A new enzyme-linked immunosorbent assay system against the N-terminal propiece of interleukin-1 α.

A new enzyme-linked immunosorbent assay system against the N-terminal propiece of interleukin-1α.
J Oral Sci. 2020 Jun 04;:
Authors: Sata E, Takada L, Kaetsu R, Fukasawa M, Ohtsu M, Motoyoshi M, Asano M
Abstract
Interleukin-1α (IL-1α) is produced inside cells in its precursor form (pIL-1α). Enzymatic cleavage yields mature (mIL-1α) and the propiece of IL-1α (ppIL-1α), which are thought to be localized in the nucleus, because of the presence of nuclear localizing signals. Studies of ppIL-1α function have been hampered by the lack of a ppIL-1α-specific antibody (Ab). In the present study, the authors generated anti-ppIL-1α Ab by using recombinant histidine-tagged ppIL-1α (His-ppIL-1α) as an immunogen. Rabbits were immunized with His-ppIL-1α, and affinity-purified Ab was obtained. Ab reactivity and specificity were examined by Western blotting. The antibody successfully recognized transfectant-derived green fluorescence protein (GFP)-tagged ppIL-1α but not GFP. A sandwich enzyme-linked immunosorbent assay (ELISA) system established by biotinylating the anti-ppIL-1α Ab successfully detected GFP-ppIL-1α. The Ab and ELISA system allows functional analysis of ppIL-1α and improves understanding of ppIL-1α.
PMID: 32493867 [PubMed - as supplied by publisher]

Source: Journal of oral science - June 6, 2020 Category: Dentistry Tags: J Oral Sci Source Type: research