Cyp1a1 Antibodies

Structure of Cyp1a1

Cyp1a1 is a membrane-bound protein with a molecular weight of approximately 58-60 kDa. Its precise molecular weight varies slightly due to differences in amino acid sequences among species.

This protein is composed of 503 amino acids, and its three-dimensional structure presents a typical P450 folding pattern. The active center of Cyp1a1 contains a heme cofactor, and this iron porphyrin structure is at the core of its catalytic function. The secondary structure of the protein alternates between α -helices and β -folds, forming hydrophobic channels to facilitate substrate binding. Conserved cysteine residues coordinate with heme iron, while adjacent threonine and glutamic acid residues jointly participate in electron transfer and REDOX reaction mechanisms.

Fig. 1 Structural model of the proximal surface of human CYP1A1.¹

Key structural properties of Cyp1a1:

• Typical P450 folding conformation form hydrophobic pocket
• Conservative heme in combination with field is located in the core protein
• Iron porphyrin cogroups are responsible for catalyzing oxidation reactions

Functions of Cyp1a1

The main function of Cyp1a1 is to metabolize exogenous compounds and play a core role in drug detoxification. In addition, it is also involved in a variety of physiological and pathological processes, including pretoxin activation and oxidative stress responses.

The substrate binding curve of Cyp1a1 shows typical type I spectral characteristics. The electron transport system composed of CYP1A1 and cytochrome P450 reductase endows it with broad-spectrum substrate recognition ability. However, its catalytic efficiency varies significantly among different species and tissues.

Applications of Cyp1a1 and Cyp1a1 Antibody in Literature

1. Kyoreva, Mariela, et al. "CYP1A1 enzymatic activity influences skin inflammation via regulation of the AHR pathway." Journal of Investigative Dermatology 141.6 (2021): 1553-1563. https://doi.org/10.1016/j.jid.2020.11.024

This study reveals that the activity of CYP1A1 enzyme is a key negative regulatory factor of the AHR signaling pathway in skin inflammation. Elevated CYP1A1 activity can exacerbate skin immunopathology, while inhibiting its activity can restore the protective effect of AHR. Inhibition of the AHR pathway and enhanced CYP1A1 activity can be observed in patients with psoriasis, suggesting that this axis may become a new therapeutic target.

2. Androutsopoulos, Vasilis P., Aristidis M. Tsatsakis, and Demetrios A. Spandidos. "Cytochrome P450 CYP1A1: wider roles in cancer progression and prevention." BMC cancer 9.1 (2009): 187. https://doi.org/10.1186/1471-2407-9-187

This study reveals that CYP1A1 is a key metabolic enzyme regulated by AhR and plays a dual role. It can not only activate environmental carcinogens, but also participate in detoxification and activate dietary compounds with anti-cancer activity. Its ultimate impact on cancer depends on the balance between this activation and detoxification.

3. Liu, Yanli, et al. "CYP1A1 methylation mediates the effect of smoking and occupational polycyclic aromatic hydrocarbons co-exposure on oxidative DNA damage among Chinese coke-oven workers." Environmental Health 18.1 (2019): 69. https://doi.org/10.1186/s12940-019-0508-0

This study explores the effect of co-exposure to smoking and occupational PAH on oxidative DNA damage. Research has found that co-exposure of the two can cause hypomethylation of the CYP1A1 gene, and hypomethylation of CYP1A1, in turn, increases the risk of oxidative DNA damage, playing a partial mediating role in this process.

4. Ugartondo, Nerea, et al. "Functional analyses of four CYP1A1 missense mutations present in patients with atypical femoral fractures." International Journal of Molecular Sciences 22.14 (2021): 7395. https://doi.org/10.3390/ijms22147395

This study provides functional evidence that CYP1A1 gene mutations increase the risk of atypical femoral fractures. Research has found that two CYP1A1 variations, P. Arg98TRP and P. Arg136His, significantly reduce their enzymatic activity, and bisphosphonate drugs also generally inhibit this activity. The superimposed effect of the two may lead to an increased susceptibility to fractures in those who take the medicine for a long time.

5. Goh, Janice Jia Ni, et al. "Structure-based virtual screening of CYP1A1 inhibitors: towards rapid tier-one assessment of potential developmental toxicants." Archives of Toxicology 95.9 (2021): 3031-3048. https://doi.org/10.1007/s00204-021-03111-2

This study successfully constructed a virtual screening model for CYP1A1 inhibitors. This model can effectively identify known inhibitors and predict the inhibitory activity of new compounds (including various contraindicated drugs during pregnancy and environmental endocrine disruptors). Experiments have confirmed that most of the prediction results are accurate, indicating that this model can be used as a reliable tool for rapid initial screening of CYP1A1 inhibitors.

Creative Biolabs: Cyp1a1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality Cyp1a1 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom Cyp1a1 Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our Cyp1a1 antibodies, custom preparations, or technical support, contact us at email.