Recombinant Human Aryl Hydrocarbon Receptor (AHR) Protein (His)

Name: Recombinant Human Aryl Hydrocarbon Receptor (AHR) Protein (His)
Brand: Beta LifeScience
SKU: BLC-01158P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Aryl Hydrocarbon Receptor (AHR) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P35869
Target Symbol	AHR
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His
Target Protein Sequence	FICRLRCLLDNSSGFLAMNFQGKLKYLHGQKKKGKDGSILPPQLALFAIATPLQPPSILEIRTKNFIFRTKHKLDFTPIGCDAKGRIVLGYTEAELCTRGSGYQFIHAADMLYCAESHIRMIKTGESGMIVFRLLTKNNRWTWVQSNARLLYKNGRPDYIIVTQRPLTDEEGTEHLRKRNTKLPFMFTTGEAVLYEATNPF
Expression Range	220-420aa
Protein Length	Partial
Mol. Weight	29.0 kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location	Cytoplasm. Nucleus.
Database References	HGNC: 348 OMIM: 600253 KEGG: hsa:196 STRING: 9606.ENSP00000242057 UniGene: PMID: 30225717 The overexpression and activation of AHR are involved in the early development of skin squamous cell carcinomas. AHR expression correlates with EGFR expression and may influence cell proliferation. PMID: 30144817 These studies identified SNPs that were cis-eQTLs for DEFB1 and AHR and, which were associated with variation in plasma KYN concentrations that were related to severity of major depressive disordersymptoms. PMID: 29317604 rs2470893 SNP, which maps 196 bp from a CYP1A1 promoter XRE, is associated with variations in 3MC-dependent AHR binding and CYP1A1 expression. PMID: 29980579 WASH-mediated AHR expression has a critical function in the maintenance of NKp46+ innate lymphoid cells PMID: 28589939 the protective role of AhR in intestinal barrier function PMID: 29992488 Elevated AhR expression may be involved in the progression of tissue remodeling in chronic rhinosinusitis without nasal polyp without allergic rhinitis similar to TGF-beta1 expression. Conversely, lower AhR expression may be involved in allergic reactions in chronic rhinosinusitis with nasal polyp with allergic rhinitis. PMID: 29183012 These results suggest that D-Kyn increases lung cancer cells to metastasize by activating Ahr. PMID: 29442266 The role of IDO1-IDO2-AHR pathway in the TLR4-induced tolerogenic phenotype in human dendritic cells has been reported. PMID: 28256612 The association between AHR Arg55Lys polymorphism and male infertility risk was not confirmed (Meta-Analysis) PMID: 29427904 A meta-analysis of five sets of data evaluated the association of aryl hydrocarbon receptor 1661G>A with male infertility. PMID: 28712079 IDO decreased glycolysis and glutaminolysis by activating GCN2K, resulting in activation of AMPactivated protein kinase. PMID: 29693118 AHR inhibition or knockdown/knockout consistently reduced human ER-/PR-/Her2- and inflammatory breast cancer cell invasion, migration, and metastasis. This was associated with a decrease in invasion-associated genes (e.g., Fibronectin, VCAM1, Thrombospondin, MMP1) and an increase in CDH1/E-cadherin, previously associated with decreased tumor aggression. PMID: 29735912 This study demonstrated that the regulation of AHR expression by miR124 is critical to the development of inflammatory response in chronic rhinosinusitis with nasal polyps. PMID: 29605298 In human keratinocytes, authors found that perillaldehyde (1) inhibited BaP-induced AHR activation and ROS production, (2) inhibited BaP/AHR-mediated release of the CCL2 chemokine, and (3) activated the NRF2/HO1 antioxidant pathway. PMID: 29643980 Infants born to women with specific AHR and XRCC1 genotypes may have higher genetic risks for birth weight reduction PMID: 28893607 ITE suppresses growth of human pulmonary artery endothelial cells independent of AhR PMID: 29140133 High AHR expression is associated with nerve sheath tumorigenesis. PMID: 29351992 IRES (ribosome entry site)activity is increased in the PTX-resistant ovarian cancer cells in which AHR protein expression was also enhanced. These results strongly suggest an important role for AHR ribosome entry site (IRES)-dependent translation mechanism in cancer cell response to paclitaxel treatment PMID: 29048649 AhR activation by FICZ reduces FcepsilonRI and upregulates IDO expression in Langerhans cells. This AhR-mediated anti-inflammatory feedback mechanism may dampen the allergen-induced inflammation in atopic dermatitis. PMID: 28376268 Report yeast estrogen screen for androgen- and estrogen-receptor mediated activities of 4-hydroxytestosterone, 4-hydroxyandrostenedione and their human metabolites. PMID: 29702199 Report AhR-dependent transcriptional activity during acute exposure of lung cells to distinct types of environmental pollutants. PMID: 29704546 The nuclear localization signal (NLS) is closed in the absence of a ligand, the structure of AhR will be changed in the presence of a ligand, which leads to NLS open, result in the nuclear translocation of AhR. PMID: 29092071 Study provides evidence that AhR plays a critical role in polycyclic aromatic hydrocarbon-mediated DNA damage. PMID: 28886471 in transcriptionally active heterodimer with ARNT, which recognizes the dioxin response element (DRE) in the promoter of downstream genes, right next to the DRE-docking