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| Alternative Names | Human IL-4 protein、IL-4 |
| Biological Activity | |
| Expression System | |
| Formulation | |
| Gene ID | |
| Molecular Weight | |
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| Protein Length | |
| Purity | |
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| Target |
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: Human IL-4 protein、IL-4.
Species origin: Human.
Human Interleukin-4 (IL-4) is a cytokine that plays an important role in regulating inflammation and immune responses. It induces the differentiation of T cells to Th2 cells. This cytokine binds the IL-4 receptor that also binds another cytokine interleukin 13 (IL-13), which may explain the overlapping functions of IL-4 and IL-13. IL-4, originally designated as B-cell growth factor-1 (BSFl), is described in the supernatant of activated EL-4 thymoma cells as a factor that can co-stimulate B-cells activated with submitogenic concentrations of anti-IgM.
Endotoxin: <1 EU per μg of the protein by the LAL metho
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.
- Source species: Human
- Molecular weight: 15.1 kDa
- Protein length: The recombinant Human IL-4 consists of 129 amino acids and predicts a molecular mass of 15.1 kDa.
- Expression region: Amino acid sequence derived from Human IL-4 (His25-Ser153) (P05112-1) was expressed.
- Purity: > 96 % as determined by SDS-PAGE
- Biological activity: Measured in a cell proliferation assay using TF-1. The ED50 for this effect is typically 0.144 ng/mL. The specific activity of recombinant Human IL4 is approximately >6.94 x 106IU/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: No tag tags are commonly used to streamline purification and enable capture/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.
Formulation: Lyophilized from sterile 20 mM Tris-HCl, 150 mM NaCl, 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.
