IL4 is produced mainly by a sub-population of activated T helper cells that also secrete IL5 and IL6. The biological activities of IL4 are mediated by a specific receptor, the extracellular domain of which is related to the receptors for EPO, IL6, and the beta chain of the IL2 receptor. IL4 participates in several B-cell activation processes as well as of other cell types. A co-stimulator of DNA-synthesis, IL4 induces the expression of class II MHC molecules on resting B-cells, enhances both secretion and cell surface expression of IgE and IgG1, and also regulates the expression of the low affinity Fc receptor for IgE on both lymphocytes and monocytes. Pre-treatment of macrophages with IL4 prevents the production of IL1, TNF-alpha and prostaglandins in response to activation of the cells by bacterial endotoxins or IFN-gamma. Recombinant Human IL4 expressed in human 293 cells is a glycosylated monomer with an apparent molecular mass of 14 and 19 kDa.
<1 EU/µg of recombinant protein as determined by the LAL method
Biological Activity Comment
The EC(50) as determined by the dose-dependent simulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) was found to be ≤0.6 ng/mL.
Weight
14 and 19 kDa, monomer, glycosylated
Description
A quick spin of the vial followed by reconstitution in sterile 1xPBS containing 0.1% endotoxin-free recombinant human serum albumin (HSA).
Format
Lyophilized Powder1x PBS
Purity
>95% as determined by SDS-PAGE
Storage
The lyophilized protein is stable for at least one year from date of receipt at -70°C. Upon reconstitution, this cytokine can be stored in working aliquots at 2° - 8°C for one month, or at -20°C for six months. Avoid repeated freeze/thaw cycles.