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rabbit anti-Ikk beta polyclonal antibody 4247


Antibody summary

  • Rabbit polyclonal to Ikk beta
  • Suitable for: ELISA,WB,ICC,IF
  • Isotype: IgG
  • 100 µg
SKU: 4247parent Category: Tags: , ,
Weight1 lbs
Dimensions9 × 5 × 2 in







1 mg/mL





available sizes

100 µg

rabbit anti-Ikk beta polyclonal antibody 4247

Tested applications
Recommended dilutions
Immunoblotting: use at 1:500-1:1,000 dilution.

Positive control: Whole cell lysate from Jurkat cells.
Peptide corresponding to aa 662-680 of human IKKb which differs from the corresponding murine sequence by one amino acid.
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
Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC (I-kappa-B kinase 2) (IKK-2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB) (Serine/threonine protein kinase IKBKB) (EC
Gene names
Protein family
Protein kinase superfamily, Ser/Thr protein kinase family, I-kappa-B kinase subfami
FUNCTION: Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484, PubMed:30337470). Acts as a part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation (PubMed:9346484). Phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues (PubMed:9346484, PubMed:20434986, PubMed:20797629, PubMed:21138416). These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome (PubMed:9346484, PubMed:20434986, PubMed:20797629, PubMed:21138416). In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (PubMed:9346484, PubMed:20434986, PubMed:20797629, PubMed:21138416). In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE (PubMed:11297557, PubMed:14673179, PubMed:20410276, PubMed:21138416). IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs (PubMed:11297557, PubMed:20410276, PubMed:21138416). Phosphorylates FOXO3, mediating the TNF-dependent inactivation of this pro-apoptotic transcription factor (PubMed:15084260). Also phosphorylates other substrates including NAA10, NCOA3, BCL10 and IRS1 (PubMed:19716809, PubMed:17213322). Phosphorylates RIPK1 at 'Ser-25' which represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death (By similarity). Phosphorylates the C-terminus of IRF5, stimulating IRF5 homodimerization and translocation into the nucleus (PubMed:25326418). {ECO:0000250|UniProtKB:O88351, ECO:0000269|PubMed:11297557, ECO:0000269|PubMed:14673179, ECO:0000269|PubMed:15084260, ECO:0000269|PubMed:17213322, ECO:0000269|PubMed:19716809, ECO:0000269|PubMed:20410276, ECO:0000269|PubMed:20434986, ECO:0000269|PubMed:20797629, ECO:0000269|PubMed:21138416, ECO:0000269|PubMed:25326418, ECO:0000269|PubMed:30337470, ECO:0000269|PubMed:9346484}.
Catalytic activity
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[I-kappa-B protein] = ADP + H(+) + O-phospho-L-seryl-[I-kappa-B protein]; Xref=Rhea:RHEA:19073, Rhea:RHEA-COMP:13698, Rhea:RHEA-COMP:13699, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=; Evidence={ECO:0000269|PubMed:9346484}; 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:25326418}; 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=; Evidence={ECO:0000305};
Subellular location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20797629}. Nucleus {ECO:0000269|PubMed:20797629}. Membrane raft {ECO:0000269|PubMed:17287217}. Note=Colocalized with DPP4 in membrane rafts. {ECO:0000269|PubMed:17287217}.
TISSUE SPECIFICITY: Highly expressed in heart, placenta, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis and peripheral blood.
SUBUNIT: Component of the I-kappa-B-kinase (IKK) core complex consisting of CHUK, IKBKB and IKBKG; probably four alpha/CHUK-beta/IKBKB dimers are associated with four gamma/IKBKG subunits (PubMed:32935379). The IKK core complex seems to associate with regulatory or adapter proteins to form a IKK-signalosome holo-complex (PubMed:12612076). The IKK complex associates with TERF2IP/RAP1, leading to promote IKK-mediated phosphorylation of RELA/p65 (By similarity). Part of a complex composed of NCOA2, NCOA3, CHUK/IKKA, IKBKB, IKBKG and CREBBP (PubMed:11971985). Part of a 70-90 kDa complex at least consisting of CHUK/IKKA, IKBKB, NFKBIA, RELA, ELP1 and MAP3K14 (PubMed:9751059). Found in a membrane raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB (PubMed:17287217). Interacts with SQSTM1 through PRKCZ or PRKCI (PubMed:10356400). Forms an NGF-induced complex with IKBKB, PRKCI and TRAF6 (By similarity). May interact with MAVS/IPS1 (PubMed:16177806). Interacts with NALP2 (PubMed:15456791). Interacts with TICAM1 (PubMed:14739303). Interacts with FAF1; the interaction disrupts the IKK complex formation (PubMed:17684021). Interacts