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HADH Matched Antibody Pair (523) (APMAB-523LY)

This antibody pair set can be used for detecting and quantifying protein level of human HADH.
See all HADH antibodies

Specifications

ApplIcation
Sandwich ELISA
Specificity
Human
Capture Antibody
Mouse anti-HADH monoclonal antibody, 100 ug
Detection Antibody
Anti-HADH Rabbit polyclonal antibody, 50 ug
Dilutions
10 ng/ml-100 ng/ml
Format
Liquid
Storage
Aliquot and store at -20°Cor -80°C. Avoid freeze-thaw cycles.
Introduction
This gene is a member of the 3-hydroxyacyl-CoA dehydrogenase gene family. The encoded protein functions in the mitochondrial matrix to catalyze the oxidation of straight-chain 3-hydroxyacyl-CoAs as part of the beta-oxidation pathway. Its enzymatic activity is highest with medium-chain-length fatty acids. Mutations in this gene cause one form of familial hyperinsulinemic hypoglycemia. The human genome contains a related pseudogene of this gene on chromosome 15. [provided by RefSeq, May 2010]
Alternative Names
Hydroxyacyl-CoA Dehydrogenase; Medium And Short-Chain L-3-Hydroxyacyl-Coenzyme A Dehydrogenase; L-3-Hydroxyacyl-Coenzyme A Dehydrogenase, Short Chain; Short-Chain 3-Hydroxyacyl-CoA Dehydrogenase; EC 1.1.1.35; HADHSC; SCHAD; HCDH; HAD;
Entrez Gene ID
3033
UniProt ID
Q16836

Fang, H., Li, H., Zhang, H., Wang, S., Xu, S., Chang, L., ... & Cui, R. (2022). Short-chain L-3-hydroxyacyl-CoA dehydrogenase: A novel vital oncogene or tumor suppressor gene in cancers. Frontiers in Pharmacology, 13, 1019312.

Xia, G., Gao, Y., Wu, C., Pan, H., Hou, J., Su, J., ... & Gao, X. (2022). A novel isoform of hydroxyacyl-CoA dehydrogenase inhibits cell proliferation. Biochemical and Biophysical Research Communications, 606, 75-79.

Karunadasa, A. K. U. I., Toma, C., Senaratne, K. M. P. H., Kumara, K. G. R. A., & Gamage, C. D. (2021). Leptospiral 3-hydroxyacyl-CoA dehydrogenase as an early urinary biomarker of leptospirosis in a Sri Lankan setting–Interim results. Sri Lankan Journal of Infectious Diseases, 11.

Wongkittichote, P., Watson, J. R., Leonard, J. M., Toolan, E. R., Dickson, P. I., & Grange, D. K. (2020). Fatal COVID‐19 infection in a patient with long‐chain 3‐hydroxyacyl‐CoA dehydrogenase deficiency: a case report. JIMD reports, 56(1), 40-45.

Bernardi, C., Tirloni, E., Stella, S., Anastasio, A., Cattaneo, P., & Colombo, F. (2019). ß-hydroxyacyl-CoA-dehydrogenase activity differentiates unfrozen from frozen-thawed Yellowfin tuna (Thunnus albacares). Italian journal of food safety, 8(3).

Fraser, H., Geppert, J., Johnson, R., Johnson, S., Connock, M., Clarke, A., ... & Stinton, C. (2019). Evaluation of earlier versus later dietary management in long-chain 3-hydroxyacyl-CoA dehydrogenase or mitochondrial trifunctional protein deficiency: a systematic review. Orphanet Journal of Rare Diseases, 14(1), 1-18.

Segawa, M., Wen, C., Orita, I., Nakamura, S., & Fukui, T. (2019). Two NADH-dependent (S)-3-hydroxyacyl-CoA dehydrogenases from polyhydroxyalkanoate-producing Ralstonia eutropha. Journal of bioscience and bioengineering, 127(3), 294-300.

Toma, C., Koizumi, N., Kakita, T., Yamaguchi, T., Hermawan, I., Higa, N., & Yamashiro, T. (2018). Leptospiral 3-hydroxyacyl-CoA dehydrogenase as an early urinary biomarker of leptospirosis. Heliyon, 4(4).

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For research use only. Not intended for any clinical use.

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We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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