The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
Rat Ephx1 encodes microsomal epoxide hydrolase 1 (EPHX1/mEH), a membrane-anchored α/β-hydrolase-fold enzyme best known for catalyzing the hydrolysis of epoxides to the corresponding vicinal diols. This reaction is central to xenobiotic detoxification (and in some cases bioactivation) because many epoxides are reactive intermediates generated by cytochrome P450s. EPHX1 is primarily localized to the endoplasmic reticulum (microsomes) with a single N-terminal membrane anchor, and it is also reported at the hepatocyte sinusoidal/plasma membrane. Catalysis proceeds by a two-step covalent mechanism requiring a conserved catalytic triad Asp226–Glu404–His431, with Tyr residues contributing to epoxide activation/positioning. Recent research (2023) has produced high-sensitivity nanobody-based ELISAs for mEH with pg/mL detection and explicit testing against rat mEH for cross-reactivity, enabling translational quantification and biomarker-oriented studies.
The target Ephx1 (rat) is the gene encoding microsomal epoxide hydrolase (mEH; EPHX1; EC 3.3.2.9), a membrane-associated member of the mammalian epoxide hydrolase family. It must be distinguished from EPHX2, the soluble epoxide hydrolase (sEH), which is cytosolic/peroxisomal and has a different physiological emphasis in lipid-epoxide signaling. Authoritative reviews explicitly separate EPHX1 (microsomal) from EPHX2 (soluble) and describe EPHX1 as the earlier-characterized membrane-anchored detoxification enzyme. (https://doi.org/10.3390/ijms22010013; published Dec 2020) (gautheron2020themultifacetedrole pages 1-2)
EPHX1 is consistently described as an α/β-hydrolase-fold enzyme with a short N-terminal transmembrane signal/anchor that retains the protein in microsomal membranes, matching the UniProt-provided domain/family expectations (AB_hydrolase_fold; epoxide hydrolase-like). (https://doi.org/10.1007/s00204-009-0416-0; published Apr 2009) (decker2009mammalianepoxidehydrolases pages 5-7)
Epoxide hydrolases catalyze addition of water to epoxides to form 1,2-diols (often called dihydrodiols for aromatic systems). For EPHX1, this is the defining biochemical activity and explains its role in xenobiotic metabolism because many drugs and pollutants are oxidized to epoxides by CYP enzymes. (https://doi.org/10.1016/j.gene.2015.07.071; published Oct 2015) (vaclavikova2015microsomalepoxidehydrolase pages 3-4)
Mammalian EPHX1/mEH uses a classic two-step α/β-hydrolase mechanism: (i) a nucleophilic attack opens the epoxide to form an enzyme–substrate ester intermediate, then (ii) water activated by a charge-relay system hydrolyzes the ester, releasing the diol. (https://doi.org/10.3390/ijms22010013; published Dec 2020) (gautheron2020themultifacetedrole pages 2-4)
Site-directed mutagenesis work summarized in authoritative reviews identifies the catalytic triad as Asp226, Glu404, and His431. Two Tyr residues (Tyr299 and Tyr374) hydrogen-bond to the epoxide oxygen to help position/activate substrate for catalysis. (https://doi.org/10.1007/s00204-009-0416-0; published Apr 2009) (decker2009mammalianepoxidehydrolases pages 5-7)
A later review reiterates a closely aligned residue set and explicitly describes Asp226 as the nucleophile, His431–Glu404 as a charge-relay system, and Tyr374 as contributing to substrate activation. (https://doi.org/10.1016/j.gene.2015.07.071; published Oct 2015) (vaclavikova2015microsomalepoxidehydrolase pages 3-4)
EPHX1/mEH is primarily an ER/microsomal enzyme, with a single N-terminal membrane anchor (~20 aa) and the catalytic C-terminal domain facing the cytosol. (https://doi.org/10.1007/s00204-009-0416-0; published Apr 2009) (decker2009mammalianepoxidehydrolases pages 5-7)
EPHX1 has also been detected at the hepatocyte sinusoidal/plasma membrane, where it has been linked to sodium-dependent bile acid transport phenomena in hepatocytes (reported in reviews as an additional function/association beyond epoxide hydrolysis). (https://doi.org/10.1016/j.gene.2015.07.071; published Oct 2015) (vaclavikova2015microsomalepoxidehydrolase pages 3-4)
