Collagen Type I, chickenCatalog number: CO20131-0.1
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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. Chicken collagen type I 100%, chicken collagen type II, III and V <0.1%; chicken fibronectin <0.1% RIA at 1:1000 dilution..
Immunogen: Purified collagen type I from chicken skin
affinity purified antibody lyophilized from phosphate buffered solution; no BSA and preservative added!
Purification Method: affinity purified antibody lyophilized from phosphate buffered solution; no BSA and preservative added!
Secondary Reagents: Anti-rabbit IgG-conjugates, e.g. anti-rabbit IgG:FITC (Art. No. FI-1000) or anti-rabbit IgG:DyLight488 (Art. No. DI-1488).
Concentration: app. 1 mg/ml
Species Reactivity: Chicken, collagen type I human, mouse, rat, cattle <0.1%
IHC(P), IFA, ELISA, RIA, IB/WB
Incubation Time: IHC(P) 60 min at RT or 2-8°C over night
Working Concentration: (purified, lyophilized) IFA ? 1:80, IHC(P) ? 1:1000, ELISA ? 1:200 (OD ? 500)
Pre-Treatment: After de-waxing the tissue slices they are treated with 0.2% hyaluronidase (app. 300 U/mg e.g. Art. No. HYA02-50) in TBS 15 min at 37°C. Thereafter non-specific binding is blocked by blocking serum or 3% BSA in TBS. For peroxidase systems blocking with 1% peroxide solution in TBS for 30 min at RT is recommended.
Positive Control: Chicken skin
This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals. It may contain hazardous ingredients. Please refer to the Safety Data Sheets (SDS) for additional information and proper handling procedures. Dispose product remainders according to local regulations.This datasheet is as accurate as reasonably achievable, but Exalpha Biologicals accepts no liability for any inaccuracies or omissions in this information.
1. Mauger A., Demarchez M., Herbage D., Grimaud J.A., Druguet M., Hartmann D., Sengel P. (1982) Immunofluorescent localization of collagen types I and III, and of fibronectin during feather morphogenesis in the chick embryo. Dev. Biol. 94, 93-105. 2. Tacchetti C., Quarto R., Nitsch L., Hartmann D.J., Cancedda R. (1987) In vitro morphogenesis of chick embryo hypertrophic cartilage. J. Cell. Biol. 105, 999-1006. 3. 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. 4. Farjanel J., Hartmann D.J., Guidet B., Luquel L., Offenstadt G. (1993) Four markers of collagen metabolism as possible indicators of disease in the adult respiratory distress syndrome. Am. Rev. Respir. DIs. 147, 1091-1099.
Database Name: UniProt
Accession Number: P02457