Measured by its binding ability in a functional ELISA.
When Recombinant Human (rh) CD55/DAF is coated at 1 μg/mL (100 μL/well), the concentration of rhCD97 that produces 50% of the optimal binding response is found to be approximately 0.5-2.5 μg/mL.
Source
Mouse myeloma cell line, NS0-derived human CD55/DAF protein
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Theoretical MW
36.0 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
61-75 kDa, reducing conditions
Publications
Read Publications using 2009-CD/CF in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 200 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human CD55/DAF Protein, CF
CD55 antigen
CD55 molecule, decay accelerating factor for complement (Cromer blood group)
CD55
CR
CRdecay accelerating factor for complement (CD55, Cromer blood group system)
CROMDAFcomplement decay-accelerating factor
DAF
decay accelerating factor for complement
TC
Background
CD55, also known as DAF or decay-accelerating factor, is a 70 - 75 kDa member of the RCA family of proteins. Human RCA (regulators of complement/C’ activation) proteins are products of chromosome 1 genes that are ubiquitously expressed on cells exposed to plasma complement proteins (1 - 4). A hallmark of RCA proteins is the presence of four to 30 SCRs (short consensus repeats; also called CCPs for C’ control protein modules) in their plasma-exposed regions. SCRs are characterized by a 60 - 65 amino acid (aa) module that contains a highly conserved Trp residue and two internal disulfide bonds that create a beta -barrel structure (1). Human CD55 is synthesized as a 381 aa precursor that contains a 34 aa signal sequence, a 319 aa mature region and a 28 aa C‑terminal prosegment (5, 6). The mature region contains four SCR modules and a C‑terminal O‑glycosylated extension (7). Following cleavage of the prosegment, a serine is exposed that serves as an anchor for a GPI-linkage (8). Multiple polymorphisms are found in the molecule. Alternate splicing also exists. One form that may not be translated shows an intron insertion in the prosegment, resulting in a 79 aa substitution for the standard C‑terminal 20 aas of the prosegment (6). Another form generates a truncated 199 aa precursor that cannot be membrane-bound and may not be secreted (9). Mature CD55 is 53% and 84% aa identical to mouse and monkey CD55, respectively. CD55 is known to bind CD97 via the first SCR (4). It also binds physiologically-generated C3 convertases with its second and third SCRs (7, 10). Binding results in an accelerated “decay”, or dissociation of active C3 convertases, thus blocking the development of C’ attack complexes on nonforeign cells (1, 2). Finally, viruses and bacteria are also known to utilize multiple SCR sites for infection (4).
Herbert, A. et al. (2002) Biochem. Soc. Trans. 30:990.
Miwa, T. and W-C. Song (2001) Int. Immunopharmacol. 1:445.
Hourcade, D. et al. (2000) Immunopharmacology 49:103.
Lea, S. (2002) Biochem. Soc. Trans. 30:1014.
Medof, M.E. et al. (1987) Proc. Natl. Acad. Sci. USA 84:2007.
Caras, I.W. et al. (1987) Nature 325:545.
Lukacik, P. et al. (2004) Proc. Natl. Acad. Sci. USA 101:1279.
Moran, P. et al. (1991) J. Biol. Chem. 266:1250.
Lublin, D.M. et al. (1994) Blood 84:1276.
Williams, P. et al. (2003) J. Biol. Chem. 278:10691.
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