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Mouse Anti-CYP27A1 Recombinant Antibody (CBYY-C2394) (V2LY-0125-LY940)


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Published Data
V2LY-0125-LY940-1
Mouse Anti-CYP27A1 Recombinant Antibody (CBYY-C2394) (V2LY-0125-LY940) in WB
Representative blots of proteins involved in cholesterol and fatty acids metabolism in the liver of rats fed standard chow (CTRL), high-fat (HFA), high-cholesterol (HCh) and high-fatþhighcholesterol (HFAþHCh) diet for 6 weeks. ...View More
Serviddio, G., Bellanti, F., Villani, R., Tamborra, R., Zerbinati, C., Blonda, M., ... & Iuliano, L. (2016). Effects of dietary fatty acids and cholesterol excess on liver injury: A lipidomic approach. Redox Biology, 9, 296-305. Distributed under Open Access license CC BY 4.0, without modification.

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBYY-C2394
Antibody Isotype
IgG1, κ
Application
WB, IP, IF, ELISA

Basic Information

Immunogen
Amino acids 335-451 mapping within an internal region of human CYP27A1.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal Antibody
Application Notes
ApplicationNote
WB1:100-1:1,000
IP1-2 μg per 100-500 μg of total protein (1 mL of cell lysate)
IF(ICC)1:50-1:500
ELISA1:100-1:1,000

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

Format
Liquid
Buffer
Gelatin & PBS
Preservative
Sodium Azide
Concentration
0.2 mg/mL
Purity
>95% as determined by analysis by SDS-PAGE
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Cytochrome P450 Family 27 Subfamily A Member 1
Entrez Gene ID
1593
UniProt ID
Q02318
Function
Cytochrome P450 monooxygenase that catalyzes regio- and stereospecific hydroxylation of cholesterol and its derivatives. Hydroxylates (with R stereochemistry) the terminal methyl group of cholesterol side-chain in a three step reaction to yield at first a C26 alcohol, then a C26 aldehyde and finally a C26 acid (PubMed:9660774, PubMed:12077124, PubMed:21411718, PubMed:28190002).

Regulates cholesterol homeostasis by catalyzing the conversion of excess cholesterol to bile acids via both the 'neutral' (classic) and the 'acid' (alternative) pathways (PubMed:9660774, PubMed:1708392, PubMed:11412116, PubMed:2019602, PubMed:7915755, PubMed:9186905, PubMed:9790667).

May also regulate cholesterol homeostasis via generation of active oxysterols, which act as ligands for NR1H2 and NR1H3 nuclear receptors, modulating the transcription of genes involved in lipid metabolism (PubMed:9660774, PubMed:12077124).

Plays a role in cholestanol metabolism in the cerebellum. Similarly to cholesterol, hydroxylates cholestanol and may facilitate sterol diffusion through the blood-brain barrier to the systemic circulation for further degradation (PubMed:28190002).

Also hydroxylates retinal 7-ketocholesterol, a noxious oxysterol with pro-inflammatory and pro-apoptotic effects, and may play a role in its elimination from the retinal pigment epithelium (PubMed:21411718).

May play a redundant role in vitamin D biosynthesis. Catalyzes 25-hydroxylation of vitamin D3 that is required for its conversion to a functionally active form (PubMed:15465040).
Biological Process
Bile acid biosynthetic process Source: UniProtKB
Calcitriol biosynthetic process from calciol Source: UniProtKB
Cholesterol catabolic process Source: UniProtKB
Cholesterol metabolic process Source: GO_Central
Sterol metabolic process Source: Reactome
Cellular Location
Mitochondrion inner membrane. Post-translationally targeted to mitochondria. All three of the receptor proteins in the TOM complex, TOMM70, TOMM20 and TOMM22 are required for the translocation across the mitochondrial outer membrane. After translocation into the matrix, associates with the inner membrane as a membrane extrinsic protein.
Involvement in disease
Cerebrotendinous xanthomatosis (CTX):
Rare sterol storage disorder characterized clinically by progressive neurologic dysfunction, premature atherosclerosis, and cataracts.
More Infomation

Cho, H., Shen, Q., Zhang, L. H., Okumura, M., Kawakami, A., Ambrose, J., ... & Forrester, W. C. (2021). CYP27A1-dependent anti-melanoma activity of limonoid natural products targets mitochondrial metabolism. Cell chemical biology, 28(10), 1407-1419.

Le Cornet, C., Walter, B., Sookthai, D., Johnson, T. S., Kühn, T., Herpel, E., ... & Fortner, R. T. (2020). Circulating 27-hydroxycholesterol and breast cancer tissue expression of CYP27A1, CYP7B1, LXR-β, and ERβ: results from the EPIC-Heidelberg cohort. Breast Cancer Research, 22(1), 1-10.

Kimbung, S., Inasu, M., Stålhammar, T., Nodin, B., Elebro, K., Tryggvadottir, H., ... & Borgquist, S. (2020). CYP27A1 expression is associated with risk of late lethal estrogen receptor-positive breast cancer in postmenopausal patients. Breast Cancer Research, 22(1), 1-13.

Griffiths, W. J., Crick, P. J., Meljon, A., Theofilopoulos, S., Abdel-Khalik, J., Yutuc, E., ... & Wang, Y. (2019). Additional pathways of sterol metabolism: evidence from analysis of Cyp27a1−/− mouse brain and plasma. Biochimica et Biophysica Acta (BBA)-Molecular and Cell Biology of Lipids, 1864(2), 191-211.

Lee, C. W., Lee, J. J., Lee, Y. F., Wang, P. W., Pan, T. L., Chang, W. N., & Tsai, M. H. (2019). Clinical and molecular genetic features of cerebrotendinous xanthomatosis in Taiwan: Report of a novel CYP27A1 mutation and literature review. Journal of Clinical Lipidology, 13(6), 954-959.

Khan, N. A., Stopsack, K. H., Allott, E. H., Gerke, T., Giovannucci, E. L., Mucci, L. A., & Kantoff, P. W. (2019). Intratumoral sterol-27-hydroxylase (CYP27A1) expression in relation to cholesterol synthesis and vitamin D signaling and its association with lethal prostate cancer. Cancer Epidemiology and Prevention Biomarkers, 28(6), 1052-1058.

Agnello, L., Scazzone, C., Lo Sasso, B., Ragonese, P., Milano, S., Salemi, G., & Ciaccio, M. (2018). CYP27A1, CYP24A1, and RXR-α Polymorphisms, Vitamin D, and multiple sclerosis: a pilot study. Journal of Molecular Neuroscience, 66(1), 77-84.

Mangum, L. C., Hou, X., Borazjani, A., Lee, J. H., Ross, M. K., & Crow, J. A. (2018). Silencing carboxylesterase 1 in human THP-1 macrophages perturbs genes regulated by PPARγ/RXR and RAR/RXR: down-regulation of CYP27A1–LXRα signaling. Biochemical Journal, 475(3), 621-642.

Alfaqih, M. A., Nelson, E. R., Liu, W., Safi, R., Jasper, J. S., Macias, E., ... & Freedland, S. J. (2017). CYP27A1 loss dysregulates cholesterol homeostasis in prostate cancer. Cancer research, 77(7), 1662-1673.

Kimbung, S., Chang, C. Y., Bendahl, P. O., Dubois, L., Thompson, J. W., McDonnell, D. P., & Borgquist, S. (2017). Impact of 27-hydroxylase (CYP27A1) and 27-hydroxycholesterol in breast cancer. Endocrine-related cancer, 24(7), 339-349.

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

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