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| Alternative Names | B-cell lgG differentiation factor; B-cell growth factor 1; B-cell stimulatory factor 1 (BSF-1); lGG1 induction factor; Lymphocyte stimulatory factor 1 |
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Background
IL-4 is supplied as a recombinant protein reagent for research use only. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.
Also known as: B-cell lgG differentiation factor; B-cell growth factor 1; B-cell stimulatory factor 1 (BSF-1); lGG1 induction factor; Lymphocyte stimulatory factor 1.
Endotoxin:<1 EU per 1 μg of the protein by the LAL method.
Interleukin-4, also known as IL4, is a secreted protein which belongs to the IL-4 / IL-13 family. Interleukin-4 / IL4 has many biological roles, including the stimulation of activated B-cell and T-cell proliferation. It enhances both secretion and cell surface expression of IgE and IgG1. Interleukin-4 / IL4 also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. Interleukin-4 is essential for the switching of B cells to IgE antibody production and for the maturation of T helper (Th) cells toward the Th2 phenotype. It participates in at least several B-cell activation processes as well as of other cell types. However, studies show that double mutant (Q116D, Y119D) of the murine IL4 protein (QY), both glutamine 116 and tyrosine 119, which binds to the IL4 receptor alpha, completely inhibites in a dose-dependent manner the IL4-induced proliferation of lipopolysaccharide-stimulated murine splenic B-cells, of the murine T cell line CTLL-2, and of the murine pre-B-cell line BA/F3. QY also inhibited the IL4-stimulated up-regulation of CD23 expression by lipopolysaccharide-stimulated murine splenic B-cells and abolished tyrosine phosphorylation of the transcription factor Stat6 and the tyrosine kinase Jak3 in IL4-stimulated BA/F3 cells.
Biological significance and function
Functionally, IL-4 mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as Immunology & Inflammation.
Molecular characteristics
Molecular characteristics: Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.
- Molecular weight: 13.4 kDa
- Protein length: The recombinant Mouse IL4 consists of 119 amino acids and predicts a molecular mass of 13.4 KDa
- Expression region: Amino acid sequence derived from Mouse IL4 (NP_067258.1) (His23-Ser140) was expressed.
- Purity: > 95% as determined by SDS-PAGE.
- Biological activity: Measured in a cell proliferation assay using NFS-60. The ED50 for this effect is typically 5.37 ng/mL. The specific activity of recombinant Mouse IL4 is approximately >1.86 x 105 IU/mg.
Post-translational considerations: E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.
Expression and purification strategy
Expression system: E. coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.
Tagging: Many recombinant proteins incorporate affinity tags (e.g., His, GST, Fc) to aid purification and capture in binding assays. Where relevant, tag status can be considered when comparing activity or interaction data.
Formulation: Lyophilized from sterile PBS, pH 7.4. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.
Research interpretation
Research interpretation: Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.
