>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA. When Recombinant Human CD52 Fc Chimera
is immobilized at 1 μg/mL, 100 μL/well, the concentration of
Human Siglec‑10 Fc Chimera (Catalog # 2130-SL)
that produces 50% of the optimal binding
response is approximately 1-5 μg/mL.
When Recombinant Human CD52 Fc Chimera is coated at 1 µg/mL, Recombinant Human Siglec-10 Fc Chimera (Catalog # 2130-SL) binds with a typical ED50 of 1-5 μg/mL.
CD52, also known as CAMPATH-1 antigen,
HE5, and gp20, is a cell surface glycoprotein that can be targeted to induce
immune suppression by complement-mediated cell lysis (1, 2). Mature human CD52
is a 12 amino acid peptide that is tethered to the cell surface with a GPI
linkage (3). It carries a large tissue-specific carbohydrate structure which
increases the molecular weight of CD52 to 15-20 kDa (3-5). CD52 is expressed on
lymphocytes, monocytes, monocycte-derived dendritic cells, eosinophils, and
neutrophils (6-8), as well as on mature spermatozoa and epithelial cells lining
the male genital tract (5, 9, 10). It protects sperm against anti-sperm
antibodies by binding to C1q and inhibiting complement activation (11). CD52
ligation on CD4+ T cells induces a suppressive population of cells that
release soluble CD52 which then binds to Siglec-10 (12-14). This interaction inhibits
the proliferation of activated T cells and the cytotoxic function of autoimmune
CD8+ T cells in type 1 diabetes (13).
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Focarelli, R et al. (1998) Mol. Hum. Reprod. 4:119.
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Toh, B.-H. et al. (2013) Cell. Mol. Immunol. 10:379.
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