Analysis Note

Retention of native structure was confirmed by ability to form microfibrils.

General description

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

Product Source: Human placenta, negative for HbsAG, HCV and HIV 1 & 2 antibodies.

COL3A1 is the gene responsible for producing the pro-alpha1(III) chain of type III procollagen. Type III collagen, which adds structure and strength to connective tissues, is found in many places in the body, especially skin, lung, intestinal walls, and the walls of blood vessels. Collagen III is initially produced as procollagen, a protein consisting of three pro-alpha1(III) chains that form the triple-stranded, rope-like molecule. After being synthesized, the procollagen molecule is modified by the cell. Enzymes modify the amino acids lysine and proline in the protein strands by adding chemical groups that are necessary for the strands to form a stable molecule and then later to crosslink to other molecules outside the cell. Other enzymes add sugars to the protein. The type III procollagen molecules are released from the cell and are processed by enzymes that clip small segments off either end of the molecules to form mature collagen. The mature collagen molecules assemble into fibrils. Cross-linking between molecules produces a very stable fibril, contributing to collagen′s tissue strengthening function.{http://ghr.nlm.nih.gov}

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

Physical form

Liquid in 0.5 M acetic acid, pH 2.5.

Storage and Stability

Maintain at -20°C in undiluted aliquots for up to 12 months from date of receipt. Avoid repeated freeze/thaw cycles.