Human Type I Collagen-Solution
Cat. No.:
1200-01S
Purified Human Type I Collagen solution for use as a coating material and standard.
$231.00
Description | Collagen is the main structural protein in the extracellular space and is the most abundant protein in the ECM. Collagens are divided into two classes - fibril (types I, II, III, V) and non-fibril (types IV, VI). Type I collagen is the most abundant collagen and is expressed in almost all connective tissues including skin, tendon, and bone tissue. It is also the predominant component of the interstitial matrix. Type I collagen mutations are associated in a range of diseases including osteogenesis imperfecta and Ehlers-Danlos syndrome. Type I collagen consists of two α1(I) chains and one α2(I) chain. |
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Source | Placental villi |
Purity | > 90% by SDS-PAGE |
Purification Method | Controlled and limited pepsin digestion followed by selective salt precipitation |
Buffer Formulation | 500 mM acetic acid |
Concentration | 0.5 mg/mL |
Volume | 1.0 mL |
Recommended Storage | 2-8°C |
Applications | ELISA – Quality tested 1-15,26 SDS-PAGE – Quality tested Western Blot – Reported in literature 16,17, 20, 21 Surface Plasmon Resonance – Reported in literature 27,28 Cell Culture – Reported in literature 18,19 Stimulation Studies – Reported in literature 25 Coating Material for – Adhesion Studies – Reported in literature 20-24 Autoimmune Studies – Reported in literature 26 Blood Disorder Studies – Reported in literature 27, 28 Differentiation Studies – Reported in literature 29 ECM Interaction Studies – Reported in literature 30-32 Migration Studies – Reported in literature 33 |
Documentation
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- 17. Atamas SP, Luzina IG, White B, inventors; University of Maryland, Baltimore, assignee. Therapeutic targeting of PARC/CCL18 and its signaling in pulmonary fibrosis. United States patent application publication US 2006/0009452 A1. 2006 Jan 12. (WB, Positive Control)
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- 25. Hawrylko E, Spertus A, Mele CA, Oster N, Frieri M. Increased interleukin-2 production in response to human type I collagen stimulation in patients with systemic sclerosis. Arthritis Rheum. 1991;34:580-7. (Stimulation Studies)
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- 27. Siekmann J, Turecek PL, Schwarz HP. The determination of von Willebrand factor activity by collagen binding assay. Haemophilia. 1998;4:15-24. (SPR, Coating, Blood Disorder Studies)
- 28. Li F, Moake JL, McIntire LV. Characterization of von Willebrand factor interaction with collagens in real time using surface plasmon resonance. Ann Biomed Eng. 2002;30:1107-16. (SPR, Coating, Blood Disorder Studies)
- 29. Andrianarivo AG, Robinson JA, Mann KG, Tracy RP. Growth on type I collagen promotes expression of the osteoblastic phenotype in human osteosarcoma MG-63 cells. J Cell Physiol. 1992;153:256-65. (Coating, Differentiation Studies)
- 30. Bidanset DJ, Guidry C, Rosenberg LC, Choi HU, Timpl R, Hook M. Binding of the proteoglycan decorin to collagen type VI. J Biol Chem. 1992;267:5250-6. (Coating, ECM Interaction Studies)
- 31. Hocking AM, Strugnell RA, Ramamurthy P, McQuillan DJ. Eukaryotic expression of recombinant biglycan. Post-translational processing and the importance of secondary structure for biological activity. J Biol Chem. 1996;271:19571-7. (Coating, ECM Interaction Studies)
- 32. Liu Z, Han X, Chen R, Zhang K, Li Y, Fruge S, et al. Microfluidic mapping of cancer cell-protein binding interaction. ACS Appl Mater Interfaces. 2017;9:22143-8. (Coating, ECM Interaction Studies)
- 33. Ji J, Zhao L, Budhu A, Forgues M, Jia H, Qin L, et al. Let-7g targets collagen type I α2 and inhibits cell migration in hepatocellular carcinoma. J Hepatol. 2010;52:690-7. (Coating, Migration Studies)
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