Catalogue

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. Chicken collagen type III 100%, chicken collagen type I <5%.

Source

Immunogen: Purified collagen type III from chicken skin

Product
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

Specificity

Species Reactivity: Chicken, cross-reaction with human, bovine, mouse and rat collagen type III <0,1%

Applications
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 1:40, IHC(P) 1:500, ELISA > 1:200

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 or liver

Storage
-20°C

Caution
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 our company accepts no liability for any inaccuracies or omissions in this information.

References
1. 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. 2. Robert J., Mauger A., Sengel P. (1989) Influence of various extracellular matrix components on the behavior of cultured chick embryo dermal cells. Int. J. Dev. Biol. 33, 227-237. 3. Duband J.L., Thiery J.P. (1987) Distribution of laminin and collagens during avian neural crest development. Development 101, 461-478. 4. Mauger A., Demarchez M., Herbage D., Grimaud J.A., Druguet M., Hartmann D.J. Foidart J.M., Sengel P. (1983) Immunofluorescent localization of collagen types I, III, IV, fibronectin and laminin during morphogenesis of scales and scaleless skin in the chick

Protein Reference(s)

Database Name: UniProt

Accession Number: P12105 (CO3A1_CHICK)

Species Accession: Chicken