- Predicted molecular weight: 11.6 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.
CXCL12 (formerly stromal cell-derived factor 1) was originally described as a vital chemoattractant for B cells and monocytes. CXCL12 is unlike other chemokines in that it binds to one single chemokine receptor, CXCR4, which itself is recognized by no other chemokines. CXCL12 binds to its receptor CXCR4 to mediate cell-type specific physiological processes including cellular migration, survival, and apoptosis. CXCL12 is produced physiologically in various tissues and its receptor CXCR4 is also expressed on various haematopoietic and non-haematopoietic cells. CXCL12 and CXCR4 are essential for life as mice deficient in either gene are unable to survive much past birth. CXCL12 and CXCR4 play a role in many different diseases, including cancer, HIV, and rheumatoid arthritis.
The recombinant mouse protein CXCL12 has a predicted molecular weight of 11.6 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 CXCL12 mouse protein can be used in cell culture, as a CXCL12 ELISA Standard, and as a Western Blot Control.
Country of Origin: USA