C3160
Complement C5 from human serum
≥90% (SDS-PAGE), >100,000 C5H50 units/mg protein
Synonim(y):
C5 human, Complement C5
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Wybierz wielkość
0.1 MG
1560,00 zł
1560,00 zł
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Informacje o tej pozycji
Form:
solution
Assay:
≥90% (SDS-PAGE)
Biological source:
human serum
Przejdź do
Pomoc techniczna
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Pozwól nam pomóc1 of 4
Ta pozycja | |||
|---|---|---|---|
| biological source human serum | biological source human | biological source human serum | biological source human |
| technique(s) activity assay: suitable | technique(s) activity assay: suitable | technique(s) activity assay: suitable | technique(s) activity assay: suitable |
| assay ≥90% (SDS-PAGE) | assay - | assay ≥85% (SDS-PAGE) | assay ≥85% (SDS-GE) |
| concentration 1 mg/mL in PBS, pH 7.2 | concentration - | concentration 1 mg/mL in 10 mM sodium phosphate, 150 mM sodium chloride, pH 7.2 | concentration - |
| form solution | form solution | form solution | form solution |
| UniProt accession no. | UniProt accession no. | UniProt accession no. | UniProt accession no. |
Application
Complement C5 is part of the terminal sequence in the complement pathway. In particular, it is cleaved into C5a and C5b which are responsible for chemotaxis, inflammation, and initiating the formation of the membrane attack complex (MAC). Drugs that inhibit complement C5 have been used in Paroxysmal nocturnal hemoglobinuria (PNH) patients to lessen thrombotic complications by lessening intravascular hemolysis.
Biochem/physiol Actions
Complement component C5 is processed by convertase enzymes in a cascade modulated in a unique way. The multi-subunit catalytic complex initially shows little activity against C5, but instead cleaves C3. A C3 cleavage product C3b covalently attaches to the complex and shifts its specificity to C5 by a factor of 1000.
Analysis Note
Functionally active by a sensitive hemolytic assay.
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.
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Klasa składowania
10 - Combustible liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
The role of complement inhibition in PNH.
Hillmen P.
Hematology / the Education Program of the American Society of Hematology. American Society of Hematology. Education Program, 2008(1), 116-123 (2008)
A M Risitano et al.
Mini reviews in medicinal chemistry, 11(6), 528-535 (2011-05-13)
Paroxysmal nocturnal hemoglobinuria (PNH) is a hematological disorder characterized by complementmediated hemolytic anemia, thrombophilia and bone marrow failure. The clinical hallmark of PNH is evident chronic hemolysis due to the absence of the complement regulators CD55 and CD59 on PNH
Peter Hillmen et al.
The New England journal of medicine, 350(6), 552-559 (2004-02-06)
Paroxysmal nocturnal hemoglobinuria (PNH) arises from a somatic mutation of the PIG-A gene in a hematopoietic stem cell and the subsequent production of blood cells with a deficiency of surface proteins that protect the cells against attack by the complement
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