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C3160

Sigma-Aldrich

Complement C5 from human serum

≥90% (SDS-PAGE), >100,000 C5H50 units/mg protein

Synonym(s):
C5 human, Complement C5
CAS Number:
MDL number:

biological source

human serum

Quality Level

Assay

≥90% (SDS-PAGE)

form

solution

specific activity

>100,000 C5H50 units/mg protein

concentration

1 mg/mL in PBS, pH 7.2

technique(s)

activity assay: suitable

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... C5(727)

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This Item
C2910C8195C0913
assay

≥90% (SDS-PAGE)

assay

≥85% (SDS-GE)

assay

-

assay

-

form

solution

form

solution

form

solution

form

liquid

specific activity

>100,000 C5H50 units/mg protein

specific activity

≥3000 C3H50 units/mg (using C3 deficient serum)

specific activity

≥300,000 C4H50 units/mg protein

specific activity

-

concentration

1 mg/mL in PBS, pH 7.2

concentration

-

concentration

-

concentration

-

technique(s)

activity assay: suitable

technique(s)

activity assay: suitable

technique(s)

activity assay: suitable

technique(s)

activity assay: suitable

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.

Quality

Functionally active by a sensitive hemolytic assay.

Other Notes

Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Customers Also Viewed

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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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