IKKα Antibody [B4D5] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat

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

Usage Information

Dilution
WB1:1000 IP1:200

Application
WB, IP

Reactivity
Human, Mouse, Rat

Source
Rabbit Monoclonal Antibody

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

Predicted MW
85 kDa

Datasheet & SDS

Biological Description

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

Clone
B4D5

Synonym(s)
Inhibitor of nuclear factor kappa-B kinase subunit alpha; I-kappa-B kinase 1; IKK-A; IKK-alpha; IkappaB kinase alpha; IKK1; Conserved helix-loop-helix ubiquitous kinase; Nuclear factor NF-kappa-B inhibitor kinase alpha; NFKBIKA; CHUK; IKKA

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.

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.

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

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%