Collagen Type II, humanCatalog number: CO20211-0.1
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. Human collagen type II, cross-reactivity with human collagen type I, IX and XI <0.1%.
Immunogen: Purified collagen type II from human 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: Human
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: Human 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. 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. 2003, 11, 35-45. 2. Freyria AM, Ronzière MC, Cortial D, Galois L, Hartmann D, Herbage D, Mallein-Gerin F. (2009) Comparative phenotypic analysis of articular chondrocytes cultured within type I or type II collagen scaffolds. Tissue Eng Part A. 2009, 15, 1233-1245. 3. Perrier E., Ronzière M.C.C., Bareille R., Pinzano A., Mallein-Gerin F., Freyria A.M (2011) Analysis of collagen expression during chondrogenic induction of human bone marrow mesenchymal stem cells. Biotechnol Lett. 2011 Oct;33(10):2091-2101 4. Claus S., Mayer N., Aubert-Foucher E., Chajra H, Perrier-Groult E., Lafond J., Piperno M., Damour O., Mallein-Gerin F.Cartilage-(2012) Characteristic Matrix Reconstruction by Sequential Addition of Soluble Factors During Expansion of Human Articular Chondrocytes and Their Cultivation in Collagen Sponges - Tissue Eng Part C Methods. 2012 Feb;18(2):104-112.
Database Name: UniProt
Accession Number: P02458 (CO2A1_HUMAN)
Species Accession: Human
Collagen Type II, human
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