Phospho-IKBKG (Ser85) Antibody

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Description

Applications

MethodDilution RangeNotes
Western Blotting1:500–1:2000 Detects phosphorylated IKBKG in lysates (e.g., HepG2 cells treated with anisomycin)
Immunohistochemistry1:100–1:300 Suitable for tissue sections (e.g., cancer biopsies)
ELISA1:40,000 Quantitative detection in serum/plasma
Immunofluorescence1:50–200 Localization studies in cultured cells

Research Context

Role in NF-κB Signaling:
IKBKG (NEMO) is a regulatory subunit of the IKK complex, which phosphorylates IκB proteins, leading to their degradation and NF-κB activation. Phosphorylation at Ser85 enhances NEMO’s interaction with ATM kinase, enabling downstream signaling .

Disease Implications:

  • Mutations in IKBKG are linked to immunodeficiencies (e.g., ectodermal dysplasia, recurrent infections) .

  • The antibody aids in studying how phosphorylation modulates NEMO’s function in these contexts .

Post-Translational Modifications:

  • Ser85 phosphorylation is induced by genotoxic stress (e.g., UV radiation) and ATM activation .

  • Cross-talk with ubiquitination (e.g., K63-linked chains) regulates NF-κB activation .

  1. St. John’s Labs, Anti-Phospho-IKBKG-Ser85 Antibody (2025).

  2. Antibodies-Online, IKBKG Antibody (ABIN6655353) (2019).

  3. PMC, IKBKG mutation and immunodeficiency (2008).

  4. Cusabio, Phospho-IKBKG (Ser85) Antibody (2025).

  5. G-Biosciences, Phospho-IKKγ (S85) Polyclonal Antibody (2025).

Product Specs

Form
Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Lead Time
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Synonyms
IkB kinase associated protein 1 antibody; IkB kinase subunit gamma antibody; Inhibitor of nuclear factor kappa B kinase subunit gamma antibody; AMCBX1 antibody; FIP 3 antibody; FIP-3 antibody; FIP3 antibody; Fip3p antibody; I kappa B kinase gamma antibody; I-kappa-B kinase subunit gamma antibody; IkB kinase gamma subunit antibody; IkB kinase subunit gamma antibody; IkB kinase-associated protein 1 antibody; Ikbkg antibody; IKK gamma antibody; IKK-gamma antibody; IKKAP1 antibody; IKKG antibody; IMD33 antibody; Incontinentia pigmenti antibody; Inhibitor of kappa light polypeptide gene enhancer in B cells, kinase gamma antibody; Inhibitor of kappa light polypeptide gene enhancer in B cells, kinase of, gamma antibody; Inhibitor of nuclear factor kappa-B kinase subunit gamma antibody; IP antibody; IP1 antibody; IP2 antibody; IPD2 antibody; NEMO antibody; NEMO_HUMAN antibody; NF kappa B essential modifier antibody; NF kappa B essential modulator antibody; NF-kappa-B essential modifier antibody; NF-kappa-B essential modulator antibody; ZC2HC9 antibody
Target Names
Uniprot No.

