Human CD93 / C1QR1 Protein (His Tag)

C1QR1, C1qR(P), C1qRP, CDw93, ECSM3, MXRA4, dJ737E23.1

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Catalog Number	P12589-H08H
Organism Species	Human
Host	Human Cells
Synonyms	C1QR1, C1qR(P), C1qRP, CDw93, ECSM3, MXRA4, dJ737E23.1
Molecular Weight	The secreted recombinant human CD93 comprises 570 amino acids and has a predicted molecular mass of 59.6 kDa. As a result of glycosylation, rh CD93 migrates as an approximately 100 kDa band in SDS-PAGE under reducing conditions.
predicted N	Thr 22
SDS-PAGE
Purity	> 90 % as determined by SDS-PAGE
Protein Construction	A DNA sequence encoding the human CD93 (Q9NPY3) extracellular domain (Met 1-Lys 580) was fused with a polyhistidine tag at the C-terminus.
Bio-activity
Research Area	Immunology |Innate Immunity |Complement System
Formulation	Lyophilized from sterile PBS, pH 7.4 1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background	CD93 or C1q receptor 1 (C1qR) is an about 120 kDa O-sialoglycoprotein that within the hematopoietic system is selectively expressed on cells of the myeloid lineage. CD93/C1qR is a highly glycosylated transmembrane protein expressed on monocytes, neutrophils, endothelial cells, and stem cells. CD93 was originally identified as a myeloid cell-surface marker and subsequently associated with an ability to modulate phagocytosis of suboptimally opsonized immunoglobulin G and complement particles in vitro. CD93/C1qR, a receptor expressed during early B-cell development, is reinduced during plasma-cell differentiation. High CD93/CD138 expression was restricted to antibody-secreting cells both in T-dependent and T-independent responses as naive, memory, and germinal-center B cells remained CD93-negative. CD93 was expressed on (pre)plasmablasts/plasma cells, including long-lived plasma cells that showed decreased cell cycle activity, high levels of isotype-switched Ig secretion, and modification of the transcriptional network. CD93 is important for the maintenance of plasma cells in bone marrow niches.
Reference	Bohlson SS, et al. (2005) CD93 is rapidly shed from the surface of human myeloid cells and the soluble form is detected in human plasma. J Immunol. 175(2): 1239-47. Norsworthy PJ, et al. (2004) Murine CD93 (C1qRp) contributes to the removal of apoptotic cells in vivo but is not required for C1q-mediated enhancement of phagocytosis. J Immunol. 172(6): 3406-14. Chevrier S, et al. (2009) CD93 is required for maintenance of antibody secretion and persistence of plasma cells in the bone marrow niche. Proc Natl Acad Sci U S A. 106(10): 3895-900.