Collagen Type II, bovineCatalog number: CO20221-0.1
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Type II collagen is an alpha1(II)-trimer, which forms 67 nm cross-banded fibrils. Typically it can be observed in cartilage and various tumours. 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 II 100%, bovine collagen XI <3.0 %; bovine collagen I and IX <0.1% (RIA at 1:200 dilution).
Immunogen: Purified collagen type II from bovine cartilage
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 horse and pig)
IHC(P), IFA, ELISA, RIA
Incubation Time: IHC(P) 60 min at RT or 2-8°C over night
Working Concentration: (purified, lyophilized) IFA 1:40, IHC(P) 1:100 - 1:500, 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: Bovine cartilage
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. Skalova A., Leivo I., Michal M. Saksela E. (1992) Analysis of collagen isotypes in crystalloid structures of salivary gland tumors. Hum. Pathol. 23, 748-754. 3. Skalova A., Michal M., Chlumska A., Leivo I. (1992) Collagen composition and ultrastructure of the so-called amianthoid fibres in palisaded myofibroblastoma. Ultrastructural and immunohistochemical study. J. Pathol. 167, 335-340. 4. 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.
Database Name: UniProt
Accession Number: P02459 (CO2A1_BOVIN)
Species Accession: Bovine