacterial infections and influences inflammation processes.
Pathways
RIP2 plays an integral role in the NOD-like receptor signaling pathway and is also involved in toll-like receptor signaling. In its pathways RIP2 interacts closely with proteins like IKK complexes and the Tak1 complex orchestrating signaling cascades leading to the activation of NF-kB and MAPK pathways. These pathways are essential for instigating the immune response and managing inflammatory signals highlighting how RIP2 acts as a pivotal mediator in these biological routes.
Specifications
Form
Liquid
Additional notes
Affinity purified.
General info
Function
Serine/threonine/tyrosine-protein kinase that plays an essential role in modulation of innate and adaptive immune responses (PubMed : 14638696, PubMed : 17054981, PubMed : 21123652, PubMed : 28656966, PubMed : 9575181, PubMed : 9642260). Acts as a key effector of NOD1 and NOD2 signaling pathways : upon activation by bacterial peptidoglycans, NOD1 and NOD2 oligomerize and recruit RIPK2 via CARD-CARD domains, leading to the formation of RIPK2 filaments (PubMed : 17054981, PubMed : 17562858, PubMed : 21123652, PubMed : 22607974, PubMed : 28656966, PubMed : 29452636, PubMed : 30026309). Once recruited, RIPK2 autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3, as well as 'Met-1'-linked (linear) polyubiquitination by the LUBAC complex, becoming a scaffolding protein for downstream effectors (PubMed : 22607974, PubMed : 28545134, PubMed : 29452636, PubMed : 30026309, PubMed : 30279485, PubMed : 30478312). 'Met-1'-linked polyubiquitin chains attached to RIPK2 recruit IKBKG/NEMO, which undergoes 'Lys-63'-linked polyubiquitination in a RIPK2-dependent process (PubMed : 17562858, PubMed : 22607974, PubMed : 29452636, PubMed : 30026309). 'Lys-63'-linked polyubiquitin chains attached to RIPK2 serve as docking sites for TAB2 and TAB3 and mediate the recruitment of MAP3K7/TAK1 to IKBKG/NEMO, inducing subsequent activation of IKBKB/IKKB (PubMed : 18079694). 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 (PubMed : 18079694). The protein kinase activity is dispensable for the NOD1 and NOD2 signaling pathways (PubMed : 29452636, PubMed : 30026309). Contributes to the tyrosine phosphorylation of the guanine exchange factor ARHGEF2 through Src tyrosine kinase leading to NF-kappa-B activation by NOD2 (PubMed : 21887730). Also involved in adaptive immunity : plays a role during engagement of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation (PubMed : 14638696). Plays a role in the inactivation of RHOA in response to NGFR signaling (PubMed : 26646181).
Sequence similarities
Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.
Post-translational modifications
Polyubiquitinated via both 'Lys-63'- and 'Met-1'-linked polyubiquitin following recruitment by NOD1 or NOD2, creating docking sites for downstream effectors, triggering activation of the NF-kappa-B and MAP kinases signaling (PubMed:22607974, PubMed:29452636, PubMed:30026309). 'Lys-63'-linked polyubiquitination by XIAP is essential for NOD2 signaling and promotes recruitment of the LUBAC complex (PubMed:22607974, PubMed:29452636, PubMed:30026309). Also polyubiquitinated with 'Lys-63'-linked chains by PELI3, BIRC2/c-IAP1 and BIRC3/c-IAP2 (PubMed:19464198, PubMed:21931591). Ubiquitinated on Lys-209 via 'Lys-63'-linked by ITCH (PubMed:18079694, PubMed:19592251). Undergoes 'Lys-63'-linked deubiquitination by MYSM1 to attenuate NOD2-mediated inflammation and tissue damage (By similarity). Polyubiquitinated with 'Lys-63'-linked chains in response to Shigella infection, promoting its SQSTM1/p62-dependent autophagic degradation (PubMed:36221902). Undergoes 'Met-1'-linked polyubiquitination; the head-to-tail linear polyubiquitination is mediated by the LUBAC complex in response to NOD2 stimulation 'Met-1'-linked polyubiquitination (PubMed:23806334). 'Lys-63'-linked polyubiquitination by XIAP is required for recruimtent of the LUBAC complex and subsequent (PubMed:22607974). Linear polyubiquitination is restricted by FAM105B/otulin, probably to limit NOD2-dependent pro-inflammatory signaling activation of NF-kappa-B (PubMed:23806334). Ubiquitination at Lys-503 by ZNRF4 via 'Lys-48'-linked polyubiquitination promotes RIPK2 degradation by the proteasome; ubiquitination by ZNRF4 takes place during both acute and NOD2 tolerance conditions (PubMed:28656966).. Autophosphorylated (PubMed:16824733, PubMed:21123652, PubMed:28545134, PubMed:29452636). Phosphorylated at Ser-176, either via autophosphorylation or by LRRK2, enhancing activity (PubMed:16824733, PubMed:27830463). Autophosphorylation at Tyr-474 is required for effective NOD2 signaling (PubMed:21123652). Autophosphorylation is however not essential for NOD2 signaling (PubMed:29452636). Phosphorylation at Tyr-381 by Src kinase CSK occurs in a ARHGEF2-dependent manner and is required for NOD2-dependent innate immune activation (PubMed:21887730).. Degraded via selective autophagy following interaction with IRGM (PubMed:36221902). IRGM promotes NOD1/NOD2-RIPK2 RIPosome recruitment to autophagosome membranes (PubMed:36221902). RIPK2 biquitinated via 'Lys-63'-linked chains is then recognized by SQSTM1/p62, leading to the SQSTM1/p62-dependent autophagic degradation of the NOD1/NOD2-RIPK2 RIPosome (PubMed:36221902).. (Microbial infection) Acetylation of Ser-174, Ser-176 and Ser-178 by Yersinia YopJ prevents phosphorylation and activation, thereby promoting cell death.
Target data
Product promise
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