Human CD93/C1qR (His Tag) recombinant protein

Human CD93/C1qR (His Tag) recombinant protein

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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.

Complement component C1q receptor

AA4.1; ECSM3; CD93; DJ737E23.1; C1QRP; MXRA4; 6030404G09RIK; C1QR(P); AA145088; CDW93; LY68; C1QR; RP23-70N3.4; AW555904; C1QR1

Q9NPY3

CD93; C1QR1; MXRA4

Human Cells

A DNA sequence encoding the human CD93 (Q9NPY3) extracellular domain (Met 1-Lys 580) was fused with a polyhistidine tag at the C-terminus.

Human

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.

> 90 % as determined by SDS-PAGE