Background: Type I Collagen usually exists as a heterotrimer formed by alpha 1(I) and alpha 2(I) chains and is found in bone, cornea, skin and tendon. In foetal tissues also homotrimers of alpha-1(I) are found, but they are not constituents of normal adult tissues. 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. Porcine Collagen Type I, cross-reactivity with collagen type III <1%, Collagen type II, IV, V Elastin and Fibronectin <0.1%.
Positive Control: Porcine skin or tendon.
Immunogen: Purified collagen type I from porcine tendon.
Purification Method: affinity purified antibody lyophilized from phosphate buffered solution; no BSA and preservative added!.
Concentration: app. 1 mg/ml.
References: 1. Rousseau C.F, Gagnieu C.H. (2002) In vitro cytocompatibility of porcine type I atelocollagen crosslinked by oxidized glycogen. Biomaterials 23, 1503-1510. 2. Beard HK, Ryvar R, Brown R, Muir H. (1980) Immunochemical localization of collagen types and proteoglycan in pig intervertebral discs. Immunology. Oct;41(2):491-501.
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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