sites is the extensive dimerization surface that is more hydrophobic than other surface areas, indicating that the dimerization interface of the AHR transcription complex is largely dictated by hydrophobic contacts PMID: 28396409 AHR signaling is essential for activin A induced regulatory T cells that restrain asthmatic responses. PMID: 28320933 Aryl hydrocarbon receptor activation induced by FICZ and Glyteer increased the expression of OVOL1 and Filaggrin in a dose- and time-dependent manner in normal human epidermal keratinocytes. PMID: 28703805 Study shows the Q-rich/PST domain of the aryl hydrocarbon receptor regulates both ligand-induced nuclear transport and nucleocytoplasmic shuttling. PMID: 27535013 Data suggest that response of bronchial epithelial cells to environmental carcinogen benzo[a]pyrene includes activation of AhR/Src/ERK signaling, CYP1A1 induction, and formation of stable DNA adducts. (AhR = aryl hydrocarbon receptor; Src = Src proto-oncogene kinase; ERK = extracellular signal-regulated kinases; CYP1A1 = cytochrome P450 family 1 subfamily A member 1) PMID: 29545172 These data support a mechanistic pathway for the putative tumour suppressive role of AHR specifically in pituitary adenomas, possibly through its role as a cell cycle co-regulator, even in the absence of exogenous ligands. PMID: 28649092 upregulation of mRNA and protein expression is associated with the pathogenesis of unexplained miscarriage PMID: 28503784 The AhR physiological role in cancer [review] PMID: 28508231 Our findings suggest that AhR-mediated IL-1beta regulation in cerebral endothelium could induce BBB breakdown and contribute to the pathogenesis of a variety of neurologic disorders. PMID: 28285151 Ultraviolet B rays suppressed SIRT1 expression by activating AhR, and subsequently inhibited DNMT1 activity in CD4+ T cells from systemic lupus erythematosus patients. PMID: 28336124 AHR regulated cell proliferation and tumorigenesis by directly targeting and activating HDAC8 expression in hepatocellular carcinoma cells. PMID: 27283490 Human CCL1 gene is selectively targeted by AhR in M(IL-4) macrophage. IL-4-induced epigenetic modification potentiates AhR-mediated CCL1 expression. PMID: 27888289 Moreover, time course and promoter activity assays suggest that TIPARP and TIPARP-AS1 work in concert to regulate AHR signaling. Collectively, these data show an added level of complexity in the AHR signaling cascade which involves lncRNAs, whose functions remain poorly understood. PMID: 29274782 Utilising a three-dimensional lymph endothelial cell (LEC) monolayer & MDA-MB231 breast cancer cell spheroid co-culture model in combination with knock-down approach allowed elucidation of the molecular/biochemical basis of AHR/CYP1A1-induced tumour breaching through the LEC barrier. PMID: 28171546 breast cancer ER status likely influences AhR activity involved in these signaling pathways. The mechanisms involved in AhR activation and target gene expression in breast cancers are also discussed PMID: 29320557 AhR modulates hyperoxic lung injury by regulating the genes that are necessary for cell proliferation and inflammation. PMID: 27103661 This study of human fibroblasts bearing endogenous heterozygous AIP mutations and transfected pituitary GH3 cells shows that AIP mutations affect the AIP protein level and alter AhR transcriptional activity in a gene- and tissue-dependent manner. PMID: 27080473 We demonstrated that infants whose mothers smoked during pregnancy with the combination of AHR, CYP1A1, and XRCC1 polymorphisms had lower birth size. PMID: 27592400 A low AHR-expression level in human lung cancer tissues is significantly associated with its malignancy.Cytoplasmic, resting AHR protein acts as an epithelial-mesenchymal transition suppressor via a non-genomic pathway. PMID: 27752740 Aryl hydrocarbon receptor signaling modifies Toll-like receptor-regulated responses in human dendritic cells. PMID: 27783115 These findings identify a role for pattern recognition receptor (PRR) signaling in regulating the AHR response through selective down-regulation of Cyp1 expression in human monocytes and macrophages. PMID: 29018148 The results of the present study suggest that AhR stimulates estrogen-dependent progression of breast carcinoma by inducing aromatase expression under some conditions. These results provide new insights on the possible roles of environmental toxins in breast cancer development. PMID: 27900579 AHR, CYP1A1, CYP1A2, or CYP1B1 variants associated with head-and-neck squamous cell carcinoma risk in smokers. PMID: 27894333 Low AHR expression is associated with Prostate Cancer. PMID: 28972393 activation of the aryl hydrocarbon receptor using the non-toxic agonist 2-(1'H-indole-3'-carbonyl)-thiazole-4-carboxylic acid methyl ester (ITE) induces human regulatory t cells. PMID: 27783946 this study demonstrates a role for the AHR in regulating human B cell development, and it suggests that transcriptional alterations of EBF1 by the AHR are involved in the underlying mechanism PMID: 28978690

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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