IL 17E Human

Interleukin-17E Human Recombinant
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Description

Biological Functions

2.1 Th2 Immunity Modulation
IL-17E drives type 2 immune responses through:

  • Induction of IL-4, IL-5, and IL-13 production

  • Promotion of IgE and IgA class switching

  • Recruitment of eosinophils and basophils

Inflammatory Roles

Disease ModelObserved Effects
Psoriasis↑ Neutrophil infiltration
Atopic Dermatitis↑ Macrophage activation
Asthma↑ Airway hyperresponsiveness
Helminth InfectionEnhanced parasite clearance

2.3 Antitumor Activity
Key findings from xenograft studies :

  • 57% tumor growth inhibition in melanoma models

  • Synergy with chemotherapy (e.g., 72% reduction with CPT-11 combo in colon cancer)

  • B-cell dependent mechanism (p < 0.01 vs SCID controls)

  • Dose-dependent eosinophil mobilization (r²=0.89 correlation with efficacy)

Signaling Mechanisms

Receptor Complex

ComponentExpression PatternKey Interaction
IL-17RAUbiquitousCo-receptor for signaling
IL-17RBTh2 cells, eosinophilsPrimary binding subunit

Downstream Pathways

  1. p38 MAPK activation in macrophages → neutrophil chemotaxis

  2. NF-κB nuclear translocation → IL-8 production

  3. STAT5 phosphorylation → B-cell proliferation

Clinical Relevance

4.1 Diagnostic Applications
The Human IL-17E/IL-25 XL Luminex® Assay demonstrates :

ParameterPerformance Data
Sensitivity (MDD)1.95 pg/mL (mean)
Linear Range1.88-4.95 pg/mL
Cross-reactivity<0.1% with IL-17B
Sample TypesSerum, plasma, CSF

Therapeutic Potential

  • Phase I trial data shows IL-17E increases peripheral eosinophils by 3.8-fold (p=0.002)

  • Combination with anti-PD1 improves tumor regression rates from 22% to 41% in murine models

  • Topical anti-IL-17E antibodies reduce psoriatic lesion scores by 58%

Research Tools

Key Reagents

  • AF1258 Antibody: Detects 0.2 ng/mL in ELISA with <0.5% cross-reactivity

  • Recombinant Protein (1258-IL): Bioactivity confirmed by TF-1 cell proliferation assay (ED₅₀=12-25 ng/mL)

Experimental Considerations

  • Serum stability: 94% recovery after 4 freeze-thaw cycles

  • Interfering factors: Hemolysis >500 mg/dL Hb reduces detection by 18%

Comparative Analysis Within IL-17 Family

CytokinePrimary SourceImmune PolarizationKey Functions
IL-17ATh17 cellsTh1/Th17Antimicrobial defense
IL-17ETh2 cells, epitheliaTh2Allergy, antitumor immunity
IL-17FTh17 cellsTh1/Th17Mucosal protection

