- Predicted molecular weight: 13.6 kDa
- No endotoxins, TAGS, and carrier-free
- Naturally folded and post-translationally modified
IBI recombinant proteins are expressed in Pichia pastoris (yeast) system which provides many advantages over E. coli systems. Yeast systems promote proper protein folding and post-translational modifications for greater bio-activity. The recombinant proteins are endotoxin free and are purified without HIS-TAGS or any other TAG. IBI’s yeast expression system has proven to produce more active proteins that more closely resemble their host form.
Interleukin-4 (IL-4)induces differentiation of naive helper T cells (Th0 cells) to Th2 cells. Upon activation by IL-4, Th2 cells subsequently produce additional IL-4. IL-4 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. It is a key regulator in humoral and adaptive immunity. IL-4 induces B-cell class switching to IgE, and up-regulates MHC class II production. Overproduction of IL-4 is associated with allergies.
The recombinant mouse protein IL-4 has a predicted molecular weight of 13.6 kDa.
All IBI recombinant proteins are lyophilized and shipped at room temperature without carrier protein. Proteins can be reconstituted in sterile PBS with at least 0.1% of carrier protein such as BSA or cell assay media.
The IL-4 mouse protein can be used in cell culture, as an IL-4 ELISA Standard, and as a Western Blot Control.
Country of Origin: USA