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. Bovine collagen type III 100%, bovine collagen I <5%; bovine collagen type II <0.1%; (solid phase RIA at 1:50 dilution), sheep collagen type III app. 50% (IHC).
Positive Control: Bovine skin or liver.
Immunogen: Purified collagen type III from bovine skin.
Purification Method: affinity purified antibody lyophilized from phosphate buffered solution; no BSA and preservative added!.
Concentration: app. 1 mg/ml.
References: 1. Guerret S., Govignon E., Hartmann D.J., Ronfard V. (2003) Long term remodeling of a bilayered living human skin equivalent (Apligraf®) grafted onto nude mice: immunolocalization of human cells and characterization of extracellular matrix. Wound Rep. Reg. 2. Perris R., Löfberg J., Fällström C., Von Boxberg Y., Olsson L., Newgreen D.F. (1990) Structural and compositional divergencies in the extracellular matrix encountered by neural crest cells in the white mutant axolotl embryo. Development 109, 533-551.
UniProt: P04258 (CO3A1_BOVIN).
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.
English
Deutsch
