Human CYP26A1 ELISA Kit (V2LY-0626-LY4473)

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Tested Data
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Basic Information

Sensitivity
0.0049 ng/mL
Detection Range
0.01-2 ng/mL
Sample Type
Serum, Plasma, cell culture supernates
Specificity
Human
Assay Type
Sandwich
Reactivity
Human
Assay Time
1.5 h
Molecule Mass
56.2 kDa
Components
  • Pre-coated ELISA Plate: 12 wells * 8 detachable strips
  • Standard solution: 0.5ml x1
  • Standard diluent: 3ml x1
  • Streptavidin-HRP: 6ml x1
  • Stop solution: 6ml x1
  • Substrate solution A: 6ml x1
  • Substrate solution B: 6ml x1
  • Wash buffer concentrate (25x): 20ml x1
  • Biotinylated antibody: 1ml x1

Formulations & Storage [For reference only, actual COA shall prevail!]

Storage
Store at 2-8°C
More Infomation

Target

Full Name
Cytochrome P450 Family 26 Subfamily A Member 1
Function
A cytochrome P450 monooxygenase involved in the metabolism of all-trans retinoic acid (atRA), a signaling molecule that binds to retinoic acid receptors and regulates gene transcription. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes the hydroxylation of carbon hydrogen bonds of atRA primarily at C-4 and C-18. Has no activity toward 9-cis and 13-cis retinoic acid stereoisomers (PubMed:22020119, PubMed:9228017, PubMed:9716180).

May play a role in the oxidative metabolism of xenobiotics such as tazarotenic acid (PubMed:26937021).
Biological Process
Kidney development Source: Ensembl
Negative regulation of retinoic acid receptor signaling pathway Source: BHF-UCL
Response to retinoic acid Source: Ensembl
Response to vitamin A Source: Ensembl
Retinoic acid catabolic process Source: BHF-UCL
Retinoic acid metabolic process Source: UniProtKB
Sterol metabolic process Source: GO_Central
Vitamin metabolic process Source: Reactome
Xenobiotic metabolic process Source: UniProtKB
Cellular Location
Endoplasmic reticulum membrane; Microsome membrane

Horiguchi, K., Fujiwara, K., Tsukada, T., Nakakura, T., Yoshida, S., Hasegawa, R., & Takigami, S. (2022). The multiciliated cells in Rathke’s cleft express CYP26A1 and respond to retinoic acid in the pituitary. Cell and Tissue Research, 1-12.

Chen, P. H., Chung, C. M., Wang, Y. Y., Huang, H. W., Huang, B., Lee, K. W., ... & Chan, L. P. (2020). CYP26A1 is a novel biomarker for betel quid-related oral and pharyngeal cancers. Diagnostics, 10(11), 982.

Sharma, S., Liu, J., Zhang, X., Sharma, S. S., Sorensen, E. J., & Bureik, M. (2020). New luciferin-based probe substrates for human CYP26A1. Biochemistry and biophysics reports, 24, 100861.

Snyder, J. M., Zhong, G., Hogarth, C., Huang, W., Topping, T., LaFrance, J., ... & Isoherranen, N. (2020). Knockout of Cyp26a1 and Cyp26b1 during postnatal life causes reduced lifespan, dermatitis, splenomegaly, and systemic inflammation in mice. The FASEB Journal, 34(12), 15788-15804.

Guo, P., Ji, Z., Jiang, H., Huang, X., Wang, C., & Pan, B. (2020). Identification of a novel CYP26A1 mutation in a Chinese family with congenital microtia. International Journal of Pediatric Otorhinolaryngology, 139, 110488.

Zhong, G., Hogarth, C., Snyder, J. M., Palau, L., Topping, T., Huang, W., ... & Isoherranen, N. (2019). The retinoic acid hydroxylase Cyp26a1 has minor effects on postnatal vitamin A homeostasis, but is required for exogenous atRA clearance. Journal of Biological Chemistry, 294(29), 11166-11179.

Zolfaghari, R., Mattie, F. J., Wei, C. H., Chisholm, D. R., Whiting, A., & Ross, A. C. (2019). CYP26A1 gene promoter is a useful tool for reporting RAR-mediated retinoid activity. Analytical biochemistry, 577, 98-109.

Jin, L., Chang, C., Pawlik, K. M., Datta, A., Johnson, L. M., Vu, T., ... & Datta, P. K. (2018). Serine threonine kinase receptor-associated protein deficiency impairs mouse embryonic stem cells lineage commitment through CYP26A1-mediated retinoic acid homeostasis. Stem Cells, 36(9), 1368-1379.

Stevison, F., Hogarth, C., Tripathy, S., Kent, T., & Isoherranen, N. (2017). Inhibition of the all-trans retinoic acid (atRA) hydroxylases CYP26A1 and CYP26B1 results in dynamic, tissue-specific changes in endogenous atRA signaling. Drug Metabolism and Disposition, 45(7), 846-854.

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

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