Human CD55/DAF (Fc Tag) recombinant protein

Human CD55/DAF (Fc Tag) recombinant protein

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CD55, also well known as decay-accelerating factor (DAF), 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. It is a major regulator of the alternative and classical pathways of complement activation and is expressed on all serum-exposed cells. CD55 is physiologically acting as an inhibitor of the complement system, but is also broadly expressed in malignant tumours. DAF seems to exert different functions beyond its immunological role such as promotion of tumorigenesis, decrease of complement mediated tumor cell lysis, autocrine loops for cell rescue and evasion of apoptosis, neoangiogenesis, invasiveness, cell motility. It is commonly hijacked by invading pathogens, including many enteroviruses and uropathogenic Escherichia coli, to promote cellular attachment prior to infection. This 70-75 kDa glycoprotein CD55 containing four SCR modules is involved in the regulation of the complement cascade. It inhibits complement activation by suppressing the function of C3/C5 convertases, thereby limiting local generation or deposition of C3a/C5a and membrane attack complex (MAC or C5b-9) production. DAF has been identified as a ligand for an activation-associated, seven-transmembrane lymphocyte receptor, CD97, which is a receptor mediating attachment and infection of several viruses and bacteria. In addition, it has been shown that DAF regulates the interplay between complement and T cell immunity in vivo, and thus may be implicated in immune and tumor biology.

Complement decay-accelerating factor

P08174

CD55; CR; DAF

Human Cells

A DNA sequence encoding the human CD55 precursor (NP_000565.1) (Met 1-Ser 353) was expressed with the C-terminal fused Fc region of human IgG1.

Human

The recombinant human CD55/Fc is a disulfide-linked homodimeric protein. The reduced monomer consists of 557 amino acids and has a predicted molecular mass of 61.7 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rhCD55/Fc monomer is approximately 95-105 kDa due to glycosylation.

> 90 % as determined by SDS-PAGE

Measured by its binding ability in a functional ELISA. Immobilized recombinant human CD97 at 10 μg/ml (100 μl/well) can bind recombinant human CD55 at a linear range of 0.46-30 μg/ml.