Collagen is an inert, rigid protein found predominantly in skin, ligaments, bones and teeth. Its most distinctive attribute, essential to a transmitter of mechanical force, is inelasticity. Its fundamental structural unit is tropo-collagen, a molecular rod about 2600A in length and 15A in diameter and 300,000 molecular weight. In tendons these macromolecules, grouped as collagen fibrils, run parallel to the axis. In skin the fibrils are interlaced and branched. Collagen type II was purified by using differential salt precipitation, alcohol precipitation and DEAE chromatography. Multiple purification steps provide final preparations of collagen types in the native triple helical form, free of any non-collagenous protein. Contamination of other collagen types in a standard preparation is lower then five percent total. Storage and Stability: May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 6 months after receipt at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Purified protein from human intervertebral discs. 90% human collagen type II. Other Components: Collagen type I: <10%, collagen type III: <10%, collagen type IV: <1%, collagen type V: <1%, non-collagen proteins: <0.5%
Formulierung:
Supplied as a liquid in 0.5M acetic acid. No preservative added.
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