TY - CHAP
T1 - Purification of C1q receptors and functional analysis
AU - Ghebrehiwet, Berhane
AU - Peerschke, Ellinor I.B.
PY - 2014
Y1 - 2014
N2 - 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.
AB - 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.
KW - C1q receptor
KW - Calreticulin
KW - Collagen C1q receptor
KW - Globular C1q receptor
UR - https://www.scopus.com/pages/publications/84934439168
U2 - 10.1007/978-1-62703-724-2_26
DO - 10.1007/978-1-62703-724-2_26
M3 - Chapter
C2 - 24218271
AN - SCOPUS:84934439168
SN - 9781627037235
T3 - Methods in Molecular Biology
SP - 319
EP - 327
BT - The Complement System
PB - Humana Press Inc.
ER -