Collagen Type I, bovineCatalog number: CO20121-0.1
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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. Bovine collagen type I 100%, bovine collagen II, IX, XI <0.1%; sheep collagen type I: 50 % (IHC estimated), bovine fibronectin <0.1%; human collagen type I <2%; chicken collagen type I <0.1% (estimates except sheep collagen I from solid phase RIA at dilution 1:500).
Immunogen: Purified collagen type I from bovine 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: Cattle, cross-reacting with sheep, swine and human (IHC)
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 ? 1:400 (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: Bovine skin or liver
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. Ricard-Blum S., Hartmann D.J., Herbage D., Payen-Meyran C., Ville G. (1982) Biochemical properties and immunolocalization of minor collagens in foetal calf cartilage. FEBS Letters 146, 343-347. 2. Ruggiero F., Petit B., Ronzière M.C., Farjanel J., Hartmann D.J., Herbage D. (1993) Composition and organization of the collagen network produced by fetal bovine chondrocytes cultured at high density. J. Histochem. Cytochem. 41, 867-875. 3. Ronziere M.C., Farjanel J., Freyria A.M., Hartmann D.J., Herbage D. (1997) Analysis of types I, II, III, IX and XI collagens synthesized by fetal bovine chondrocytes in high-density culture. Osteoarthritis Cart. 5, 205-214. 4. Laurent R, Nallet A, Obert L, Nicod L, Gindraux F. (2014) Storage and qualification of viable intact human amniotic graft and technology transfer to a tissue bank. Cell Tissue Bank.Jun;15(2):267-75.
Database Name: UniProt
Accession Number: P02453 (CO1A1_BOVIN)
Species Accession: Bovine