Reviews list a broad range of xenobiotic epoxides as EPHX1 substrates, including epoxides derived from styrene, ethylene, cis-stilbene, and various aromatic/industrial chemicals. (https://doi.org/10.1016/j.gene.2015.07.071; published Oct 2015) (vaclavikova2015microsomalepoxidehydrolase pages 3-4)
EPHX1 is also implicated in metabolism of epoxide intermediates from major toxicants and carcinogens, including aflatoxin B1-8,9-epoxide and polycyclic aromatic hydrocarbon (PAH) epoxides (e.g., benzo[a]pyrene epoxides), with the critical caveat that EPHX1 can contribute to either detoxification or bioactivation depending on the substrate and downstream pathways. (https://doi.org/10.1007/s00204-009-0416-0; published Apr 2009) (decker2009mammalianepoxidehydrolases pages 5-7)
Although historically viewed as a xenobiotic-detoxification enzyme, EPHX1 is also reported to act on endogenous epoxides, including:
A notable non-canonical activity discussed in reviews is metabolism of the endocannabinoid 2-arachidonoylglycerol (2-AG) to arachidonic acid + glycerol, expanding EPHX1’s potential relevance to lipid mediator networks. (https://doi.org/10.1016/j.gene.2015.07.071; published Oct 2015) (vaclavikova2015microsomalepoxidehydrolase pages 3-4)
EPHX1’s ER localization places it in proximity to CYP epoxygenases, enabling coupled generation and hydrolysis of epoxides in microsomal membranes. Reviews emphasize that EPHX1 and EPHX2 can have overlapping substrate selectivity, particularly for lipid epoxides, but EPHX1 remains especially associated with xenobiotic epoxide turnover. (https://doi.org/10.3390/ijms22010013; published Dec 2020) (gautheron2020themultifacetedrole pages 10-12)
A key rat-specific finding repeatedly cited in reviews is that EPHX1 protein levels in cultured primary rat hepatocytes are positively regulated by insulin and negatively regulated by glucagon. (https://doi.org/10.3390/ijms22010013; published Dec 2020) (gautheron2020themultifacetedrole pages 2-4)
Reviews cite older primary studies documenting transcriptional regulation/induction of rat liver microsomal epoxide hydrolase by xenobiotics such as phenobarbital and chemical exposures, indicating EPHX1 is part of inducible hepatic biotransformation programs. (https://doi.org/10.1016/j.gene.2015.07.071; published Oct 2015) (vaclavikova2015microsomalepoxidehydrolase pages 11-12)
Across mammals, EPHX1 is described as widely expressed, with particularly high expression in liver and additional expression in other organs (e.g., lung, kidney, intestine, brain). However, within the retrieved full-text evidence here, rat-specific quantitative tissue distribution values (e.g., absolute protein levels across rat organs) were not available; therefore, tissue distribution is reported at a general mammalian level with rat-specific regulation emphasized where explicitly supported. (https://doi.org/10.1007/s00204-009-0416-0; published Apr 2009) (decker2009mammalianepoxidehydrolases pages 5-7)
A major 2023 methodological advance is development of nanobody-based sandwich ELISAs for human mEH/EPHX1, designed to enable sensitive and standardized protein quantification in tissues and potentially plasma. The strongest amplified format (SA-PolyHRP) achieved a reported limit of detection (LOD) of 0.012 ng/mL and sensitivity of 3.130 OD·mL/ng, representing ~22-fold lower LOD and ~28-fold higher sensitivity relative to the conventional format. (https://doi.org/10.3390/ijms241914698; published Sep 2023) (he2023thegenerationof pages 4-5)
The same study reports minimal cross-reactivity to related epoxide hydrolases and includes explicit cross-reactivity testing against rat mEH, reporting 0.11% cross-reactivity (with <0.01% for human sEH/EH-3/EH-4). (https://doi.org/10.3390/ijms241914698; published Sep 2023) (he2023thegenerationof pages 4-5)
The ELISA measurements in tissues were reported to correlate strongly with activity assays (R² > 0.95). (https://doi.org/10.3390/ijms241914698; published Sep 2023) (he2023thegenerationof pages 1-2)
Visual evidence (tables/figures) supporting these 2023 assay metrics and cross-reactivity is available from the paper’s Table 1 (cross-reactivity) and an inset table in Figure 2 (LOD/sensitivity), plus a schematic assay overview. (he2023thegenerationof media 7adc8f19, he2023thegenerationof media 41860dae, he2023thegenerationof media da255d4a)
