Purification of C1q receptors and functional analysis.
The recognition subunit of C1, C1q, has emerged as an important player in various pathophysiologic conditions largely in part due to its ability to interact with pathogen-associated or cell surface expressed ligands and receptors. Identification and purification of these molecules is therefore of paramount importance if we are to procure valuable information with regards to the structure, function, and cell surface distribution. Since the interaction of C1q is better served when the receptors are purified from homologous species, we discuss here a simple guideline for the purification and characterization of the two C1q receptors, cC1qR (calreticulin) and gC1qR, from human cell lines.
The Department of Medicine, Stony Brook University, Stony Brook, NY, USA.
Berhane
B
Ghebrehiwet
Ellinor I B
EI
Peerschke
D019921:Biotinylation; D018929:Cell Culture Techniques; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism; D002853:Chromatography, Liquid / Q000379:methods; D006801:Humans; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D011951:Receptors, Complement / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D020298:U937 Cells
D008562:Membrane Glycoproteins; D011951:Receptors, Complement; C032402:complement 1q receptor