Recombinant IL-4, Mouse
Catalogue Numbers: BK0246-10, BK0246-50
Sizes: 10μg, 50μg
Source: CHO
Molecular Weight: 15 kDa, observed by reducing SDS-PAGE.
Purity: > 95% as analyzed by SDS-PAGE and HPLC.
Biological Activity: ED50 < 2 ng/ml, measured in a cell proliferation assay using murine HT-2 cells, corresponding to a specific activity of >5 x 10ˆ5 units/mg.
Physical Appearance: Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation: Lyophilized after extensive dialysis against PBS.
AA Sequence: HIHGCDKNHLREIIGILNEVTGEGTPCTEMDVPNVLTATKNTTESELVCRASKVLRIFYLKHGKTPCLKKNSSVLMELQR
LFRAFRCLDSSISCTMNESKSTSLKDFLESLKSIMQMDYS
Endotoxin: < 0.2 EU/μg, determined by LAL method.
Reconstitution: Reconstituted in ddH2O or PBS at 100 μg/ml.
Storage: Lyophilized recombinant Murine Interleukin 4 (IL-4) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rmIL-4 should be stable up to 1 week at 4°C or up to 2 months at -20°C.
Usage: This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. For research use only.
Description: 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[1]. 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[2]. IL-4 also plays a major role in inflammation response and wound repair via activation of macrophage into M2 cells[3]. IL-4 is stabilized by three disulphide bonds forming a compact globular protein structure[4]. 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[5].