Within the retrieved 2024 literature set in this run, most newly retrieved review activity focused on EPHX2/sEH rather than EPHX1. In parallel, reviews continued to note that a complete 3D structure for human EPHX1 was not yet available (limiting structure-guided advances for EPHX1 relative to some other family members). (https://doi.org/10.3390/ijms22010013; published Dec 2020) (gautheron2020themultifacetedrole pages 1-2)
In drug metabolism and toxicology practice, microsomal epoxide hydrolase activity is a key component of microsomal clearance and bioactivation/detoxification for compounds that form epoxide intermediates. Reviews emphasize EPHX1’s centrality to detoxifying CYP-generated epoxides from drugs, pollutants, and toxins, while also highlighting cases where EPHX1 contributes to formation of reactive or carcinogenic products (substrate-dependent bioactivation). (https://doi.org/10.3390/ijms22010013; published Dec 2020) (gautheron2020themultifacetedrole pages 1-2)
mEH has been discussed as a candidate biomarker/antigen in certain diseases, motivating the 2023 development of sensitive nanobody ELISAs. The authors argue these reagents could enable standardized quantification and potentially a bedside assay, though this remains translational/developmental. (https://doi.org/10.3390/ijms241914698; published Sep 2023) (he2023thegenerationof pages 1-2)
Across authoritative reviews, a consistent expert view is that EPHX1’s “primary job” is epoxide-to-diol conversion at microsomal membranes, positioning it as a frontline defense against reactive epoxide intermediates in the ER. At the same time, the field recognizes an expanding set of endogenous substrates (epoxy-fatty acids, epoxysteroids; and evidence for 2-AG hydrolysis), suggesting EPHX1 contributes to lipid mediator homeostasis alongside EPHX2, but typically with different subcellular context and (often) lower catalytic prominence for classic EET turnover compared with sEH. (gautheron2020themultifacetedrole pages 2-4, gautheron2020themultifacetedrole pages 10-12)
From He et al. 2023 (Int. J. Mol. Sci.; Sep 2023; https://doi.org/10.3390/ijms241914698):
These metrics are supported by extracted table/figure images from the publication. (he2023thegenerationof media 7adc8f19, he2023thegenerationof media 41860dae, he2023thegenerationof media da255d4a)
In the retrieved evidence for this run, rat-specific kinetic constants (kcat, KM) for defined EPHX1 substrates and quantitative organ-by-organ expression (e.g., pmol/mg microsomal protein in specific rat tissues) were not present in the available excerpts. Consequently, the report emphasizes: (i) residue-level catalytic mechanism (strongly supported), (ii) substrate examples (strongly supported), and (iii) a recent quantitative assay platform (strongly supported). (vaclavikova2015microsomalepoxidehydrolase pages 3-4, decker2009mammalianepoxidehydrolases pages 5-7, he2023thegenerationof pages 1-2, he2023thegenerationof pages 4-5)
| Category | Summary |
|---|---|
| identity | Rat Ephx1 (UniProt P07687) corresponds to microsomal epoxide hydrolase 1 (EPHX1/mEH; EC 3.3.2.9), a membrane-anchored α/β-hydrolase-fold enzyme distinct from EPHX2/sEH, which is the soluble epoxide hydrolase. Conserved mammalian descriptions match the UniProt family/domain assignment and explicitly distinguish EPHX1 as the microsomal isoform. (gautheron2020themultifacetedrole pages 2-4, vaclavikova2015microsomalepoxidehydrolase pages 3-4, decker2009mammalianepoxidehydrolases pages 5-7) |
| reaction | The primary reaction is hydrolysis of epoxides to vicinal diols/dihydrodiols. In current understanding, EPHX1 acts mainly in detoxification of reactive xenobiotic epoxides but also contributes to metabolism of selected endogenous lipid and steroid epoxides. (gautheron2020themultifacetedrole pages 2-4, vaclavikova2015microsomalepoxidehydrolase pages 3-4, gautheron2020themultifacetedrole pages 1-2) |
| mechanism/residues | Catalysis proceeds through a two-step mechanism: nucleophilic attack on the epoxide to form a covalent ester intermediate, followed by hydrolysis by activated water. Key conserved residues are Asp226, Glu404, His431 (catalytic triad) with Tyr299 and Tyr374 helping orient/activate the epoxide oxygen. (vaclavikova2015microsomalepoxidehydrolase pages 3-4, decker2009mammalianepoxidehydrolases pages 5-7) |
