IRF-7 Antibody [C15N21] | Primary Antibodies

Application: Reactivity: Mouse, Rat, Hamster

Usage Information

Dilution
WB1:1000 IP1:100

Application
WB, IP

Reactivity
Mouse, Rat, Hamster

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 Observed MW
54 kDa 45-60 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
IRF-7 Antibody [C15N21] detects endogenous levels of total IRF-7 protein.

Clone
C15N21

Synonym(s)
Interferon regulatory factor 7; IRF-7; Irf7; OTTMUSP00000029373

Background
Interferon regulatory factor 7 (IRF-7) is a member of the IRF transcription factor family that binds specific DNA elements in interferon-stimulated promoters and integrates upstream innate immune receptor signaling into type I and III interferon gene expression, especially in plasmacytoid dendritic cells and lymphoid lineages, where its expression is enriched and inducible by virus, lipopolysaccharide, and type I interferons. The N-terminal region contains a conserved helix–turn–helix DNA-binding domain that recognizes interferon regulatory elements, while the C-terminal regulatory region carries multiple serine-rich motifs and interaction surfaces that control dimerization, nuclear import, and cofactor recruitment. Upstream activation begins at pattern-recognition receptors such as endosomal Toll-like receptors and cytosolic nucleic acid sensors, which signal through adaptor proteins including MyD88 or TRIF, TRAF family ubiquitin ligases, and TANK-binding kinase 1 or IKK-related kinases that phosphorylate IRF-7 on clustered serine residues in the C terminus. Phosphorylated IRF-7 forms homodimers or heterodimers with other IRFs, undergoes conformational exposure of its nuclear localization signal, accumulates in the nucleus, and assembles on interferon promoters together with chromatin-modifying coactivators to drive a broad antiviral transcriptional program. This transcriptional output reinforces interferon signaling through a positive feedback loop, shapes the amplitude and duration of type I interferon waves, and coordinates expression of numerous interferon-stimulated genes that regulate viral replication, antigen presentation, and inflammatory mediator production. Multiple post-translational modifications fine-tune this activity: phosphorylation marks correlate with activation, K63-linked ubiquitination promotes full transactivation, and other ubiquitin linkages or proteasomal targeting limit IRF-7 abundance and prevent excessive interferon output. IRF-7 also interfaces with NF-κB and AP-1 pathways at shared target promoters and participates in Epstein–Barr virus latency programs, where its induction and activation by latent membrane protein 1 link viral oncogenic signaling to interferon-related transcriptional networks. In physiological immunity, IRF-7 is critical for early systemic antiviral defense, shaping plasmacytoid dendritic cell function, influencing B cell responses, and contributing to broader orchestration of innate and adaptive immune communication. Dysregulated IRF-7 expression or activity alters interferon production thresholds, associates with autoimmune phenotypes characterized by chronic type I interferon signatures, and influences susceptibility or progression in infection, cancer, and other inflammation-associated pathologies where interferon balance is a major determinant of tissue outcome.

Background

Interferon regulatory factor 7 (IRF-7) is a member of the IRF transcription factor family that binds specific DNA elements in interferon-stimulated promoters and integrates upstream innate immune receptor signaling into type I and III interferon gene expression, especially in plasmacytoid dendritic cells and lymphoid lineages, where its expression is enriched and inducible by virus, lipopolysaccharide, and type I interferons. The N-terminal region contains a conserved helix–turn–helix DNA-binding domain that recognizes interferon regulatory elements, while the C-terminal regulatory region carries multiple serine-rich motifs and interaction surfaces that control dimerization, nuclear import, and cofactor recruitment. Upstream activation begins at pattern-recognition receptors such as endosomal Toll-like receptors and cytosolic nucleic acid sensors, which signal through adaptor proteins including MyD88 or TRIF, TRAF family ubiquitin ligases, and TANK-binding kinase 1 or IKK-related kinases that phosphorylate IRF-7 on clustered serine residues in the C terminus. Phosphorylated IRF-7 forms homodimers or heterodimers with other IRFs, undergoes conformational exposure of its nuclear localization signal, accumulates in the nucleus, and assembles on interferon promoters together with chromatin-modifying coactivators to drive a broad antiviral transcriptional program. This transcriptional output reinforces interferon signaling through a positive feedback loop, shapes the amplitude and duration of type I interferon waves, and coordinates expression of numerous interferon-stimulated genes that regulate viral replication, antigen presentation, and inflammatory mediator production. Multiple post-translational modifications fine-tune this activity: phosphorylation marks correlate with activation, K63-linked ubiquitination promotes full transactivation, and other ubiquitin linkages or proteasomal targeting limit IRF-7 abundance and prevent excessive interferon output. IRF-7 also interfaces with NF-κB and AP-1 pathways at shared target promoters and participates in Epstein–Barr virus latency programs, where its induction and activation by latent membrane protein 1 link viral oncogenic signaling to interferon-related transcriptional networks. In physiological immunity, IRF-7 is critical for early systemic antiviral defense, shaping plasmacytoid dendritic cell function, influencing B cell responses, and contributing to broader orchestration of innate and adaptive immune communication. Dysregulated IRF-7 expression or activity alters interferon production thresholds, associates with autoimmune phenotypes characterized by chronic type I interferon signatures, and influences susceptibility or progression in infection, cancer, and other inflammation-associated pathologies where interferon balance is a major determinant of tissue outcome.

References
https://pubmed.ncbi.nlm.nih.gov/37638030/ https://pubmed.ncbi.nlm.nih.gov/21490621/

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%