Skip to content

rabbit anti-RICK (CT) polyclonal antibody 6694


Antibody summary

  • Rabbit polyclonal to RICK (CT)
  • Suitable for: ELISA,WB,ICC,IF
  • Isotype: IgG
  • 100 µg
SKU: 6694parent Category: Tags: , ,
Weight1 lbs
Dimensions9 × 5 × 2 in







1 mg/mL





available sizes

100 µg

Available product – rabbit anti-RICK (CT) polyclonal antibody 6694

Tested applications
Recommended dilutions
Immunoblotting : use at 1-2ug/mL.

Positive control: A431 cell lysate.

Immunocytochemistry: use at 5ug/mL.
Synthetic peptide corresponding to aa 508-522 of human RICK (accession no. AF027706).
Size and concentration
100µg and lot specific
Storage Instructions
This antibody is stable for at least one (1) year at -20°C. Avoid multiple freeze-thaw cycles.
Storage buffer
PBS, pH 7.4.
peptide affinty purifcation
Compatible secondaries
goat anti-rabbit IgG, H&L chain specific, peroxidase conjugated, conjugated polyclonal antibody 9512
goat anti-rabbit IgG, H&L chain specific, biotin conjugated polyclonal antibody 2079
goat anti-rabbit IgG, H&L chain specific, FITC conjugated polyclonal antibody 7863
goat anti-rabbit IgG, H&L chain specific, Cross Absorbed polyclonal antibody 2371
goat anti-rabbit IgG, H&L chain specific, biotin conjugated polyclonal antibody, crossabsorbed 1715
goat anti-rabbit IgG, H&L chain specific, FITC conjugated polyclonal antibody, crossabsorbed 1720
Isotype control
Rabbit polyclonal - Isotype Control
target relevance
Protein names
Receptor-interacting serine/threonine-protein kinase 2 (EC (CARD-containing interleukin-1 beta-converting enzyme-associated kinase) (CARD-containing IL-1 beta ICE-kinase) (RIP-like-interacting CLARP kinase) (Receptor-interacting protein 2) (RIP-2) (Tyrosine-protein kinase RIPK2) (EC
Gene names
Protein family
Protein kinase superfamily, TKL Ser/Thr protein kinase family
FUNCTION: Serine/threonine/tyrosine-protein kinase that plays an essential role in modulation of innate and adaptive immune responses (PubMed:9575181, PubMed:9642260, PubMed:14638696, PubMed:21123652, PubMed:17054981, PubMed:28656966). 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:17562858, PubMed:21123652, PubMed:17054981, 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:29452636, PubMed:28545134, PubMed:30279485, PubMed:30478312, PubMed:30026309). 'Met-1'-linked polyubiquitin chains attached to RIPK2 recruit IKBKG/NEMO, which undergoes 'Lys-63'-linked polyubiquitination in a RIPK2-dependent process (PubMed:22607974, PubMed:17562858, 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). {ECO:0000269|PubMed:14638696, ECO:0000269|PubMed:17054981, ECO:0000269|PubMed:17562858, ECO:0000269|PubMed:18079694, ECO:0000269|PubMed:21123652, ECO:0000269|PubMed:21887730, ECO:0000269|PubMed:22607974, ECO:0000269|PubMed:26646181, ECO:0000269|PubMed:28545134, ECO:0000269|PubMed:28656966, ECO:0000269|PubMed:29452636, ECO:0000269|PubMed:30026309, ECO:0000269|PubMed:30279485, ECO:0000269|PubMed:30478312, ECO:0000269|PubMed:9575181, ECO:0000269|PubMed:9642260}.
Catalytic activity
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=; Evidence={ECO:0000269|PubMed:16824733}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=; CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=; Evidence={ECO:0000255|PROSITE-ProRule:PRU10027, ECO:0000269|PubMed:21123652};
Subellular location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21887730}. Cell membrane {ECO:0000269|PubMed:17355968}; Peripheral membrane protein {ECO:0000305|PubMed:17355968}. Endoplasmic reticulum {ECO:0000269|PubMed:28656966}. Note=Recruited to the cell membrane by NOD2 following stimulation by bacterial peptidoglycans. {ECO:0000269|PubMed:17355968}.
