C5938
Complement factor I from human plasma
>90% (SDS-PAGE)
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Application
Complement factor I from human plasma has been used in a case study of glucose-starved Staphylococcus aureus. Complement factor I from human plasma has also been used to study the human complement cascade of proteolysis as a target of laser irradiation.
Biochem/physiol Actions
Protease which cleaves and inactivates C3b and C4b
Physical form
Supplied as a 1mg/ml solution in PBS, pH 7.2
Other Notes
View more information on the complement pathway at www.sigma-aldrich.com/enzymeexplorer
Disclaimer
RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.
Storage Class Code
10 - Combustible liquids
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Molecular immunology, 48(14), 1611-1620 (2011-05-03)
Factor I (FI) is a crucial inhibitor controlling all complement pathways due to its ability to degrade activated complement proteins C3b and C4b in the presence of cofactors such as factor H, C4b-binding protein, complement receptor 1 or CD46. Complete
The study of the human complement cascade of proteolysis as a target of laser irradiation
Biomeditsinskaia Khimiia, 55, 68-72 (2012)
Clinical journal of the American Society of Nephrology : CJASN, 7(5), 748-756 (2012-03-10)
The principle defect in dense deposit disease and C3 glomerulonephritis is hyperactivity of the alternative complement pathway. Eculizumab, a monoclonal antibody that binds to C5 to prevent formation of the membrane attack complex, may prove beneficial. In this open-label, proof
Molecular & cellular proteomics : MCP, 11(9), 558-570 (2012-05-05)
The cellular amount of proteins not only depends on synthesis but also on degradation. Here, we expand the understanding of differential protein levels by complementing synthesis data with a proteome-wide, mass spectrometry-based stable isotope labeling with amino acids in cell
Factor H-related protein 4 activates complement by serving as a platform for the assembly of an alternative pathway C3 convertase via its interaction with C3b
The Journal of Biological Chemistry, 287(23), 19258-19236 (2012)
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