Collagen Type V, humanCatalog number: CO20511-0.1
Collagen type V is found as short fibrils in skin, bone and placenta. Often it is found in conjunction with other collagen types, especially type I and III. 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 V 100%, human collagen type I, III and IV <0.1%, human fibronectin and laminin <0.1% (RIA at 1:100 dilution).
Immunogen: Purified collagen type V from human placenta
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, strong cross- reactivity with cattle and pig, very low with rat and mouse
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) ? 1:500, 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: Human placenta
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. 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. 2. Black A.F., Bouez C., Perrier E., Schlotmann K., Chapuis F., Damour O. (2005) Optimization and characterization of an Engineered human skin equivalent. Tissue Engineering 11, 723-733. 3. Chanut-Delalande H., Fichard A., Bernocco S., Garrone R., Hulmes D.J.S., Ruggiero F. (2001) Control of heterotypic fibril formation by collagen V is determined by chain stoichiometry. J. Biol. Chem. 276, 24352-24359. 4. Kleman J.P., Hartmann D.J., Ramirez F., Van der Rest M. (1992) The human rhabdomyosarcoma cell line A204 lays down a highly insoluble matrix composed mainly of 1 type-XI and 2 type-V collagen chains. Eur. J. Biochem. 210, 329-335.
Database Name: UniProt
Accession Number: P20908 (CO5A1_HUMAN)
Species Accession: Human