Recombinant Human HIF1B Protein

Name: Recombinant Human HIF1B Protein
Brand: Beta LifeScience
SKU: BL-1559SG
Availability: InStock

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

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Product Overview

Tag	GST
Host Species	Human
Accession	NM_001668
Synonym	ARNT; bHLHe2; HIF-1-beta; HIF-1beta; HIF1-beta; HIF1BETA; TANGO
Background	The transcription factor Aryl hydrocarbon receptor nuclear translocator (ARNT), alternatively named Hypoxia-inducible factor (HIF)-1beta, is part of the Hypoxia-inducible factor (HIF) pathway which mediates cellular adaptations to hypoxia and promotes tumour progression. Unlike HIF-1alpha that is regulated in an oxygen-dependent manner, HIF-1beta is constitutively expressed. It has been shown that some tumour cells are capable to elevate HIF-1beta in response to hypoxia to for a clonal advantage. HIF-1beta binds HIF-1alpha, and forms the transcriptional active HIF-1 complex in the nucleus.
Description	Full-length recombinant human HIF1B was produced by baculovirus in Sf9 cells, fused with a GST tag at N-terminus. This protein is purified with our unique purification methods.
Source	Sf9 insect cells
AA Sequence	Full Length
Molecular Weight	120 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human HIF1B Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Required for activity of the Ah (dioxin) receptor. This protein is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex then initiates transcription of genes involved in the activation of PAH procarcinogens. The heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters and functions as a transcriptional regulator of the adaptive response to hypoxia. 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	Nucleus.
Database References	HGNC: 700 OMIM: 126110 KEGG: hsa:405 STRING: 9606.ENSP00000351407 UniGene: PMID: 27774982 in transcriptionally active heterodimer with AHR, 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 Here the authors examined the crystal structures of multi-domain NPAS1-ARNT and NPAS3-ARNT-DNA complexes, discovering each to contain four putative ligand-binding pockets. PMID: 27782878 Findings reveal that certain blood cancers rely on ARNT isoform 1 to potentiate proliferation by antagonizing RelB and p53-dependent cell cycle arrest and apoptosis. PMID: 26909609 The structure clearly disclosed that AhRR competitively represses AhR binding to ARNT and target DNA and further suggested the existence of an AhRR-ARNT-specific repression mechanism. This study provides a structural basis for understanding the mechanism by which AhRR represses AhR-mediated gene transcription. PMID: 28904176 Study showed that polymorphism rs2228099 of the ARNT gene could be a novel susceptibility gene to essential hypertension. PMID: 27977510 The results revealed a HIF-1alpha-dependent mechanism leading to ARNT upregulation in hypoxia. PMID: 27362802 The protein levels of phosphorylated (p)Akt, Erk1/2, pErk1/2, HIF1alpha and HIF1beta were significantly increased by 5.89, 0.5, 0.59, 1.46 and 0.92fold, respectively, in the patients with PAH, compared with those in the controls group PMID: 27667582 this study shows that ARNT is upregulated in skin from atopic dermatitis patients in China PMID: 27129092 Authors report here that not only HIF1alpha but also ARNT regulates VEGF expression in 3D cancer spheroids. Results suggest the utility of the in vitro 3D cancer spheroid model for investigating angiogenesis in cancerous tissues. PMID: 27542820 The results of this study indicate that ARNT depletion renders tumour cells susceptible to radiation whereas overexpression of this transcription factor confers radioresistance PMID: 26572229 HIF-1beta might act as a novel cross-link between the HIF and NF-kappaB pathways in suppression of angiogenesis by LDL, while proteasome inhibitors might promote angiogenesis by reactivating this signaling cascade under hyperlipidemia. PMID: 26388611 ARNT Val189Val polymorphism is not associated with endometriosis in Asians. PMID: 26101050 HIF1 regulates claudin-1 in intestinal epithelium. This regulation is important for intestinal epithelial tight junction integrity. PMID: 25904334 Down-regulation of ARNT promotes colorectal cancer metastasis by activating the fibronectin/integrin beta1/FAK axis. PMID: 25839165 AhR/ARNT activation and overexpression of BCL6 are collectively responsible for differential expression of more than 100 genes in diffuse large B-cell lymphoma cell line. PMID: 25769544 Data indicate that silencing of hypoxia-inducible factor-1 beta (HIF-1beta) sensitizes tumor cells to hypoxic apoptosis. PMID: 25068796 ARNT expression in the placental vasculature mediates key angiogenic expression and fetoplacental endothalial cell angiogenesis, and low ARNT expression in FGRadv ECs appears to be a key factor in deficient angiogenesis. PMID: 25343232 findings suggest that TACC3 could be recruited as a