Target Background

Function
IKBKG, also known as NEMO, is the regulatory subunit of the IKK core complex. It plays a crucial role in the phosphorylation of NF-κB inhibitors, leading to their dissociation from the NF-κB complex and subsequent degradation. This process ultimately activates NF-κB signaling. IKBKG's binding to scaffolding polyubiquitin is essential for IKK activation triggered by various signaling receptor pathways. Notably, IKBKG exhibits high affinity for linear polyubiquitin, recognizing and binding both 'Lys-63'-linked and linear polyubiquitin upon cellular stimulation. IKBKG's involvement in NF-κB-mediated protection from cytokine toxicity suggests its potential role in mitigating inflammatory responses. Furthermore, IKBKG is crucial for viral activation of IRF3 and participates in TLR3- and IFIH1-mediated antiviral innate responses, requiring 'Lys-27'-linked polyubiquitination. Beyond its role in antiviral responses, IKBKG is implicated in HTLV-1 Tax oncoprotein activation of NF-κB, potentially contributing to viral-induced oncogenesis.
Gene References Into Functions
  1. Computational analysis has identified two miR-107 binding sites in the 3'UTR of IKBKG, suggesting that miR-107 regulates IKBKG expression. PMID: 30396951
  2. Research indicates that human IKBKG does not interact with mammalian Atg8-family proteins. PMID: 29097655
  3. Studies suggest the ANGPTL8/p62-IKBKG axis as a negative feedback loop that regulates NF-κB activation and expands the role of selective autophagy in fine-tuning inflammatory responses. PMID: 29255244
  4. A study highlights immunodeficiency in two female patients with Incontinentia Pigmenti, diagnosed by lipopolysaccharide unresponsiveness, due to a heterozygous NEMO mutation. PMID: 28702714
  5. GSK-3beta plays a critical role in regulating NF-κB signaling by modulating NEMO phosphorylation. PMID: 27929056
  6. HOTAIR influences the activity of IKKalpha, IKKbeta, and IKBKG in liver cancer stem cells. PMID: 27367027
  7. A study demonstrated that the loss of the NEMO-SHARPIN interaction hinders the recruitment of truncated NEMO forms into punctuate structures, which are transiently formed upon cell stimulation, leading to a defect in linear ubiquitination. PMID: 28249776
  8. NEMO is critically involved in the cGAS-STING pathway. PMID: 28939760
  9. Research shows that ASAP3 regulates NEMO expression by directly interacting with it and reducing its poly-ubiquitinylation. PMID: 28502111
  10. Treatment of breast cancer cells with estrogen and progesterone (E+P) increases ER binding to the NEMO promoter, thereby enhancing NEMO expression. PMID: 28515148
  11. Hematopoietic stem cell transplantation can effectively cure most clinical features in patients with various IKBKG mutations. PMID: 28679735
  12. NEMO stabilizes HIFalpha through direct interaction, independent of NF-κB signaling in vitro. This stabilization prolongs tumor cell survival by regulating apoptosis and activating epithelial-to-mesenchymal transition, thereby facilitating tumor metastasis. PMID: 26500060
  13. Research provides the first evidence of father-to-daughter transmission of Incontinentia Pigmenti, demonstrating a pathogenic mutation in IKBKG. PMID: 27037530
  14. Molluscum contagiosum virus MC005 inhibits NF-κB signaling upstream of the IKK complex. Affinity purification revealed that MC005 interacts with the IKK subunit NEMO. PMID: 28490597
  15. Data suggest that molluscum contagiosum virus MC159 competitively binds to NEMO, preventing cIAP1-induced NEMO polyubiquitination. PMID: 28515292
  16. High IKBKG expression is associated with multiple myeloma. PMID: 27454822
  17. Studies illuminate the nature of the interaction between NEMO and poly-ubiquitin, suggesting that NEMO regulation is differentially influenced by poly-ubiquitin chain length. This regulation appears to occur through modulation of the available equilibrium of conformational states rather than gross structural changes. PMID: 27028374
  18. FADD, along with NEMO, is a substrate for the LUBAC ubiquitin ligase (E3) complex, composed of the HOIP, HOIL-1L, and SHARPIN subunits. PMID: 28189684
  19. Experimental evidence supports the essential role of the zinc ion in mechanically stabilizing the functional, folded conformation of NEMO. PMID: 28035815
  20. Simulations of the zinc finger NEMO (2JVX) using multiple simulations of length 15, 30, 1000, and 3000 ns provide clarity on the significance of the zinc ion in maintaining NEMO's structure and function. PMID: 25734227
  21. Deletion of exons 4 to 10 (NEMODelta4-10) accounts for approximately 80% of cases (familial and sporadic) of Incontinentia pigmenti. PMID: 26564087
  22. Research reveals that cFLIPL requires the linear ubiquitin chain assembly complex and the kinase TAK1 for activation of the IKK kinase. PMID: 26865630
  23. USP18 negatively regulates NF-κB signaling by targeting TAK1 and NEMO for deubiquitination through distinct mechanisms. PMID: 26240016
  24. A missense mutation in IKBKG causes either a Nager syndrome or an atypical incontinentia pigmenti phenotype. While IKBKG mutations typically lead to preterm male death, this variant is associated with survival for 8-15 days. PMID: 25441681
