<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Veuskens BRJ</submitter><funding>Sanquin Research Fund</funding><funding>European Union's Horizon 2020 research and innovation programme</funding><pagination>10669</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11950314</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>15(1)</volume><pubmed_abstract>Factor H-related (FHR) protein 1 and 2 form dimers resulting in FHR-1 and -2 homodimers, and FHR-1/2 heterodimers. Dimerization is hypothesized to further increase their antagonistic function with complement regulator factor H (FH). So far, only FHR-1 homodimers and FHR-1/2 heterodimers could be quantified in a direct way. With the reported genetic associations between CFHR2 and complement-related diseases such as age related macular degeneration and C3-glomerulopathy, direct assessment of FHR-2/2 levels determining the dimer distribution of FHR-1 and -2 is needed to further elucidate their role within complement regulation. Therefore, novel in-house generated FHR-2 antibodies were used to develop a specific ELISA to enable direct quantification of FHR-2 homodimers. Allowing for the first </pubmed_abstract><journal>Scientific reports</journal><pubmed_title>Factor H-related 2 levels dictate FHR dimer composition.</pubmed_title><pmcid>PMC11950314</pmcid><funding_grant_id>899163</funding_grant_id><funding_grant_id>SRF-YIA-23-06</funding_grant_id><pubmed_authors>Brouwer MC</pubmed_authors><pubmed_authors>Keijzer NCH</pubmed_authors><pubmed_authors>van Mierlo G</pubmed_authors><pubmed_authors>Veuskens BRJ</pubmed_authors><pubmed_authors>Hoogenboezem M</pubmed_authors><pubmed_authors>Pouw RB</pubmed_authors><pubmed_authors>Geissler J</pubmed_authors><pubmed_authors>van Leeuwen K</pubmed_authors><pubmed_authors>Derlagen M</pubmed_authors><pubmed_authors>Kuijpers TW</pubmed_authors></additional><is_claimable>false</is_claimable><name>Factor H-related 2 levels dictate FHR dimer composition.</name><description>Factor H-related (FHR) protein 1 and 2 form dimers resulting in FHR-1 and -2 homodimers, and FHR-1/2 heterodimers. Dimerization is hypothesized to further increase their antagonistic function with complement regulator factor H (FH). So far, only FHR-1 homodimers and FHR-1/2 heterodimers could be quantified in a direct way. With the reported genetic associations between CFHR2 and complement-related diseases such as age related macular degeneration and C3-glomerulopathy, direct assessment of FHR-2/2 levels determining the dimer distribution of FHR-1 and -2 is needed to further elucidate their role within complement regulation. Therefore, novel in-house generated FHR-2 antibodies were used to develop a specific ELISA to enable direct quantification of FHR-2 homodimers. Allowing for the first </description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Mar</publication><modification>2026-06-03T02:35:31.689Z</modification><creation>2025-07-09T03:04:32.341Z</creation></dates><accession>S-EPMC11950314</accession><cross_references><pubmed>40148491</pubmed><doi>10.1038/s41598-025-94064-4</doi></cross_references></HashMap>