Tropoelastin

E. Coli

Tropoelastin is produced from full length sequence as a full-length protein. Tropoelastin is the soluble pre-cursor to elastin as it is made in vivo. In the body, a leader sequence is cleaved off of tropoelastin which takes it from a soluble format inside the cell to a solid cross-linked elastin fibrous protein. One major advantage of being able to work with a full length tropoelastin is that it retains much of its native properties, far more than any peptide sequence.

Yes – there is a poly-His tag at the carboxy terminus.

No.

The tropoelastin is soluble in water at a pH below 6.5 to 7 and at temperatures below 30°C. Tropoelastin will tend to precipitate at higher pH and temperatures approaching 37°C. Solubility in water improves with lower pH. Tropoelastin is soluble in acetic acid.

Tropoelastin will form a stable solution at a concentration of up to 100 mg/ml.

Tropoelastin is soluble in butanol and hexafluoro propanol.

We are able to purify the Tropoelastin to near-homogeneity using affinity chromatography. The laddering on the SDS is a result of the Tropoelastin hypersensitive protease cleavage site on the Tropoelastin molecule. Small residual amounts of protease during production clip the Tropoelastin and cause some of those smaller bands to appear.

You can assume that the material is pure Tropoelastin without additional impurities, stabilizers, fillers, etc.