| localization/topology | EPHX1 is primarily a microsomal/endoplasmic reticulum protein with a short N-terminal transmembrane anchor and a catalytic domain exposed on the cytosolic face. It has also been detected at the hepatocyte sinusoidal/plasma membrane, consistent with reported bile-acid transport-associated functions. (gautheron2020themultifacetedrole pages 2-4, vaclavikova2015microsomalepoxidehydrolase pages 3-4, decker2009mammalianepoxidehydrolases pages 5-7, morisseau2013roleofepoxide pages 2-3) |
| xenobiotic substrates/examples | Reported xenobiotic substrates include styrene oxide, cis-stilbene oxide, cyclohexene oxide, indene 1,2-oxide, ethylene oxide, anticonvulsant-derived epoxides, and epoxides from polycyclic aromatic hydrocarbons and aflatoxin B1. Depending on substrate context, EPHX1 can contribute to detoxification or to bioactivation pathways that generate carcinogenic metabolites. (gautheron2020themultifacetedrole pages 2-4, vaclavikova2015microsomalepoxidehydrolase pages 3-4, decker2009mammalianepoxidehydrolases pages 5-7, gautheron2020themultifacetedrole pages 4-6, gautheron2020themultifacetedrole pages 13-15) |
| endogenous substrates/examples | Endogenous substrates/processes include epoxy-fatty acids such as EETs and EpOMEs (to DHETs and DiHOMEs), epoxysteroids such as androstene oxide/estroxide, and a reported non-canonical hydrolytic activity toward 2-arachidonoylglycerol (2-AG) yielding arachidonic acid + glycerol. Reviews note overlap with EPHX2 for some lipid epoxides, but EPHX1 is especially linked to xenobiotic metabolism. (gautheron2020themultifacetedrole pages 2-4, vaclavikova2015microsomalepoxidehydrolase pages 3-4, gautheron2020themultifacetedrole pages 4-6, gautheron2020themultifacetedrole pages 13-15, gautheron2020themultifacetedrole pages 10-12, morisseau2013roleofepoxide pages 2-3) |
| regulation/expression in rat | Rat-specific evidence shows insulin positively and glucagon negatively regulate EPHX1 in primary cultured rat hepatocytes. Additional rat hepatic studies cited in reviews report xenobiotic/transcriptional induction of mEH in liver, supporting a regulated role in hepatic biotransformation. (gautheron2020themultifacetedrole pages 2-4, gautheron2020themultifacetedrole pages 12-13, vaclavikova2015microsomalepoxidehydrolase pages 1-3, vaclavikova2015microsomalepoxidehydrolase pages 3-4, gautheron2020themultifacetedrole pages 13-15, vaclavikova2015microsomalepoxidehydrolase pages 11-12) |
| recent 2023-2024 developments/applications | A notable recent development is a 2023 nanobody-based ELISA for human mEH/EPHX1, relevant to translational biomarker work and potentially adaptable for comparative mammalian studies. The assay supports applications in tissue quantification, disease biomarker research, and standardized detection of mEH, while cross-reactivity testing included rat mEH. (he2023thegenerationof pages 1-2, he2023thegenerationof pages 4-5, he2023thegenerationof pages 10-11, he2023thegenerationof pages 5-7) |
| quantitative data | In the 2023 ELISA study, the best amplified format achieved LOD 0.012 ng/mL and sensitivity 3.130 OD·mL/ng, with about 22-fold lower LOD and ~28-fold higher sensitivity than the conventional format; correlation with enzyme activity in tissues was R² > 0.95. Reported cross-reactivity was 0.11% for rat mEH, 0.02% for denatured mEH, and <0.01% for human sEH/EH-3/EH-4; spike recoveries were approximately 73–126% in plasma and extended to roughly 72–141% in tissue matrices depending on format/dilution. (he2023thegenerationof pages 1-2, he2023thegenerationof pages 4-5, he2023thegenerationof pages 10-11, he2023thegenerationof pages 5-7, he2023thegenerationof media 7adc8f19, he2023thegenerationof media 41860dae, he2023thegenerationof media da255d4a) |
Table: This table summarizes the core functional annotation of rat Ephx1/EPHX1 (microsomal epoxide hydrolase), including identity, reaction chemistry, localization, substrates, rat-specific regulation, and recent assay developments. It is useful as a compact evidence-backed overview for gene/protein annotation and literature synthesis.
