Thr22-Lys580 with Human IgG1 Fc at the C-Terminus
Greenlee-Wacker M C. et al. (2011) Membrane-Associated CD93 Regulates Leukocyte Migration and C1q-Hemolytic Activity during Murine Peritonitis. J. Immunol. 187: 3353-3361.
Nepomuceno R R. et al. (1997) cDNA cloning and primary structure analysis of C1qRp, the human C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro. Immunity. 6: 119-129.
Nepomuceno R R. et al. (1998) C1qRp, the C1q receptor that enhances phagocytosis, is detected specifically in human cells of myeloid lineage, endothelial cells, and platelets. J. Immunol. 160: 1929-1935.
Complement component 1q (C1q) receptor 1 (C1qR1, also known as C1qRp, or cluster of differentiation 93-CD93) is a 126-kDa type 1 transmembrane glycoprotein expressed in endothelial and hematopoietic cells, and responsible for C1q-induced phagocytosis. CD93 contains one C-type lectin domain and five EGF-like domains. Mature human CD93 consists of a 557 amino acid (aa) extracellular domain (ECD) with one C‑type lectin domain, four tandem EGF‑like domains, and a mucin‑like domain, followed by a 21 aa transmembrane segment and a 51 aa cytoplasmic domain. CD93 is receptor for C1q, mannose-binding lectin (MBL2) and pulmonary surfactant protein A (SPA). Soluble CD93 promotes the differentiation of monocytes to macrophages, phagocytosis of apoptotic cells, and inflammatory responsiveness to multiple TLR ligands.
1μg (R: reducing condition, N: non-reducing condition).
The purity of C1qR1/CD93 Fc Chimera Protein, Human is greater than 95% as determined by SEC-HPLC.
Immobilized C1qR1/CD93 Fc Chimera Protein, Human (Cat. No. UA011087) at 5.0μg/mL (100μL/well) can bind IGFBP-7 His Tag, Human (Cat. No. UA010394) with EC50 of 1.12-1.31μg/mL.