• Predicted molecular weight: 13.3 kDa
• No endotoxins, TAGS, and carrier-free
• Naturally folded and post-translationally modified

IBI recombinant proteins are expressed inPichia pastoris(yeast) system which provides many advantages overE. colisystems. 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 13(IL-13) is secreted by many cell types, but especially T helper type 2 (Th2) cells. IL-13 is an important mediator of allergic inflammation and disease. In addition to effects on immune cells, IL-13 is implicated as a central mediator of the physiologic changes induced by allergic inflammation in many tissues. The functions of IL-13 overlap considerably with those of IL-4, especially with regard to changes induced on hematopoietic cells. Although IL-13 can induce immunoglobulin E (IgE) secretion from activated human B cells, deletion of IL-13 from mice does not markedly affect either Th2 cell development or antigen-specific IgE responses induced by potent allergens. In comparison, deletion of IL-4 abrogates these responses. Thus, rather than a lymphoid cytokine, IL-13 acts more prominently as a molecular bridge linking allergic inflammatory cells to the non-immune cells in contact with them, thereby altering physiological function.

The recombinant rat protein IL-13 has a predicted molecular weight of 13.3 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-13 rat protein can be used in cell culture, as an IL-13 ELISA Standard, and as a Western Blot Control.

Country of Origin: USA