Interaction of antirenalase antibodies with recombinant human renalases 1 and 2 and their C-terminal regions encoded by the alternative exones

The interaction of antirenalase antibodies with full-length recombinant human renalases RNLS1 and RNLS2, as well as fragments of these proteins encoded by alternative exons 9 and 10 and expressed as fusion proteins with dihydrofolate reductase (DHFR) in Escherichia coli cells has been investigated....

Full description

Saved in:
Bibliographic Details
Published in:Biomeditsinskaia khimiia Vol. 71; no. 4; p. 283
Main Authors: Fedchenko, V I, Kaloshin, A A, Kaloshina, S A, Buneeva, O A, Kopylov, A T, Medvedev, A E
Format: Journal Article
Language:English
Published: Russia (Federation) 01.09.2025
Subjects:
Antibodies, Monoclonal - chemistry
Antibodies, Monoclonal - immunology
Escherichia coli - genetics
Exons
Humans
Monoamine Oxidase
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - immunology
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - immunology
Tetrahydrofolate Dehydrogenase - chemistry
Tetrahydrofolate Dehydrogenase - genetics
Tetrahydrofolate Dehydrogenase - immunology
fusion proteins DHFR-RNLS-9ex and DHFR-RNLS-10ex
C-terminal regions encoded by alternative exons
human renalase-2 (RNLS2)
polyclonal and monoclonal antirenalase antibodies
human renalase-1 (RNLS1)
ISSN:2310-6972
Online Access:Get more information
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The interaction of antirenalase antibodies with full-length recombinant human renalases RNLS1 and RNLS2, as well as fragments of these proteins encoded by alternative exons 9 and 10 and expressed as fusion proteins with dihydrofolate reductase (DHFR) in Escherichia coli cells has been investigated. In this study we used custom made polyclonal antibodies to the full-length recombinant RNLS1 (amino acid residues (aa) 1-342), created at our request, as well as commercially available monoclonal antibodies to the renalase fragment (aa - 18-342), specific for the RNLS1 isoform and its C-terminal sequence encoded by exon 9. According to Western blot analysis, the antibodies interacted not only with recombinant RNLS1 and RNLS2 preparations, but also with fusion proteins containing C-terminal sequences specific for these isoforms (DHFR-RNLS-9ex and DHFR-RNLS-10ex). The results obtained indicate that the studied antibodies, in addition to their direct targets, also "recognized" other protein constructs of RNLS1 and RNLS2, which were absent in the immunogen preparations used for antibody generation.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:2310-6972
DOI:10.18097/PBMCR1608