Choose Your Country or Region

Anti-Phospho-IRF3 (Ser386) Rabbit Antibody [L20H23]

Catalog No.: F4013

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000 - 1:10000

Application
WB

Reactivity
Human

Source
Rabbit

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
47 kDa

Datasheet & SDS

Biological Description

Specificity
Anti-Phospho-IRF3 (Ser386) Rabbit Antibody [L20H23] detects endogenous levels of total IRF3 protein only when phosphorylated at Ser 386.

Clone
L20H23

Synonym(s)
Interferon regulatory factor 3, IRF-3, IRF3

Background
Phosphorylation of Interferon Regulatory Factor 3 (IRF3) at serine 386 (Ser386) is a critical post-translational modification essential for its activation in the innate immune response against viral infections. IRF3 is a transcription factor that, upon phosphorylation at multiple C-terminal serine/threonine residues, including Ser386, undergoes dimerization and translocates to the nucleus. Ser386 lies within the serine-rich region of the C-terminal domain, where phosphorylation triggers conformational changes promoting IRF3 interaction with coactivators like CREB-binding protein (CBP)/p300. This interaction facilitates transcription of type I interferons and other antiviral genes. Phosphorylation at Ser386 works synergistically with phosphorylation at Ser396, forming oligomers that strongly bind CBP, which is crucial for full IRF3 activation. Mutation at Ser386 significantly impairs IRF3 dimerization, nuclear translocation, and activation of antiviral gene expression. Regulatory kinases such as TBK1 and IKKε mediate this phosphorylation upon pathogen recognition receptor activation. This phosphorylation also alleviates IRF3 autoinhibition, facilitating a two-step activation process.

Background

Phosphorylation of Interferon Regulatory Factor 3 (IRF3) at serine 386 (Ser386) is a critical post-translational modification essential for its activation in the innate immune response against viral infections. IRF3 is a transcription factor that, upon phosphorylation at multiple C-terminal serine/threonine residues, including Ser386, undergoes dimerization and translocates to the nucleus. Ser386 lies within the serine-rich region of the C-terminal domain, where phosphorylation triggers conformational changes promoting IRF3 interaction with coactivators like CREB-binding protein (CBP)/p300. This interaction facilitates transcription of type I interferons and other antiviral genes. Phosphorylation at Ser386 works synergistically with phosphorylation at Ser396, forming oligomers that strongly bind CBP, which is crucial for full IRF3 activation. Mutation at Ser386 significantly impairs IRF3 dimerization, nuclear translocation, and activation of antiviral gene expression. Regulatory kinases such as TBK1 and IKKε mediate this phosphorylation upon pathogen recognition receptor activation. This phosphorylation also alleviates IRF3 autoinhibition, facilitating a two-step activation process.

References
https://pubmed.ncbi.nlm.nih.gov/32826280/ https://pubmed.ncbi.nlm.nih.gov/18440553/

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

Tech Support

Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.

Handling Instructions

Tel: +1-832-582-8158 Ext:3
If you have any other enquiries, please leave a message.

* Indicates a Required Field

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%