IL-4

Product Information
Primary Accession	P05112
Species	Human
Sequence	His25-Ser153
Purity	> 95% as analyzed by SDS-PAGE > 95% as analyzed by HPLC
Endotoxin Level	< 0.2 EU/ µg of protein by gel clotting method
Biological Activity	ED₅₀ < 0.25 ng/ml, measured in a cell proliferation assay using TF-1 human erythroleukemic cells, corresponding to a specific activity of > 4.0 × 10⁶ units/mg
Expression System	CHO
Formulation	Lyophilized after extensive dialysis against PBS.
Reconstitution	It is recommended that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute the lyophilized powder in ddH₂O or PBS up to 100 µg/ml.
Storage & Stability	Upon receiving, this product remains stable for up to 6 months at lower than -70°C. Upon reconstitution, the product should be stable for up to 1 week at 4°C or up to 3 months at -20°C. For long term storage it is recommended that a carrier protein (example 0.1% BSA) be added. Avoid repeated freeze-thaw cycles.

Additional Information
Gene ID	3565
Other Names	Interleukin-4, IL-4, B-cell stimulatory factor 1, BSF-1, Binetrakin, Lymphocyte stimulatory factor 1, Pitrakinra, IL4
Target Background	Interleukin-4 (IL-4) is a pleiotropic cytokine regulates diverse T and B cell responses including cell proliferation, survival, and gene expression. It has important effects on the growth and differentiation of different immunologically competent cells. Interleukin-4 is produced by mast cells, T cells, and bone marrow stromal cells. IL-4 regulates the differentiation of native CD4⁺ T cells (Th0 cells) into helper Th2 cells, and regulates the immunoglobulin class switching to the IgG1 and IgE isotypes. IL-4 has numerous important biological functions including stimulating B-cells activation, T-cell proliferation and CD4⁺ T-cells differentiation to Th2 cells. It is a key regulator in hormone control and adaptive immunity. IL-4 also plays a major role in inflammation response and wound repair via activation of macrophage into M2 cells. IL-4 is stabilized by three disulphide bonds forming a compact globular protein structure. Four alpha-helix bundle with left-handed twist is dominated half of the protein structure with 2 overhand connections and fall into a 2-stranded anti-parallel beta sheet.

For Research Use Only. Not For Use In Diagnostic Procedures.

Protein Information
Name	IL4
Function	Cytokine secreted primarily by mast cells, T-cells, eosinophils, and basophils that plays a role in regulating antibody production, hematopoiesis and inflammation, and the development of effector T-cell responses (PubMed:1993171, PubMed:3016727). Induces the expression of class II MHC molecules on resting B-cells. Enhances both secretion and cell surface expression of IgE and IgG1 (PubMed:1993171). Also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes (PubMed:2521231). Positively regulates IL31RA expression in macrophages. Stimulates autophagy in dendritic cells by interfering with mTORC1 signaling and through the induction of RUFY4. In addition, plays a critical role in higher functions of the normal brain, such as memory and learning (By similarity). Upon binding to IL4, IL4R receptor dimerizes either with the common IL2R gamma chain/IL2RG to produce the type 1 signaling complex, located mainly on hematopoietic cells, or with the IL13RA1 to produce the type 2 complex, which is also expressed on nonhematopoietic cells (PubMed:10219247, PubMed:11526337, PubMed:18243101). Engagement of both types of receptors initiates JAK3 and to a lower extend JAK1 phosphorylation leading to activation of the signal transducer and activator of transcription 6/STAT6 (PubMed:7721895).
Cellular Location	Secreted.