- Predicted molecular weight: 15.0 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.
IL-17A is a member of the IL-17 family, whichis comprised of 6 members [IL-17A, IL-17B, IL-17C, IL-17D, IL-17E (also called IL-25), and IL-17F]. IL-17 family members are involved in numerous immune regulatory functions, including inducing and mediating pro-inflammatory responses and allergic responses. IL-17 induces the production of many other cytokines (IL-6, G-CSF, GM-CSF, IL-1 beta, TGF-beta, and TNF-alpha), chemokines, including IL-8 (CXCL8), GRO-alpha (CXCL1)and MCP-1 (CCL2)and prostaglandins from many cell types (fibroblasts, endothelial cells, epithelial cells, keratinocytes and macrophages).
The recombinant mouse protein IL-17A has a predicted molecular weight of 15.0 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-17A mouse protein can be used in cell culture, as an IL-17A ELISA Standard, and as a Western Blot Control.
Country of Origin: USA