- Predicted molecular weight: 17.4 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.
The IL-1 family of cytokines encompasses eleven proteins that each share a similar β-barrel structure and bind to Ig-like receptors. Several of the well characterized members of the IL-1-like cytokines play key roles in the development and regulation of inflammation. IL-1α (IL-1F1), IL-1β (IL-1F2), and IL-18 (IL-1F4) are well-known inflammatory cytokines active in the initiation of the inflammatory reaction and in driving Th1 and Th17 inflammatory responses. In contrast, IL-1 receptor antagonist (IL-1ra; IL-1F3) and IL-36 receptor antagonist (IL-36ra; IL-1F5) reduce inflammation by blocking the binding of the agonist receptor ligands.
The recombinant mouse protein IL-1 beta has a predicted molecular weight of 17.4 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-1B mouse protein can be used in cell culture, as an IL-1 beta ELISA Standard, and as a Western Blot Control.
Country of Origin: USA