Recombinant Mouse IL-4 protein

Background

Interleukin-4 (IL-4) is a pleiotropic cytokine that induces differentiation of naive helper T cells (Th0 cells) to Th2 cells. It is produced by mast cells, activated T cells and bone marrow stromal cells. It has many biological roles, including the stimulation of activated B-cell and T-cell proliferation, and the differentiation of CD4+ T-cells into Th2 cells. IL-4 enhances both secretion and cell surface expression of IgE and IgG1 and also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. The mouse IL-4 has a compact, globular fold, stabilised by 3 disulphide bonds and contains 121 amino acids residues which is a single non-glycosylated polypeptide. The human IL-4 shares about 40 % a.a. sequence identity with mouse/rat IL-4 and they are species-specific in their activities.

Expression system

Escherichia coli.

Purity

> 97 % by SDS-PAGE and HPLC analyses.

Molecular weight

Approximately 13.5 kDa, a single non-glycosylated polypeptide chain containing 121 amino acids.

Endotoxin

Less than 1 EU/μg of rMuIL-4 as determined by LAL method.

Form

Sterile Filtered White lyophilized (freeze-dried) powder. Formulation Lyophilized from a 0.2 μm filtered solution in PBS, pH 7.4.

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