IL4 Antibodies

Structure of IL4

IL4 is a glycoprotein with a molecular weight of approximately 15-20 kDa. Its precise molecular weight varies slightly due to the degree of glycosylation and species differences.

IL4 is composed of 129 amino acids and features A typical four-helix bundle structure (A-D helix), maintaining stability through three conserved disulfide bonds. Its functionality depends on the binding to the IL4 receptor (IL4Rα/γc), where key sites such as Arg88 and Tyr124 are directly involved in receptor interactions. The secondary structure of IL4 is dominated by α -helices, forming a hydrophobic core, while the surface-exposed charged residues regulate its specific recognition with receptors. This protein plays a core role in immune regulation, particularly influencing the differentiation of Th2 cells and the conversion of IgE categories.

Fig. 1 IL-4 receptor type I/II in hematopoiesis and hematopoietic cell difference expression and functional regulation.¹

Key structural properties of IL4:

• Four-helix bundle structure (A-D helix)
• Conserved disulfide bonds (Cys3-Cys127, Cys24-Cys65, Cys46-Cys99)
• Key receptor binding sites (Arg88, Tyr124, Glu9)
• Glycosylation modification sites (such as Asn38, etc)
• Hydrophobic core and hydrophilic surface

Functions of IL4

The core function of IL4 (interleukin-4) is to regulate immune responses, especially playing a key role in Th2-type immune responses, and it is also involved in various pathophysiological processes.

The signal transduction of IL4 shows a biphase concentration dependence: at low concentrations, the STAT6 pathway is preferentially activated, while at high concentrations, the IRS pathway can be additionally activated. This characteristic enables it to precisely regulate the intensity and duration of immune responses. Unlike the broad-spectrum effects of most cytokines, the function of IL4 has significant cell type specificity, such as differentiated regulation of B cells and T cells, highlighting its pivotal position in the immune network.

Applications of IL4 and IL4 Antibody in Literature

1. Junttila, Ilkka S. "Tuning the cytokine responses: an update on interleukin (IL)-4 and IL-13 receptor complexes." Frontiers in immunology 9 (2018): 888.https://doi.org/10.3389/fimmu.2018.00888

Studies have shown that IL-4 and IL-13 are key cytokines regulating allergic inflammation, which can induce Th2 cell differentiation, IgE category conversion and alternative activation of macrophages. The receptor binding kinetics and chain expression determine the signal efficiency, and the related mechanism research lays the foundation for targeted therapy of allergic diseases. The pioneering work of William E. Paul and others has promoted the development of this field.

2. Zakaria, Marwa, et al. "Role of interleukin 4 (IL4) and interleukin 6 (IL6) in the pathogenesis and prognosis of childhood primary immune thrombocytopenia." European journal of pediatrics 182.7 (2023): 3129-3138. https://doi.org/10.1007/s00431-023-04945-x

Studies have shown that the levels of serum IL-4 and IL-6 in children with immune thrombocytopenia (ITP) are significantly elevated, especially in the initial and persistent ITP. Those with a higher level of IL-4 are more likely to achieve remission, suggesting that it may be involved in the pathogenesis of ITP and can be used as a predictor of treatment response.

3. Steen-Louws, Cristine, et al. "Sialic acid-engineered IL4–10 fusion protein is bioactive and rapidly cleared from the circulation." Pharmaceutical Research 37.2 (2020): 17. https://doi.org/10.1007/s11095-019-2744-y

Research has found that the in vitro and in vivo activities of the IL4-10 fusion protein (IL4-10 FP) with low sialacidification and high sialacidification are similar, but the initial clearance rate of the low sialacidification version is higher, with a half-life of 20.7 minutes for both. Differential sialacidification does not affect the efficacy of the drug, but it can regulate the systemic exposure level. The low sialacidification type is more suitable for local administration to reduce systemic exposure.

4. Piloto, Ana Margarida, et al. "Plastic antibodies tailored on quantum dots for an optical detection of myoglobin down to the femtomolar range." Scientific reports 8.1 (2018): 4944. https://doi.org/10.1155/2013/263952

This study made the first attempt to predict IL4-induced peptides. By analyzing 904 IL4-induced peptides and 742 non-induced peptides, it was found that there were differences in their amino acid composition and motif patterns. The classification model developed based on this has an accuracy rate of 75.76% and can be used to design peptides that induce Th2 immune responses.

5. Zhou, Xiaolai, Björn Spittau, and Kerstin Krieglstein. "TGFβ signalling plays an important role in IL4-induced alternative activation of microglia." Journal of neuroinflammation 9.1 (2012): 210. https://doi.org/10.1186/1742-2094-9-210

Research has found that TGFβ can enhance IL4-induced alternative activation of microglia (M2 type), significantly increasing the expression of Arg1 and Ym1. IL4 can also promote the secretion of TGFβ2, and blocking TGFβ receptor I inhibits this process, indicating that IL4-induced M2 polarization depends on the TGFβ signaling pathway.

Creative Biolabs: IL4 Antibodies for Research

Creative Biolabs specializes in the production of high-quality IL4 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom IL4 Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our IL4 antibodies, custom preparations, or technical support, contact us at email.