  25. Recruitment of A20 to the C-terminal domain of NEMO represents a novel mechanism limiting NF-κB activation by NEMO. Its absence results in autoinflammatory disease. PMID: 26802121
  26. Research indicates that Rab11-GMPPNP-FIP3-Rabin8 is more stable than Rab11-GMPPNP-Rabin8 due to direct interaction between Rabin8 and FIP3 within the dual effector-bound complex. PMID: 26258637
  27. Somatic mosaicism of a novel IKBKG nonsense mutation has been observed in a male patient with incontinentia pigmenti. PMID: 25944529
  28. COMMD7's binding to NEMO does not interfere with the binding to the IKKs. Disrupting the IKK complex using the NBP competitor impairs the termination of NF-κB activity. PMID: 26060140
  29. Findings suggest that rare, functional variants in MYD88, IRAK4, or IKBKG do not significantly contribute to IPD susceptibility in adults at the population level. PMID: 25886387
  30. Incontinentia pigmenti patients typically present with a common IKBKG exon 4-10 deletion. PMID: 24073555
  31. A novel mutation, designated c.916G>A (p.D306N), has been identified. While NEMO expression remains unaffected, ubiquitylation is decreased, causing ectodermal dysplasia, immunodeficiency, incontinentia pigmenti, and immune thrombocytopenic purpura. PMID: 26117626
  32. IKKgamma, a parallel coiled-coil, exhibits localized twisting in response to binding of vFLIP or IKKbeta. PMID: 25979343
  33. IPO3 binds NEMO, promoting its nuclear import, and is critical for DNA damage-dependent NF-κB activation. PMID: 26060253
  34. Unanchored polyubiquitin plays a regulatory role by inducing NEMO conformational change through an allosteric mechanism. PMID: 25866210
  35. The stability of the NEMO coiled coil is maintained by strong interhelix interactions in the region centered on residue 54. PMID: 25400026
  36. Mass spectrometric analysis revealed that WA covalently modifies NEMO on a cysteine residue within the C-terminal zinc finger (ZF) domain. Point mutations within the ZF can reverse the WA-induced Lys-48-polyubiquitin binding phenotype. PMID: 25296760
  37. NEMO patients without ectodermal dysplasia and anhidrosis exhibit more robust immunologic responses. PMID: 24682681
  38. The rescuing of binding affinity suggests that a preordered IKK-binding region of NEMO is compatible with IKK binding, and the observed conformational heterogeneity in NEMO(44-111) may be an artifact of the truncation. PMID: 25286246
  39. IKBKG gene mutation has been identified as a cause for incontinentia pigmenti. (Meta-analysis) PMID: 23802866
  40. Genomic analysis of a girl with incontinentia pigmenti, but without NEMO mutation, has been reported. PMID: 24487970
  41. Data suggest the potential of targeting Nemo-Like Kinase (NLK) to treat a range of tumourigenic conditions characterized by PTEN deficiency. PMID: 23144700
  42. 21 new point mutations have been reported, expanding the spectrum of pathologic variants in Incontinentia pigmenti patients. These include premature stop codon, frameshift mutation, or partial loss of NEMO/IKKgamma activity (splicing and missense). PMID: 24339369
  43. p62 interacts with NEMO, the regulatory subunit of the complex responsible for activating the NF-κB transcription factor. PMID: 24270048
  44. NEMO is essential for Kaposi's sarcoma-associated herpesvirus-encoded vFLIP K13-induced gene expression and protection against death receptor-induced cell death. PMID: 24672029
  45. A post-translational modification of NEMO has been identified - phosphorylation of residue 387. Phosphorylation of serine 387 is not an absolute requirement for NF-κB signaling. PMID: 24012789
  46. IKKgamma facilitates RhoA activation via a guanine nucleotide exchange factor, which, in turn, activates ROCK to phosphorylate IKKbeta, leading to NF-κB activation that induces chemokine expression and cell migration upon TGF-beta1. PMID: 24240172
  47. Research indicates that all seven cysteines (4 in the zinc finger domain) of NEMO can be simultaneously mutated to alanine without affecting NEMO's binding affinity for the I-kappa B kinase beta catalytic subunit. PMID: 24266532
  48. USP10 inhibits genotoxic NF-κB activation by MCPIP1-facilitated deubiquitination of NEMO. PMID: 24270572
  49. Merkel cell polyomavirus small T antigen targets the NEMO adaptor protein to disrupt inflammatory signaling. PMID: 24109239
  50. NEMO ZF, similar to other NEMO-related ZFs, binds mono-Ub and di-Ub with distinct stoichiometries, indicating the presence of a new Ub site within the NEMO ZF. PMID: 24100029

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Database Links

HGNC: 5961

OMIM: 300248

KEGG: hsa:8517

STRING: 9606.ENSP00000358622

UniGene: Hs.43505

Involvement In Disease
Ectodermal dysplasia, anhidrotic, with immunodeficiency X-linked (EDAID); Ectodermal dysplasia, anhidrotic, with immunodeficiency, osteopetrosis and lymphedema (OLEDAID); Immunodeficiency, NEMO-related, without anhidrotic ectodermal dysplasia (NEMOID); Immunodeficiency 33 (IMD33); Recurrent isolated invasive pneumococcal disease 2 (IPD2); Incontinentia pigmenti (IP)
Subcellular Location
Cytoplasm. Nucleus.
Tissue Specificity
Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.

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