Purification of C1q receptors and functional analysis Journal Article


Authors: Ghebrehiwet, B.; Peerschke, E. I. B.
Article Title: Purification of C1q receptors and functional analysis
Abstract: 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. © 2014 Springer Science+Business Media, New York.
Keywords: unclassified drug; protein function; protein analysis; cell growth; protein purification; cell membrane; high performance liquid chromatography; biotinylation; cell surface; calreticulin; human; priority journal; article; complement component c1q; c1q receptor; collagen c1q receptor; globular c1q receptor; complement component c1q receptor; fast protein liquid chromatography
Journal Title: Methods in Molecular Biology
Volume: 1100
ISSN: 1064-3745
Publisher: Humana Press Inc  
Date Published: 2014-01-01
Start Page: 319
End Page: 327
Language: English
DOI: 10.1007/978-1-62703-724-2_26
PROVIDER: scopus
PUBMED: 24218271
DOI/URL:
Notes: Chapter 26 in "The Complement System: Methods and Protocols" (ISBN: 978-1-62703-723-5) -- Export Date: 3 August 2015 -- Source: Scopus
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