Datasheet

生物学的記述

Specificity	IKKα Antibody [B4D5] detects endogenous levels of total IKKα protein.
Background	IKKα constitutes one of the two catalytic subunits of the IκB kinase complex, alongside IKKβ, with NEMO serving as the regulatory scaffold in the canonical NF-κB pathway. The protein possesses an N-terminal kinase domain, a central ubiquitin-binding leucine zipper motif, and a C-terminal helix-loop-helix domain that mediates dimerization and complex assembly. Activation occurs through phosphorylation at serines within the activation loop by upstream kinases such as NIK and TAK1, inducing conformational shifts that enable substrate access and trans-autophosphorylation. IKKα phosphorylates IκBα at serines 32 and 36, marking it for K48-linked ubiquitination and proteasomal degradation, thereby liberating NF-κB dimers for nuclear translocation and transcription of genes involved in inflammation, survival, and proliferation. In the non-canonical pathway, NIK stabilizes and activates dimeric IKKα, which phosphorylates p100/RelB precursors to trigger their processing into p52/RelB, driving lymphoid organogenesis and B cell survival. IKKα interacts with RIP1, TRAF2/3, and TAX1BP1 to fine-tune signaling duration via negative feedback, including A20-mediated deubiquitination of adaptors. Beyond NF-κB, IKKα phosphorylates histone H3, Raptor, and TSC1 to integrate metabolic control with cytokine responses in keratinocytes and fibroblasts. Dimerization with IKKβ amplifies IκBα turnover under TNF stimulation, while NEMO polyubiquitination recruits IKKα to signaling platforms at receptor complexes. Dysregulation through amplification or constitutive activation promotes chronic inflammation, squamous cell carcinoma, and rheumatoid arthritis progression.

Specificity

IKKα Antibody [B4D5] detects endogenous levels of total IKKα protein.

Background

IKKα constitutes one of the two catalytic subunits of the IκB kinase complex, alongside IKKβ, with NEMO serving as the regulatory scaffold in the canonical NF-κB pathway. The protein possesses an N-terminal kinase domain, a central ubiquitin-binding leucine zipper motif, and a C-terminal helix-loop-helix domain that mediates dimerization and complex assembly. Activation occurs through phosphorylation at serines within the activation loop by upstream kinases such as NIK and TAK1, inducing conformational shifts that enable substrate access and trans-autophosphorylation. IKKα phosphorylates IκBα at serines 32 and 36, marking it for K48-linked ubiquitination and proteasomal degradation, thereby liberating NF-κB dimers for nuclear translocation and transcription of genes involved in inflammation, survival, and proliferation. In the non-canonical pathway, NIK stabilizes and activates dimeric IKKα, which phosphorylates p100/RelB precursors to trigger their processing into p52/RelB, driving lymphoid organogenesis and B cell survival. IKKα interacts with RIP1, TRAF2/3, and TAX1BP1 to fine-tune signaling duration via negative feedback, including A20-mediated deubiquitination of adaptors. Beyond NF-κB, IKKα phosphorylates histone H3, Raptor, and TSC1 to integrate metabolic control with cytokine responses in keratinocytes and fibroblasts. Dimerization with IKKβ amplifies IκBα turnover under TNF stimulation, while NEMO polyubiquitination recruits IKKα to signaling platforms at receptor complexes. Dysregulation through amplification or constitutive activation promotes chronic inflammation, squamous cell carcinoma, and rheumatoid arthritis progression.

使用情報

Application

WB, IP

Dilution

WB	IP
1:1000	1:200

Reactivity

Human, Mouse, Rat

Source

Rabbit Monoclonal Antibody

MW

85 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

プロトコール

References

https://pubmed.ncbi.nlm.nih.gov/10779355/
https://pubmed.ncbi.nlm.nih.gov/18626576/

Application Data

WB

Validated by Selleck

Lane 1: HCT116, Lane 2: Daudi, Lane 3: A549, Lane 4: A20