bridge to cooperatively mediate between the HIF-2alpha PAS-B.ARNT PAS-B complex, thereby participating more directly in HIF-dependent gene transcription than previously anticipated PMID: 25627682 The objective of this review is therefore to highlight and summarize current knowledge regarding the hypoxia-dependent upregulation of ARNT PMID: 24849811 Arnt suppressed CXCL8, but did not prevent the p65-activation directly. PMID: 25201625 knockdown of ARNT in cancer cells reduced the proliferation rate and the transformation ability of those cells. PMID: 24921657 Myeloid ARNT is important for innate immune function and wound healing. PMID: 24990649 We demonstrate that Arnt is an interaction partner for Miz-1, and that Arnt has a functional role in the regulation of CDKN2B PMID: 24618291 Here we discuss recent findings from our lab and others that define roles of the HIF-VEGF axis in the retina. PMID: 24664708 ARNT gene deletion is associated with chronic lymphocytic leukemia. PMID: 24249660 These findings highlight the importance of the hypoxia-sensing pathway and HIFs in clinical hematology. PMID: 24371328 Understanding the DNA binding-independent functions of ARNT may identify novel therapeutic options for the treatment of a large spectrum of disease states. PMID: 23116263 ARNT may modulate reactive oxygen species signaling and drug response in acute myeloid leukemia. PMID: 24220583 ARNT was found to be responsible for establishing the drug-resistant properties of cancer cells by upregulation of MDR1. PMID: 23907215 results suggest that polymorphism located in the promoter of the AHR gene is associated with a protective effect on vitiligo in Han Chinese populations PMID: 22211302 In loco synthesis of these highly potent AhR inducers by Malassezia yeasts could have a significant impact on skin homeostatic mechanisms and disease development. PMID: 23448877 results show that ER-beta suppresses HIF-1alpha-mediated transcription via aryl hydrocarbon receptor nuclear translocator (ARNT) downregulation, which may account for the tumour suppressive function of ER-beta PMID: 21435239 Among a panel of five different cell lines, in 518A2 cells exposed to hypoxia-mimetic cobalt chloride, HIF-1beta is rapidly elevated on protein level. PMID: 23541582 ARNT controls AREG expression and the downstream EGFR-ERK pathway in keratinocytes, at least in part, by modulating HDAC activity. PMID: 22505606 Binding of the ERalpha and ARNT1 AF2 domains to exon 21 of the SRC1 isoform SRC1e is essential for estrogen- and dioxin-transcription. PMID: 22328528 Ainp1 reduces the interaction between ARNT and HIF-1alpha, suppresses the formation of the HIF-1 gel shift complex, and suppresses the ARNT recruitment to the vegf promoter. PMID: 22306343 miR-24 negatively regulates ARNT expression in human liver, affecting the expression of its downstream genes. miR-24 would be one of the factors underlying the mechanisms by which ARNT protein is decreased by reactive oxygen species PMID: 22387692 Data show that ARNT is an important regulator of hepatocellular carcinoma (HCC) growth and metastasis and could be a promising prognostic candidate in HCC patients. PMID: 21544813 The presence of five unique SNPs at the ARNT locus are shown. PMID: 21828933 ARNT may regulate many processes relevant to the biology of age related macular degeneration. PMID: 22183315 mutations on ARNT PAS-B modulate coactivator selectivity and target gene induction by HIF in vivo, demonstrating a bifunctional role for transcriptional regulation by PAS domains within bHLH-PAS transcription factors PMID: 21512126 NF-kB controls the levels of HIF-1a and HIF-1b genes by direct regulation. PMID: 21298084 Cloning and functional analysis of the HIF-1beta promoter identifies a prominent region for interferon (IFN)-gamma-dependent repression. PMID: 21199896 These results reveal a novel mechanism by which ARNT acts as a modulator to bridge the c-Jun/Sp1 interaction and plays a role in EGF-mediated gene expression under normoxic conditions. PMID: 20508969 Reverse transcriptase-polymerase chain reaction analysis disclosed the existence of a ETV6-ARNT fusion gene in a patient with childhood T lymphoblastic leukemia. PMID: 20804916 the expression of miR-101 is also modulated at different physiological conditions, such as androgen stimulation and HIF-1alpha/HIF-1beta induction. PMID: 20478051 the expression of ARNT protein is significantly reduced in aryl hydrocarbon receptor interacting protein mutation+ tumors PMID: 19850893 SRC-1, NCoA-2, and p/CIP are capable of independently enhancing TCDD-dependent induction of a luciferase reporter gene by the AHR/ARNT dimer PMID: 12024042 modification by SUMO-1 chiefly at Lys(245) within the PAS domain of this protein, both in vivo and in vitro PMID: 12354770

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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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