C3660
Complement C9 from human serum
≥150,000 C9H50 units/mg (using C9 deficient serum)
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Application
Complement C9 from human serum is an essential part of the terminal complement system. It has been a topic in cancer research, where extracellular phosphorylation by ecto-PK of K562 cells on serine residues may serve as a protective mechanism against complement in tumor cells. Additionally, it can be used as a biomarker (in fucosylated form) for squamous cell lung cancer, as patients tend to show elevated levels of C9 protein.
Biochem/physiol Actions
Complement component C9 is the final component of the membrane attack complex (MAC) responsible for cell lysis by complement. CD59 binds to both C8 and C9 and prevents assembly of an active MAC, protecting cells against lytic activity.
Quality
Functionally pure by a sensitive hemolytic assay using deficient sera.
Physical form
Supplied as a solution in phosphate buffered saline, 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.
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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Y Paas et al.
Archives of biochemistry and biophysics, 316(2), 780-788 (1995-02-01)
Ecto-protein kinases (ecto-PK), primarily of the serine/threonine kinase type, have been previously described on the surface of various normal, transformed, and tumor cells. We have found that in the presence of ATP and Mg2+, exogenously added substrates such as phosvitin
Phosphorylation of the complement component, C9, by an ecto-protein kinase of human leukemic cells
Paasa, Y., et al.
Immunopharmacology and Immunotoxicology, 42, 175-785 (1999)
Yoshimitsu Kuwabara et al.
PloS one, 13(6), e0198472-e0198472 (2018-06-13)
Immunoproteomic analysis was performed to identify unknown, pathology-related molecules in patients with seronegative (SN) obstetric antiphospholipid syndrome (APS) who clinically satisfied the diagnostic criteria for APS, but not the serological criteria. We collected peripheral blood from 13 SN-APS outpatients with
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