References
(gautheron2020themultifacetedrole pages 1-2): Jérémie Gautheron and Isabelle Jéru. The multifaceted role of epoxide hydrolases in human health and disease. International Journal of Molecular Sciences, 22:13, Dec 2020. URL: https://doi.org/10.3390/ijms22010013, doi:10.3390/ijms22010013. This article has 122 citations.
(decker2009mammalianepoxidehydrolases pages 5-7): Martina Decker, Michael Arand, and Annette Cronin. Mammalian epoxide hydrolases in xenobiotic metabolism and signalling. Archives of Toxicology, 83:297-318, Apr 2009. URL: https://doi.org/10.1007/s00204-009-0416-0, doi:10.1007/s00204-009-0416-0. This article has 274 citations and is from a highest quality peer-reviewed journal.
(vaclavikova2015microsomalepoxidehydrolase pages 3-4): Radka Václavíková, David J. Hughes, and Pavel Souček. Microsomal epoxide hydrolase 1 (ephx1): gene, structure, function, and role in human disease. Gene, 571 1:1-8, Oct 2015. URL: https://doi.org/10.1016/j.gene.2015.07.071, doi:10.1016/j.gene.2015.07.071. This article has 127 citations and is from a peer-reviewed journal.
(gautheron2020themultifacetedrole pages 2-4): Jérémie Gautheron and Isabelle Jéru. The multifaceted role of epoxide hydrolases in human health and disease. International Journal of Molecular Sciences, 22:13, Dec 2020. URL: https://doi.org/10.3390/ijms22010013, doi:10.3390/ijms22010013. This article has 122 citations.
(gautheron2020themultifacetedrole pages 10-12): Jérémie Gautheron and Isabelle Jéru. The multifaceted role of epoxide hydrolases in human health and disease. International Journal of Molecular Sciences, 22:13, Dec 2020. URL: https://doi.org/10.3390/ijms22010013, doi:10.3390/ijms22010013. This article has 122 citations.
(vaclavikova2015microsomalepoxidehydrolase pages 11-12): Radka Václavíková, David J. Hughes, and Pavel Souček. Microsomal epoxide hydrolase 1 (ephx1): gene, structure, function, and role in human disease. Gene, 571 1:1-8, Oct 2015. URL: https://doi.org/10.1016/j.gene.2015.07.071, doi:10.1016/j.gene.2015.07.071. This article has 127 citations and is from a peer-reviewed journal.
(he2023thegenerationof pages 4-5): Qiyi He, Mark R. McCoy, Meng Qi, Christophe Morisseau, Huiyi Yang, Chengpeng Xu, Rachel Shey, Michael C. Goodman, Suqing Zhao, and Bruce D. Hammock. The generation of a nanobody-based elisa for human microsomal epoxide hydrolase. International Journal of Molecular Sciences, 24:14698, Sep 2023. URL: https://doi.org/10.3390/ijms241914698, doi:10.3390/ijms241914698. This article has 5 citations.
(he2023thegenerationof pages 1-2): Qiyi He, Mark R. McCoy, Meng Qi, Christophe Morisseau, Huiyi Yang, Chengpeng Xu, Rachel Shey, Michael C. Goodman, Suqing Zhao, and Bruce D. Hammock. The generation of a nanobody-based elisa for human microsomal epoxide hydrolase. International Journal of Molecular Sciences, 24:14698, Sep 2023. URL: https://doi.org/10.3390/ijms241914698, doi:10.3390/ijms241914698. This article has 5 citations.
(he2023thegenerationof media 7adc8f19): Qiyi He, Mark R. McCoy, Meng Qi, Christophe Morisseau, Huiyi Yang, Chengpeng Xu, Rachel Shey, Michael C. Goodman, Suqing Zhao, and Bruce D. Hammock. The generation of a nanobody-based elisa for human microsomal epoxide hydrolase. International Journal of Molecular Sciences, 24:14698, Sep 2023. URL: https://doi.org/10.3390/ijms241914698, doi:10.3390/ijms241914698. This article has 5 citations.
