IL17A Mouse, Sf9
Description
Production and Formulation
Produced in Sf9 cells infected with recombinant baculovirus, IL17A Mouse is purified via proprietary chromatographic techniques . Two formulations are available:
Functional Properties
IL17A Mouse, Sf9 exhibits potent bioactivity:
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ED₅₀: 0.25–1.25 ng/mL in murine fibroblast proliferation assays
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Receptor Binding: Signals through IL-17RA/IL-17RC heterodimers, activating NF-κB and MAPK pathways
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Key Roles:
Autoimmune Disease Models
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Experimental Autoimmune Encephalomyelitis (EAE):
Infectious Disease Studies
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Antiviral Defense: Enhances B cell responses in H5N1 influenza and West Nile virus infections .
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Bacterial Clearance: Critical for Staphylococcus aureus skin infection control via neutrophil activation .
Cancer and Inflammation
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Dual Role: Promotes tumorigenesis in colitis-associated cancer but inhibits metastasis in melanoma .
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Therapeutic Target: Cyanidin derivatives (e.g., A18) block IL-17A/IL-17RA binding, reducing psoriasis and asthma severity .
Stability and Handling
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Storage: Stable at -20°C for years; short-term storage at 4°C requires carrier protein (e.g., 0.1% HSA/BSA) .
Key Research Findings
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Transcriptomic Analysis: IL-17A deficiency alters 149 genes in brain tissue during HSV-IL-2-induced demyelination, affecting neuron projection and ensheathment pathways .
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Neutrophil Specificity: A18 inhibits IL-17A-driven Ly6G⁺ neutrophil infiltration in EAE without affecting CD4⁺/CD8⁺ T cells .
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Cross-Species Activity: Human and mouse IL-17RA share conserved binding residues (e.g., Asp²⁶²), enabling translational studies .
Product Specs
Interleukin-17A, also known as IL17A, is a cytokine with a critical role in chronic and antimicrobial inflammation. Mice, rats, and humans share approximately 60% similarity in the amino acid sequence of IL17A. During bacterial infection, IL17A amplifies mucosal and epidermal inflammation, leading to increased chemokine production, neutrophil recruitment, and production of antibacterial proteins.
Produced in Sf9 insect cells using a baculovirus expression system, IL17A Mouse is a single, glycosylated polypeptide chain containing 141 amino acids (26-158 a.a) with a molecular weight of 16kDa. An 8 amino acid His tag is fused to the C-terminus to facilitate purification, which is carried out using proprietary chromatographic techniques.
The IL17A solution is provided at a concentration of 0.5mg/ml in a buffer consisting of 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Avoid repeated freeze-thaw cycles to prevent protein degradation.
Purity is determined by SDS-PAGE analysis and is consistently greater than 95%.
IL17A, Ctla-8, Ctla8, IL-17, IL-17A, Il17, Interleukin-17A, Cytotoxic T-lymphocyte-associated antigen 8, CTLA-8.
Sf9, Baculovirus cells.
AAIIPQSSAC PNTEAKDFLQ NVKVNLKVFN SLGAKVSSRR PSDYLNRSTS PWTLHRNEDP DRYPSVIWEA QCRHQRCVNA EGKLDHHMNS VLIQQEILVL KREPESCPFT FRVEKMLVGV GCTCVASIVR QAALEHHHHH H
Q&A
FAQs on IL-17A in Mouse Models and Sf9-Based Research
Advanced Research Questions
How does IL-17A modulate neuronal activity in neurodevelopmental disorders?
IL-17A rescues social deficits in maternal immune activation (MIA) offspring by reducing hyperactivity in the somatosensory cortex (S1DZ). Direct IL-17A delivery to S1DZ restores sociability in monogenic autism models (e.g., Cntnap2−/−), while IL-17Ra deletion abolishes this effect .
What structural features govern IL-17A’s interaction with its receptor?
IL-17A binds IL-17RA via three regions:
How to resolve contradictions in IL-17A’s pro-inflammatory vs. protective roles?
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Pathogenic role: Drives autoimmunity (e.g., EAE , DVT ) and neutrophil-mediated tissue damage .
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Protective role: Essential for mucosal immunity against Candida albicans and Staphylococcus aureus via antimicrobial peptide induction .
Methodological approach: Use conditional knockouts (e.g., myeloid- or T cell-specific Il17a deletion) to dissect context-dependent functions.
What are the technical challenges in tracking IL-17A expression kinetics in vivo?
The Smart-17A reporter mouse addresses this by marking IL-17A-producing cells with hNGFR. Key limitations include:
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Reporter half-life: ~24–48 hours, necessitating frequent sampling .
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False positives: 30% of hNGFR+ cells lack intracellular IL-17A due to prior secretion .
Solution: Combine reporter models with intracellular cytokine staining for validation.
Methodological Considerations
Experimental Design Table for IL-17A Studies
Product Science Overview
Interleukin-17A (IL-17A) is a cytokine that plays a crucial role in chronic and antimicrobial inflammation. It is part of the interleukin-17 family, which includes six members (IL-17A to IL-17F). IL-17A is primarily produced by activated CD4+ T cells, also known as T helper 17 (Th17) cells. This cytokine is involved in various inflammatory diseases, including rheumatoid arthritis, asthma, multiple sclerosis, psoriasis, and transplant rejection .
The mouse recombinant IL-17A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 141 amino acids (26-158 a.a.) and has a molecular mass of approximately 16 kDa . The recombinant protein is fused to an 8 amino acid His tag at the C-terminus and purified using proprietary chromatographic techniques . The amino acid sequence of the mouse IL-17A is as follows:
AAIIPQSSAC PNTEAKDFLQ NVKVNLKVFN SLGAKVSSRR PSDYLNRSTS PWTLHRNEDP DRYPSVIWEA QCRHQRCVNA EGKLDHHMNS VLIQQEILVL KREPESCPFT FRVEKMLVGV GCTCVASIVR QAALEHHHHH
IL-17A enhances mucosal and epidermal inflammation during bacterial infections by inducing the production of chemokines, which attract neutrophils to the site of infection . It also stimulates the production of antibacterial proteins. In human fibroblasts, IL-17A enhances the expression of intracellular adhesion molecule-1 (ICAM-1) and stimulates epithelial, endothelial, and fibroblastic cells to secrete other cytokines such as IL-6, IL-8, granulocyte-colony stimulating factor (G-CSF), and prostaglandin E2 (PGE2) .
Recombinant IL-17A is used in various research applications, including:
