Background: Type III collagen is an alpha1(III)-trimer, which forms 67 nm cross-banded fibrils. Typically it can be observed in skin, cartilage and vitreous body. Collagens consist of a family of highly specialized glycoproteins of which at least 16 genetically distinct types are known to date. The basal unit of a collagen molecule consists of a triple-helical structure formed by 3 alpha-chains. Predominant amino acids are glycine, proline and hydroxproline. Regularly also lysines and hydroxylysines occur, which are responsible for cross-linkage and glycosylation of the protein chains. Different composition of alpha-chains and different glycosylation contribute to the high variability of collagens in different tissues and organs. Chicken collagen type III 100%, chicken collagen type I <5%.
Positive Control: Chicken skin or liver
Immunogen: Purified collagen type III from chicken skin
Purification Method: affinity purified antibody lyophilized from phosphate buffered solution; no BSA and preservative added!
Concentration: app. 1 mg/ml
References: 1. Robert J., Hartmann D.J., Sengel P. (1989) Production of fibronectin and collagen types I and III by chick embryo dermal cells cultured on extracellular matrix substrates. Int. J. Dev. Biol. 33, 267-275. 2. Robert J., Mauger A., Sengel P. (1989) Influence of various extracellular matrix components on the behavior of cultured chick embryo dermal cells. Int. J. Dev. Biol. 33, 227-237. 3. Duband J.L., Thiery J.P. (1987) Distribution of laminin and collagens during avian neural crest development. Development 101, 461-478. 4. Mauger A., Demarchez M., Herbage D., Grimaud J.A., Druguet M., Hartmann D.J. Foidart J.M., Sengel P. (1983) Immunofluorescent localization of collagen types I, III, IV, fibronectin and laminin during morphogenesis of scales and scaleless skin in the chick
UniProt: P12105 (CO3A1_CHICK)
Caution: *These antibodies are intended for in vitro research use only. They must not be used for clinical diagnostics and not for in vivo experiments in humans or animals.
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