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, 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. Human type III collagen purified by serial salt precipitations, alcohol precipitation and DEAE chromatography of an acetic acid extraction of human placenta, following mild pepsin digestion. Composition: (a1(III))3, native triple helix. Ability to form native helical structure verified by ORD measurement, competence in microfibril formation and reactivity with anti-collagen type-specific monoclonal antibodies. Contaminants: >2% collagen type I, >2% collagen type IV, >1% collagen type V and 0.5% non-collagen proteins 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.