TISSUE SPECIFICITY: Detected in heart, brain, placenta, lung, peripheral blood leukocytes, spleen, kidney, testis, prostate, pancreas and lymph node. {ECO:0000269|PubMed:9575181, ECO:0000269|PubMed:9642260}.
SUBUNIT: Interacts (via CARD domain) with NOD2 (via CARD domain) (PubMed:15044951, PubMed:17355968, PubMed:19592251, PubMed:21887730, PubMed:27812135, PubMed:30279485, PubMed:30478312). Interacts (via CARD domain) with NOD1 (via CARD domain) (PubMed:17054981, PubMed:30478312). Homooligomer; following interaction with NOD1 or NOD2, homooligomerizes via its CARD domain and forms long filaments named RIPosomes (PubMed:30279485, PubMed:30478312). Found in a signaling complex consisting of at least ARHGEF2, NOD2 and RIPK2 (PubMed:21887730). Interacts with ARHGEF2; the interaction mediates tyrosine phosphorylation of RIPK2 by Src kinase CSK (PubMed:21887730). Interacts with MAP3K4; this interaction sequesters RIPK2 from the NOD2 signaling pathway (PubMed:18775659). Interacts with IKBKG/NEMO (PubMed:18079694). The polyubiquitinated protein interacts with MAP3K7/TAK1; interaction is indirect and is mediated by TAB2 and TAB3 that bind to polyubiquitin chains attached to RIPK2 (PubMed:18079694). Binds to CFLAR/CLARP and CASP1 via their CARD domains (PubMed:9575181). Binds to BIRC3/c-IAP1 and BIRC2/c-IAP2, TRAF1, TRAF2, TRAF5 and TRAF6 (PubMed:21931591). Interacts with NLRP10 (PubMed:22672233). Interacts with CARD9 (By similarity). Interacts with INAVA; the interaction takes place upon PRR stimulation (PubMed:28436939). Interacts (via CARD domain) with NGFR (via death domain) (PubMed:26646181). Interacts with IRGM; promoting RIPK2 degradation (PubMed:36221902). {ECO:0000250|UniProtKB:P58801, ECO:0000269|PubMed:15044951, ECO:0000269|PubMed:17054981, ECO:0000269|PubMed:17355968, ECO:0000269|PubMed:18079694, ECO:0000269|PubMed:18775659, ECO:0000269|PubMed:19592251, ECO:0000269|PubMed:21887730, ECO:0000269|PubMed:21931591, ECO:0000269|PubMed:22672233, ECO:0000269|PubMed:26646181, ECO:0000269|PubMed:27812135, ECO:0000269|PubMed:28436939, ECO:0000269|PubMed:30279485, ECO:0000269|PubMed:30478312, ECO:0000269|PubMed:36221902, ECO:0000269|PubMed:9575181}.
Post-translational modification
PTM: 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). {ECO:0000250|UniProtKB:P58801, ECO:0000269|PubMed:18079694, ECO:0000269|PubMed:19464198, ECO:0000269|PubMed:19592251, ECO:0000269|PubMed:21931591, ECO:0000269|PubMed:22607974, ECO:0000269|PubMed:23806334, ECO:0000269|PubMed:28656966, ECO:0000269|PubMed:29452636, ECO:0000269|PubMed:30026309, ECO:0000269|PubMed:36221902}.; PTM: Autophosphorylated (PubMed:16824733, PubMed:21123652, PubMed:29452636, PubMed:28545134). 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). {ECO:0000269|PubMed:16824733, ECO:0000269|PubMed:21123652, ECO:0000269|PubMed:21887730, ECO:0000269|PubMed:27830463, ECO:0000269|PubMed:28545134, ECO:0000269|PubMed:29452636}.; PTM: 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). {ECO:0000269|PubMed:36221902}.; PTM: (Microbial infection) Acetylation of Ser-174, Ser-176 and Ser-178 by Yersinia YopJ prevents phosphorylation and activation, thereby promoting cell death. {ECO:0000269|PubMed:22520462}.
Target Relevance information above includes information from UniProt accession : O43353
The UniProt Consortium


Western blot analysis of RICK in (A) 3T3 and (B) K562 cell lysate with RICK antibody at 0.5 µg/mL
Immunocytochemistry of RICK in K562 cells with RICK antibody at 5 µg/mL.
Immunofluorescence of RICK in K562 cells with RICK antibody at 20 µg/mL.


Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.



relevant to this product
Western blot


No results found


There are no reviews yet.

Only logged in customers who have purchased this product may leave a review.