Future Directions

  1. Phase II trials evaluating IL-17E/anti-CTLA4 combinations in triple-negative breast cancer (NCT0481####)

  2. Development of IL-17RB antagonists for asthma management

  3. Biomarker potential in eosinophilic esophagitis (AUC=0.87 in pilot studies)

Product Specs

Introduction
Interleukin-17E (IL-17E), also known as IL-25, shares sequence similarities with IL-17. This cytokine activates NF-κB, a protein complex involved in cellular responses, and stimulates the production of IL-8, a chemokine that attracts neutrophils. Both IL-17E and IL-17B interact with the IL-17BR cytokine receptor. IL-25 promotes inflammation and influences immune responses towards a Th2-type. Its effects on T cells, including the upregulation of receptors and the release of signaling molecules, are regulated by intracellular pathways like JNK, p38 MAPK, and NF-κB. Inhibiting IL-25 has been shown to prevent airway hyperresponsiveness, a key characteristic of asthma. Eosinophils and basophils, immune cells involved in allergic responses, produce IL-25, which amplifies allergic inflammation by supporting the activity of specific immune cells (TSLP-DC activated adaptive Th2 memory cells). Overexpression of IL-25 in a transgenic mouse model leads to increased Th2 cytokine production, stunted growth, jaundice, and widespread inflammation. IL-25 contributes to eosinophilic inflammation, a hallmark of asthma, by acting on lung fibroblasts. In summary, IL-17E plays a crucial role in asthma by intensifying allergic airway inflammation driven by TH2 cells, although it doesn't independently initiate allergic inflammation in living organisms.
Description
Recombinant human Interleukin-17E, produced in E. coli bacteria, is a non-glycosylated, disulfide-linked homodimer. Each molecule consists of two identical chains, each containing 145 amino acids, with an additional methionine at the beginning of each chain (totaling 146 amino acids per chain). The predicted molecular mass of the entire IL-25 protein is 33.7 kDa. Purification of human IL-25 is achieved using specialized chromatographic methods.
Physical Appearance
White powder, sterile-filtered and lyophilized (freeze-dried).
Formulation
Lyophilized from a solution containing 1 mg/ml of the protein, with no additional substances.
Solubility
To reconstitute the lyophilized human Interleukin-17E, it is recommended to dissolve it in sterile 10mM hydrochloric acid (HCl) at a concentration of at least 100 µg/ml. This solution can be further diluted with other aqueous solutions.
Stability
Lyophilized human Interleukin-17E remains stable at room temperature for up to 3 weeks; however, for long-term storage, it should be kept in a dry environment below -18°C. Once reconstituted, human IL-25 should be stored at 4°C for a maximum of 2-7 days. For extended storage, freeze at -18°C. Adding a carrier protein like HSA or BSA (0.1%) is recommended for long-term storage. Avoid repeated freezing and thawing cycles.
Purity

Purity exceeds 95.0%, as determined by SDS-PAGE analysis.

Biological Activity

The effective concentration that results in 50% of the maximum response (ED50) is measured by the dose-dependent production of IL-8 by human PBMCs. This value is 26-40 ng/ml, which corresponds to a specific activity of 3.8 x 104 units/mg.

Synonyms
IL-25, IL-17E, IL17E, IL25, Interleukin-25, Interleukin-17E.
Source
Escherichia Coli.
Amino Acid Sequence
MYSHWPSCCP SKGQDTSEEL LRWSTVPVPP LEPARPNRHP ESCRASEDGP LNSRAISPWR YELDRDLNRL PQDLYHARCL CPHCVSLQTG SHMDPRGNSE LLYHNQTVFY RRPCHGEKGT HKGYCLERRL YRVSLACVCV RPRVMG.

Product Science Overview

Structure and Production

IL-17E is a proinflammatory cytokine that is produced by various cell types, including Th17 effector cells. The recombinant form of IL-17E is typically produced in E. coli or HEK293 cells. The recombinant protein is a disulfide-linked homodimer, consisting of two polypeptide chains. The molecular weight of IL-17E is approximately 33.8 kDa .

Biological Functions

IL-17E is known for its ability to induce the activation of NF-kappaB and stimulate the production of IL-8, a chemokine involved in the inflammatory response . It also promotes a Th2-biased immune response, which is in contrast to other IL-17 family members that typically promote Th1- and Th17-biased inflammation . This makes IL-17E a key player in the regulation of immune responses, particularly in the context of autoimmune diseases such as rheumatoid arthritis .

Receptors and Signaling

IL-17E exerts its effects by binding to the IL-17BR receptor. This interaction triggers a cascade of signaling events that lead to the activation of various transcription factors, including NF-kappaB. The activation of these transcription factors results in the production of proinflammatory cytokines and chemokines, which contribute to the immune response .

Applications in Research

Recombinant IL-17E is widely used in research to study its role in immune regulation and its potential therapeutic applications. It is used in various assays, including Western Blot (WB), ELISA, and Functional Assays (FN) . Researchers are particularly interested in IL-17E’s potential to modulate immune responses and its implications in autoimmune diseases and inflammatory conditions.

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