• Predicted molecular weight: 9.1 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-8 (IL-8), also known as CXCL8, is a CXC family member chemokine produced by macrophages and other cell types such as epithelial cells. There have been 17 different CXC chemokines described in mammals, that are subdivided into two categories, those with a specific amino acid sequence (or motif) of glutamic acid-leucine-arginine (or ELR for short) immediately before the first cysteine of the CXC motif (ELR-positive), and those without an ELR motif (ELR-negative). ELR-positive CXC chemokines such as IL-8 specifically induce the migration of neutrophils, and interact with chemokine receptors CXCR1 and CXCR2.

The recombinant human protein IL-8 has a predicted molecular weight of 9.1 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-8 human protein can be used in cell culture, as an IL-8 ELISA Standard, and as a Western Blot Control.

Country of Origin: USA..