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AHR, Alexa Fluor 488, clone: 4MEJJ, eBioscience™

Rat Monoclonal Antibody

Manufacturer:  Life Technologies LS53592580

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Catalog No. 501124601



Description

Description

The aryl hydrocarbon receptor (AhR), also known as the dioxin receptor, is a ligand-activated helix/loop/helix transcription factor found in a variety of vertebrate species. The known ligands for AhR are foreign planar aromatic compounds, such as polycyclic aromatic compounds and halogenated aromatic compounds such as 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). Unlike the steroid/thyroid hormone receptors, there is no known physiological ligand for the Ah Receptor. Studies indicate that in non-ligand activated cells, AhR is found complexed with HSP90 predominantly in the cytoplasm. Upon binding to an agonist, the ligand-activated AhR is believed to transform to a nuclear, DNA binding form. This transformation process appears to involve dissociation of HSP90 from AhR followed by formation of a heterodimer with AhR nuclear translocator protein (Arnt). The AhR-ligand complex appears to initiate gene transcription of cytochrome P450 1A1.

Applications Tested: This 4MEJJ antibody has been tested by intracellular staining and flow cytometric analysis of TH17 polarized mouse splenocytes using the Intracellular Fixation & Permeabilization Buffer Set (cat. 88-8824) and protocol. Please refer to Best Protocols: Protocol A: Two step protocol for (cytoplasmic) intracellular proteins located under the Resources Tab online. This can be used at less than or equal to 0.5 µg per test. A test is defined as the amount (µg) of antibody that will stain a cell sample in a final volume of 100 µL. Cell number should be determined empirically but can range from 10^5 to 10^8 cells/test. It is recommended that the antibody be carefully titrated for optimal performance in the assay of interest. Excitation: 488 nm; Emission: 519 nm; Laser: Blue Laser. Filtration: 0.2 μm post-manufacturing filtered. AHR (Ah Receptor) belongs to a family of proteins comprised of its dimerization partner ARNT (HIF-1 Beta) and the Drosophila proteins PER and SIM. AHR contains an N-terminal sequence of approximately 200 amino acids termed the PAS domain. AHR, found in a variety of tissues, binds to a specific DNA enhancer sequence and initiates transcription of the mRNA for the cytochrome P-450 (CYPIA1) gene. The gene for AHR encodes a ligand-activated transcription factor involved in the regulation of biological responses to planar aromatic hydrocarbons. AHR has been shown to regulate xenobiotic-metabolizing enzymes such as cytochrome P450, and its ligands included a variety of aromatic hydrocarbons. AHR is a ligand-activated helix/loop/helix transcription factor found in a variety of vertebrate species. The known ligands for AHR are foreign planar aromatic compounds, such as polycyclic aromatic compounds and halogenated aromatic compounds such as 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). Unlike the steroid/thyroid hormone receptors, there is no known physiological ligand for AHR. Studies indicate that in non-ligand activated cells, AHR is found complexed with HSP90 predomitly in the cytoplasm. Upon binding to an agonist, the ligand-activated AhR is believed to transform to a nuclear, DNA binding form, and this transformation process appears to involve dissociation of HSP90 from AhR followed by formation of a heterodimer with AhR nuclear translocator protein (Arnt). Diseases associated with AHR include eosinophilic fasciitis and seborrheic dermatitis.
Specifications

Specifications

AHR
Monoclonal
0.5 mg/mL
PBS with 0.1% gelatin and 0.09% sodium azide; pH 7.2
P30561
Ah receptor, AhR, Class E basic helix-loop-helix protein 76, bHLHe76, AHR, BHLHE76
Rat
Affinity chromatography
RUO
Antibody
Monoclonal
Mouse
Flow Cytometry
4MEJJ
Alexa Fluor® 488
Ahr
Liquid
Ahr
IgG2a, kappa
25 μg
4° C, store in dark, DO NOT FREEZE!
Primary
11622
Documents

For Research Use Only.