(he2023thegenerationof media 41860dae): Qiyi He, Mark R. McCoy, Meng Qi, Christophe Morisseau, Huiyi Yang, Chengpeng Xu, Rachel Shey, Michael C. Goodman, Suqing Zhao, and Bruce D. Hammock. The generation of a nanobody-based elisa for human microsomal epoxide hydrolase. International Journal of Molecular Sciences, 24:14698, Sep 2023. URL: https://doi.org/10.3390/ijms241914698, doi:10.3390/ijms241914698. This article has 5 citations.
(he2023thegenerationof media da255d4a): Qiyi He, Mark R. McCoy, Meng Qi, Christophe Morisseau, Huiyi Yang, Chengpeng Xu, Rachel Shey, Michael C. Goodman, Suqing Zhao, and Bruce D. Hammock. The generation of a nanobody-based elisa for human microsomal epoxide hydrolase. International Journal of Molecular Sciences, 24:14698, Sep 2023. URL: https://doi.org/10.3390/ijms241914698, doi:10.3390/ijms241914698. This article has 5 citations.
(morisseau2013roleofepoxide pages 2-3): Christophe Morisseau. Role of epoxide hydrolases in lipid metabolism. Biochimie, 95 1:91-5, Jan 2013. URL: https://doi.org/10.1016/j.biochi.2012.06.011, doi:10.1016/j.biochi.2012.06.011. This article has 114 citations and is from a peer-reviewed journal.
(gautheron2020themultifacetedrole pages 4-6): Jérémie Gautheron and Isabelle Jéru. The multifaceted role of epoxide hydrolases in human health and disease. International Journal of Molecular Sciences, 22:13, Dec 2020. URL: https://doi.org/10.3390/ijms22010013, doi:10.3390/ijms22010013. This article has 122 citations.
(gautheron2020themultifacetedrole pages 13-15): Jérémie Gautheron and Isabelle Jéru. The multifaceted role of epoxide hydrolases in human health and disease. International Journal of Molecular Sciences, 22:13, Dec 2020. URL: https://doi.org/10.3390/ijms22010013, doi:10.3390/ijms22010013. This article has 122 citations.
(gautheron2020themultifacetedrole pages 12-13): Jérémie Gautheron and Isabelle Jéru. The multifaceted role of epoxide hydrolases in human health and disease. International Journal of Molecular Sciences, 22:13, Dec 2020. URL: https://doi.org/10.3390/ijms22010013, doi:10.3390/ijms22010013. This article has 122 citations.
(vaclavikova2015microsomalepoxidehydrolase pages 1-3): Radka Václavíková, David J. Hughes, and Pavel Souček. Microsomal epoxide hydrolase 1 (ephx1): gene, structure, function, and role in human disease. Gene, 571 1:1-8, Oct 2015. URL: https://doi.org/10.1016/j.gene.2015.07.071, doi:10.1016/j.gene.2015.07.071. This article has 127 citations and is from a peer-reviewed journal.
(he2023thegenerationof pages 10-11): Qiyi He, Mark R. McCoy, Meng Qi, Christophe Morisseau, Huiyi Yang, Chengpeng Xu, Rachel Shey, Michael C. Goodman, Suqing Zhao, and Bruce D. Hammock. The generation of a nanobody-based elisa for human microsomal epoxide hydrolase. International Journal of Molecular Sciences, 24:14698, Sep 2023. URL: https://doi.org/10.3390/ijms241914698, doi:10.3390/ijms241914698. This article has 5 citations.
(he2023thegenerationof pages 5-7): Qiyi He, Mark R. McCoy, Meng Qi, Christophe Morisseau, Huiyi Yang, Chengpeng Xu, Rachel Shey, Michael C. Goodman, Suqing Zhao, and Bruce D. Hammock. The generation of a nanobody-based elisa for human microsomal epoxide hydrolase. International Journal of Molecular Sciences, 24:14698, Sep 2023. URL: https://doi.org/10.3390/ijms241914698, doi:10.3390/ijms241914698. This article has 5 citations.