This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 35.8 kDa. The protein migrates as 50-65 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Crystallography grade
CD55
Spezies: Human
Wirt: Insektenzellen
Recombinant
>95 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
SDS, ELISA, WB, Crys
CD55
Spezies: Human
Wirt: Tobacco (Nicotiana benthamiana)
Recombinant
SDS
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Lyophilized
Buffer
PBS, pH 7.4
Handhabung
Please avoid repeated freeze-thaw cycles.
Lagerung
-20 °C
Informationen zur Lagerung
No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C-8 °C), After reconstitution under sterile conditions for 1 month (4 °C-8 °C) or 3 months (-20 °C to -70 °C).
Kwon, Kim, Meyer, Di Bisceglie, Ray: "Distinct CD55 Isoform Synthesis and Inhibition of Complement-Dependent Cytolysis by Hepatitis C Virus." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 197, Issue 4, pp. 1127-36, (2017) (PubMed).
CD55 is also known as DAF or decay-accelerating factor, is a member of the RCA (regulators of complement activation) family characterized by four to 30 SCRs (short consensus repeats) in their plasma-exposed regions. CD55 /DAF is a 70 kDa membrane protein that regulates the complement system on the cell surface. It prevents the assembly of the C3bBb complex (the C3-convertase of the alternative pathway) or accelerates the disassembly of preformed convertase, thus blocking the formation of the membrane attack complex. This glycoprotein is broadly distributed among hematopoietic and non-hematopoietic cells. It is a determinant for the Cromer blood group system. CD55 is known to bind CD97 via the first SCR. It also binds physiologically-generated C3 convertases with its second and third SCRs. Binding results in an accelerated ""decay"", or dissociation of active C3 convertases, thus blocking the development of C' attack complexes on nonforeign cells. Finally, viruses and bacteria are also known to utilize multiple SCR sites for infection.