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Heavy chain single-domain antibodies to detect native human soluble epoxide hydrolase.
- Source :
- Analytical and bioanalytical chemistry; vol 407, iss 24, 7275-7283; 1618-2642
- Publication Year :
- 2015
-
Abstract
- The soluble epoxide hydrolase (sEH) is a potential pharmacological target for treating hypertension, vascular inflammation, pain, cancer, and other diseases. However, there is not a simple, inexpensive, and reliable method to estimate levels of active sEH in tissues. Toward developing such an assay, a polyclonal variable domain of heavy chain antibody (VHH) sandwich immunoassay was developed. Ten VHHs, which are highly selective for native human sEH, were isolated from a phage-displayed library. The ten VHHs have no significant cross-reactivity with human microsomal epoxide hydrolase, rat and mouse sEH, and denatured human sEH. There is a high correlation between protein levels of the sEH determined by the enzyme-linked immunosorbent assay (ELISA) and the catalytic activity of the enzyme in S9 fractions of human tissues (liver, kidney, and lung). The VHH-based ELISA appears to be a new reliable method for monitoring the sEH and may be useful as a diagnostic tool for diseases influenced by sEH. This study also demonstrates the broad utility of VHH in biochemical and pharmacological research.
Details
- Database :
- OAIster
- Journal :
- Analytical and bioanalytical chemistry; vol 407, iss 24, 7275-7283; 1618-2642
- Notes :
- application/pdf, Analytical and bioanalytical chemistry vol 407, iss 24, 7275-7283 1618-2642
- Publication Type :
- Electronic Resource
- Accession number :
- edsoai.on1377973436
- Document Type :
- Electronic Resource