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AB182642

Anti-Aryl hydrocarbon Receptor (phospho S36) antibody

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(2 Publications)

Rabbit Polyclonal Aryl hydrocarbon Receptor phospho S36 antibody. Suitable for WB and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Synthetic Peptide within Human AHR pS36 conjugated to Keyhole Limpet Haemocyanin.

View Alternative Names

BHLHE76, AHR, Aryl hydrocarbon receptor, Ah receptor, AhR, Class E basic helix-loop-helix protein 76, bHLHe76

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

Synthetic Peptide within Human AHR pS36 conjugated to Keyhole Limpet Haemocyanin. The exact immunogen used to generate this antibody is proprietary information.

P35869

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
ab182642 was purified by affinity-chromatography using epitope-specific phosphopeptide. Non-phospho specific antibodies were removed by chromatography using non-phosphopeptide.
Storage buffer
pH: 7.4 Preservative: 0.02% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.88% Sodium chloride
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The Aryl hydrocarbon Receptor (AhR) also known as the Ah receptor is a ligand-activated transcription factor expressed in various tissues including liver lung and skin. The AhR has a molecular mass of approximately 96 kDa. It forms a complex with the aryl hydrocarbon receptor nuclear translocator (ARNT) upon ligand binding. AhR can bind to several compounds including aryl azide influencing the expression of numerous genes involved in xenobiotic metabolism.
Biological function summary

The AhR plays an important role in the regulation of detoxification enzymes such as cytochrome P450s. This receptor functions as a sensor for environmental toxins activating detoxification pathways once bound to ligands. It also contributes to the modulation of immune responses and development processes. The AhR often forms part of a larger protein complex to exert its effects on gene expression and cellular processes.

Pathways

The AhR significantly participates in the xenobiotic metabolism pathway and the dioxin signaling pathway. It interacts with proteins such as ARNT and cytochrome P450 enzymes to mediate the cellular response to toxins. The activity of AhR regulates the expression of phase I and phase II detoxification enzymes making it an integral part of the body’s defense against environmental chemicals.

Disturbances in AhR activity have been linked to cancer and autoimmune diseases. Altered expression or function of AhR can contribute to aberrant cell proliferation and immune dysregulation. The AhR interacts with other proteins like peroxidase and its substrates playing a role in oxidative stress responses associated with these conditions. Understanding these links can offer insights into therapeutic targets for related diseases.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Ligand-activated transcription factor that enables cells to adapt to changing conditions by sensing compounds from the environment, diet, microbiome and cellular metabolism, and which plays important roles in development, immunity and cancer (PubMed : 23275542, PubMed : 30373764, PubMed : 32818467, PubMed : 7961644). Upon ligand binding, translocates into the nucleus, where it heterodimerizes with ARNT and induces transcription by binding to xenobiotic response elements (XRE) (PubMed : 23275542, PubMed : 30373764, PubMed : 7961644). Regulates a variety of biological processes, including angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility and immune modulation (PubMed : 12213388). Xenobiotics can act as ligands : upon xenobiotic-binding, activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene) (PubMed : 7961644, PubMed : 33193710). Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons (PubMed : 34521881, PubMed : 7961644). Next to xenobiotics, natural ligands derived from plants, microbiota, and endogenous metabolism are potent AHR agonists (PubMed : 18076143). Tryptophan (Trp) derivatives constitute an important class of endogenous AHR ligands (PubMed : 32818467, PubMed : 32866000). Acts as a negative regulator of anti-tumor immunity : indoles and kynurenic acid generated by Trp catabolism act as ligand and activate AHR, thereby promoting AHR-driven cancer cell motility and suppressing adaptive immunity (PubMed : 32818467). Regulates the circadian clock by inhibiting the basal and circadian expression of the core circadian component PER1 (PubMed : 28602820). Inhibits PER1 by repressing the CLOCK-BMAL1 heterodimer mediated transcriptional activation of PER1 (PubMed : 28602820). The heterodimer ARNT : AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (PubMed : 28602820).
See full target information AHR pS36

Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Experimental and therapeutic medicine 22:1187 PubMed34475977

2021

Effect of the acid suppressor omeprazole on the proliferation, migration, invasion and cell cycle of esophageal squamous cell carcinoma cells via the aryl hydrocarbon receptor pathway.

Applications

Unspecified application

Species

Unspecified reactive species

Yu Bai,Peiyao Zhu,Kun Zhou,Shu-Guang Zhang

EBioMedicine 45:447-455 PubMed31204276

2019

Placental effects and transfer of sildenafil in healthy and preeclamptic conditions.

Applications

Unspecified application

Species

Unspecified reactive species

Emilie Hitzerd,Michelle Broekhuizen,Katrina M Mirabito Colafella,Marija Glisic,René de Vries,Birgit C P Koch,Michiel A de Raaf,Daphne Merkus,Sam Schoenmakers,Irwin K M Reiss,A H Jan Danser,Sinno H P Simons
View all publications

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