Recombinant IL-4, Human 
Datasheet
COA
MSDS
SHIP
Recombinant :
Recombinant IL-4, Human Source :
CHO Molecular Weight :
15 kDa, observed by non-reducing SDS-PAGE. Purity :
> 95% as analyzed by SDS-PAGE and HPLC. 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 x 10ˆ6 units/mg Physical Appearance :
Sterile Filtered White lyophilized (freeze-dried) powder. Formulation :
Lyophilized after extensive dialysis against PBS. AA Sequence :
HKCDITLQEIIKTLNSLTEQKTLCTELTVTDIFAASKNTTEKETFCRAATVLRQFYSH HEKDTRCLGATAQQFHRHKQLIRFLKRLDRNLWGLAGLNSCPVKEANQSTLENFLERL KTIMREKYSKCSS Endotoxin :
<0.2 EU/μg, determined by LAL method. Reconstitution :
Reconstituted in ddH2O or PBS at 100 μg/ml. Storage :
Lyophilized recombinant human Interleukin 4 (IL-4) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rhIL-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. 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. 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.Recombinant human IL-4 (rhIL-4) is a 129 amino acid protein expressed in mammalian CHO system. The approximate molecular weight is 15 kDa analyzed by non-reducing SDS-PAGE.
Recombinant IL-4, Human Source :
CHO Molecular Weight :
15 kDa, observed by non-reducing SDS-PAGE. Purity :
> 95% as analyzed by SDS-PAGE and HPLC. 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 x 10ˆ6 units/mg Physical Appearance :
Sterile Filtered White lyophilized (freeze-dried) powder. Formulation :
Lyophilized after extensive dialysis against PBS. AA Sequence :
HKCDITLQEIIKTLNSLTEQKTLCTELTVTDIFAASKNTTEKETFCRAATVLRQFYSH HEKDTRCLGATAQQFHRHKQLIRFLKRLDRNLWGLAGLNSCPVKEANQSTLENFLERL KTIMREKYSKCSS Endotoxin :
<0.2 EU/μg, determined by LAL method. Reconstitution :
Reconstituted in ddH2O or PBS at 100 μg/ml. Storage :
Lyophilized recombinant human Interleukin 4 (IL-4) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rhIL-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. 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. 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.Recombinant human IL-4 (rhIL-4) is a 129 amino acid protein expressed in mammalian CHO system. The approximate molecular weight is 15 kDa analyzed by non-reducing SDS-PAGE.
Blocking peptide available as BK0245-1mgP