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Mouse Anti-AHR Recombinant Antibody (V2-180278) (CBMAB-A1718-YC)

Provided herein is a Mouse monoclonal antibody against Human Aryl Hydrocarbon Receptor. The antibody can be used for immunoassay techniques, such as ELISA.
See all AHR antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
V2-180278
Antibody Isotype
IgG2a, κ
Application
ELISA

Basic Information

Immunogen
AHR (NP_001612, 279-376 aa) full length recombinant protein with GST tag.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Buffer
PBS, pH 7.4
Preservative
None
Concentration
Batch dependent
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
aa 279-376

Target

Full Name
aryl hydrocarbon receptor
Introduction
AHR is a ligand-activated helix-loop-helix transcription factor involved in the regulation of biological responses to planar aromatic hydrocarbons. This receptor has been shown to regulate xenobiotic-metabolizing enzymes such as cytochrome P450. Before li
Entrez Gene ID
196
UniProt ID
P35869
Alternative Names
Aryl Hydrocarbon Receptor; Class E Basic Helix-Loop-Helix Protein 76; Ah Receptor; BHLHe76; Aromatic Hydrocarbon Receptor; AH-Receptor; AhR;
Function
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. Upon ligand binding, translocates into the nucleus, where it heterodimerizes with ARNT and induces transcription by binding to xenobiotic response elements (XRE). Regulates a variety of biological processes, including angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility and immune modulation. 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). Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons. Next to xenobiotics, natural ligands derived from plants, microbiota, and endogenous metabolism are potent AHR agonists. Tryptophan (Trp) derivatives constitute an important class of endogenous AHR ligands. 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. Regulates the circadian clock by inhibiting the basal and circadian expression of the core circadian component PER1 Inhibits PER1 by repressing the CLOCK-ARNTL/BMAL1 heterodimer mediated transcriptional activation of PER1. 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.
Biological Process
Apoptotic process
Blood vessel development
cAMP-mediated signaling
Cell cycle
Cellular response to 2,3,7,8-tetrachlorodibenzodioxine
Cellular response to cAMP
Cellular response to forskolin
Circadian regulation of gene expression
Negative regulation of T cell mediated immune response to tumor cell
Negative regulation of transcription, DNA-templated
Positive regulation of transcription, DNA-templated
Positive regulation of transcription by RNA polymerase II
Regulation of adaptive immune response
Regulation of B cell proliferation
Regulation of gene expression
Regulation of transcription, DNA-templated
Regulation of transcription by RNA polymerase II
Response to toxic substance
Response to xenobiotic stimulus
Xenobiotic metabolic process
Cellular Location
Cytoplasm; Nucleus. Initially cytoplasmic; upon binding with ligand and interaction with a HSP90, it translocates to the nucleus.
Involvement in disease
Retinitis pigmentosa 85 (RP85): A form of retinitis pigmentosa, a retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. RP85 is an autosomal recessive form manifesting as early-onset progressive difficulty to adapt in dim light and gradually decreasing visual acuity in both eyes.
PTM
Mono-ADP-ribosylated, leading to inhibit transcription activator activity of AHR.

Pernomian, L., Duarte-Silva, M., & de Barros Cardoso, C. R. (2020). The aryl hydrocarbon receptor (AHR) as a potential target for the control of intestinal inflammation: insights from an immune and bacteria sensor receptor. Clinical reviews in allergy & immunology, 59(3), 382-390.

Bock, K. W. (2020). Aryl hydrocarbon receptor (AHR) functions: balancing opposing processes including inflammatory reactions. Biochemical Pharmacology, 178, 114093.

Safe, S., Jin, U. H., Park, H., Chapkin, R. S., & Jayaraman, A. (2020). Aryl hydrocarbon receptor (AHR) ligands as selective AHR modulators (SAhRMs). International Journal of Molecular Sciences, 21(18), 6654.

Sun, M., Ma, N., He, T., Johnston, L. J., & Ma, X. (2020). Tryptophan (Trp) modulates gut homeostasis via aryl hydrocarbon receptor (AhR). Critical reviews in food science and nutrition, 60(10), 1760-1768.

Bock, K. W. (2020). Aryl hydrocarbon receptor (AHR)-mediated inflammation and resolution: Non-genomic and genomic signaling. Biochemical Pharmacology, 114220.

Bock, K. W. (2019). Aryl hydrocarbon receptor (AHR): From selected human target genes and crosstalk with transcription factors to multiple AHR functions. Biochemical pharmacology, 168, 65-70.

Shinde, R., & McGaha, T. L. (2018). The aryl hydrocarbon receptor: connecting immunity to the microenvironment. Trends in immunology, 39(12), 1005-1020.

Neavin, D. R., Liu, D., Ray, B., & Weinshilboum, R. M. (2018). The role of the aryl hydrocarbon receptor (AHR) in immune and inflammatory diseases. International journal of molecular sciences, 19(12), 3851.

Seok, S. H., Ma, Z. X., Feltenberger, J. B., Chen, H., Chen, H., Scarlett, C., ... & Xing, Y. (2018). Trace derivatives of kynurenine potently activate the aryl hydrocarbon receptor (AHR). Journal of Biological Chemistry, 293(6), 1994-2005.

Esser, C., Lawrence, B. P., Sherr, D. H., Perdew, G. H., Puga, A., Barouki, R., & Coumoul, X. (2018). Old receptor, new tricks—the ever-expanding universe of aryl hydrocarbon receptor functions. Report from the 4th AHR Meeting, 29–31 August 2018 in Paris, France. International journal of molecular sciences, 19(11), 3603.

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

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