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Heavy chain single-domain antibodies to detect native human soluble epoxide hydrolase.

Authors :
Cui, Yongliang
Cui, Yongliang
Li, Dongyang
Morisseau, Christophe
Dong, Jie-Xian
Yang, Jun
Wan, Debin
Rossotti, Martín A
Gee, Shirley J
González-Sapienza, Gualberto G
Hammock, Bruce D
Cui, Yongliang
Cui, Yongliang
Li, Dongyang
Morisseau, Christophe
Dong, Jie-Xian
Yang, Jun
Wan, Debin
Rossotti, Martín A
Gee, Shirley J
González-Sapienza, Gualberto G
Hammock, Bruce D
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