<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Geno KA</submitter><funding>NIAID NIH HHS</funding><funding>NHLBI NIH HHS</funding><funding>NIH</funding><pagination>106-10</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4560653</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>424</volume><pubmed_abstract>The human opsonin ficolin-2 (L-ficolin) is an innate pattern-recognizing molecule that binds to acetylated moieties. Upon binding, ficolin-2 activates complement through the lectin pathway, opsonizing the target to promote phagocytic clearance. Ficolin-2 has been found to interact with a growing number of pathogenic bacteria, fungi, and viruses. Ficolin-2 also has proposed roles in host homeostasis, including the clearance of apoptotic cells. Consequently, there is an increased interest in studying ficolin-2, and access to purified ficolin-2 is necessary for these studies. Ficolin-2 purified from serum, plasma, or cell culture supernatants has been a useful tool in the characterization of ficolin-2 function; however, available protocols are laborious and inefficient, requiring additional p</pubmed_abstract><journal>Journal of immunological methods</journal><pubmed_title>Rapid and efficient purification of ficolin-2 using a disposable CELLine bioreactor.</pubmed_title><pmcid>PMC4560653</pmcid><funding_grant_id>T32 HL105346</funding_grant_id><funding_grant_id>R56 AI031473</funding_grant_id><pubmed_authors>Geno KA</pubmed_authors><pubmed_authors>Nahm MH</pubmed_authors><pubmed_authors>Spencer BL</pubmed_authors></additional><is_claimable>false</is_claimable><name>Rapid and efficient purification of ficolin-2 using a disposable CELLine bioreactor.</name><description>The human opsonin ficolin-2 (L-ficolin) is an innate pattern-recognizing molecule that binds to acetylated moieties. Upon binding, ficolin-2 activates complement through the lectin pathway, opsonizing the target to promote phagocytic clearance. Ficolin-2 has been found to interact with a growing number of pathogenic bacteria, fungi, and viruses. Ficolin-2 also has proposed roles in host homeostasis, including the clearance of apoptotic cells. Consequently, there is an increased interest in studying ficolin-2, and access to purified ficolin-2 is necessary for these studies. Ficolin-2 purified from serum, plasma, or cell culture supernatants has been a useful tool in the characterization of ficolin-2 function; however, available protocols are laborious and inefficient, requiring additional p</description><dates><release>2015-01-01T00:00:00Z</release><publication>2015 Sep</publication><modification>2025-05-29T20:59:42.09Z</modification><creation>2019-03-27T01:57:53Z</creation></dates><accession>S-EPMC4560653</accession><cross_references><pubmed>26021447</pubmed><doi>10.1016/j.jim.2015.05.008</doi></cross_references></HashMap>