with ATM (PubMed:16497931). Part of a ternary complex consisting of TANK, IKBKB and IKBKG (PubMed:12133833). Interacts with NIBP; the interaction is direct (PubMed:15951441). Interacts with ARRB1 and ARRB2 (PubMed:15173580). Interacts with TRIM21 (PubMed:19675099). Interacts with NLRC5; prevents IKBKB phosphorylation and kinase activity (PubMed:20434986). Interacts with PDPK1 (PubMed:16207722). Interacts with EIF2AK2/PKR (PubMed:10848580). The phosphorylated form interacts with PPM1A and PPM1B (PubMed:18930133). Interacts with ZNF268 isoform 2; the interaction is further increased in a TNF-alpha-dependent manner (PubMed:23091055). Interacts with IKBKE (PubMed:23453969). Interacts with AKAP13 (PubMed:23090968). Interacts with IFIT5; the interaction synergizes the recruitment of IKK to MAP3K7 and enhances IKK phosphorylation (PubMed:26334375). Interacts with LRRC14; disrupts IKBKB-IKBKG interaction preventing I-kappa-B-kinase (IKK) core complex formation and leading to a decrease of IKBKB phosphorylation and NF-kappaB activation (PubMed:27426725). Interacts with SASH1 (PubMed:23776175). Interacts with ARFIP2 (PubMed:26296658). Interacts with FKBP5 (PubMed:31434731, PubMed:26101251). {ECO:0000250|UniProtKB:O88351, ECO:0000250|UniProtKB:Q9QY78, ECO:0000269|PubMed:10356400, ECO:0000269|PubMed:10848580, ECO:0000269|PubMed:11971985, ECO:0000269|PubMed:12133833, ECO:0000269|PubMed:12612076, ECO:0000269|PubMed:14739303, ECO:0000269|PubMed:15173580, ECO:0000269|PubMed:15456791, ECO:0000269|PubMed:15951441, ECO:0000269|PubMed:16177806, ECO:0000269|PubMed:16207722, ECO:0000269|PubMed:16497931, ECO:0000269|PubMed:17287217, ECO:0000269|PubMed:17684021, ECO:0000269|PubMed:18930133, ECO:0000269|PubMed:19675099, ECO:0000269|PubMed:20434986, ECO:0000269|PubMed:23091055, ECO:0000269|PubMed:23453969, ECO:0000269|PubMed:23776175, ECO:0000269|PubMed:26101251, ECO:0000269|PubMed:26296658, ECO:0000269|PubMed:26334375, ECO:0000269|PubMed:27426725, ECO:0000269|PubMed:31434731, ECO:0000269|PubMed:32935379, ECO:0000269|PubMed:9751059}.; SUBUNIT: (Microbial infection) Interacts with Yersinia YopJ. {ECO:0000269|PubMed:16728640}.; SUBUNIT: (Microbial infection) Interacts with vaccinia virus protein B14. {ECO:0000269|PubMed:29748387}.
Post-translational modification
PTM: Upon cytokine stimulation, phosphorylated on Ser-177 and Ser-181 by MEKK1 and/or MAP3K14/NIK as well as TBK1 and PRKCZ; which enhances activity (PubMed:10022904, PubMed:16207722). Phosphorylated by MAP3K7/TAK1 in response to NOD1 and NOD2 signaling, promoting activation and phosphorylation of NF-kappa-B inhibitors, leading to NF-kappa-B activation (PubMed:11460167). Once activated, autophosphorylates on the C-terminal serine cluster; which decreases activity and prevents prolonged activation of the inflammatory response (PubMed:10195894). Phosphorylated by the IKK-related kinases TBK1 and IKBKE, which is associated with reduced CHUK/IKKA and IKBKB activity and NF-kappa-B-dependent gene transcription (PubMed:10783893). Dephosphorylated at Ser-177 and Ser-181 by PPM1A and PPM1B (PubMed:18930133). {ECO:0000269|PubMed:10022904, ECO:0000269|PubMed:10195894, ECO:0000269|PubMed:10783893, ECO:0000269|PubMed:11460167, ECO:0000269|PubMed:16207722, ECO:0000269|PubMed:18930133}.; PTM: (Microbial infection) Acetylation of Thr-180 by Yersinia YopJ prevents phosphorylation and activation, thus blocking the I-kappa-B pathway. {ECO:0000269|PubMed:16728640, ECO:0000269|PubMed:17116858}.; PTM: Ubiquitinated. Monoubiquitination involves TRIM21 that leads to inhibition of Tax-induced NF-kappa-B signaling. According to PubMed:19675099, 'Ser-163' does not serve as a monoubiquitination site. According to PubMed:16267042, ubiquitination on 'Ser-163' modulates phosphorylation on C-terminal serine residues. {ECO:0000269|PubMed:16267042, ECO:0000269|PubMed:19675099}.; PTM: (Microbial infection) Monoubiquitination by TRIM21 is disrupted by Yersinia YopJ. {ECO:0000269|PubMed:19675099}.; PTM: Hydroxylated by PHD1/EGLN2, loss of hydroxylation under hypoxic conditions results in activation of NF-kappa-B. {ECO:0000269|PubMed:17114296}.
Target Relevance information above includes information from UniProt accession : O14920
The UniProt Consortium


Western blot analysis of IKK beta in Jurkat whole cell lysate with IKK beta antibody (C3) at 1:500 dilution.
Immunocytochemistry staining of HeLa cells using IKK beta antibody at 10 µg/mL.
Immunofluorescence of IKK beta in Hela cells with IKK beta antibody at 10 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


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