Recombinant Human ARNT/HIF-1 beta GST (N-Term) Protein

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SDS-Page: Recombinant Human ARNT/HIF-1 beta GST (N-Term) Protein [H00000405-Q01] - SDS-PAGE analysis using Recombinant Human ARNT/HIF-1 beta GST (N-Term) protein on 12.5% gel stained with Coomassie Blue.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications WB, ELISA, PA, PAGE, AP

Order Details

Recombinant Human ARNT/HIF-1 beta GST (N-Term) Protein Summary

Description
A recombinant protein with a N-terminal GST tag corresponding to the amino acid sequence 1-110 of Human ARNT/HIF-1 beta

Source: Wheat Germ (in vitro)

Amino Acid Sequence: MAATTANPEMTSDVPSLGPAIASGNSGPGIQGGGAIVQRAIKRRPGLDFDDDGEGNSKFLRCDDDQMSNDKERFARSDDEQSSADKERLARENHSEIERRRRNKMTAYIT

Preparation
Method
in vitro wheat germ expression system
Details of Functionality
This protein was produced in an in vitro wheat germ expression system that should preserve correct conformational folding that is necessary for biological function. While it is possible that this protein could display some level of activity, the functionality of this protein has not been explicitly measured or validated.
Source
Wheat germ
Protein/Peptide Type
Partial Recombinant Protein
Gene
ARNT
Purity
>80% by SDS-PAGE and Coomassie blue staining

Applications/Dilutions

Theoretical MW
37.73 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

Storage
Store at -80C. Avoid freeze-thaw cycles.
Buffer
50 mM Tris-HCI, 10 mM reduced Glutathione, pH 8.0 in the elution buffer.
Preservative
No Preservative
Purity
>80% by SDS-PAGE and Coomassie blue staining

Notes

This product is produced by and distributed for Abnova, a company based in Taiwan.

Alternate Names for Recombinant Human ARNT/HIF-1 beta GST (N-Term) Protein

  • ARNT protein
  • ARNT
  • aryl hydrocarbon receptor nuclear translocator
  • BHLHE2
  • Class E Basic Helix-Loop-Helix Protein 2
  • Dioxin Receptor, Nuclear Translocator
  • HIF1 beta
  • HIF-1 beta
  • HIF1B
  • HIF1BETA
  • HIF-1beta
  • HIF-1-beta
  • HIF1-beta
  • hypoxia-inducible factor 1, beta subunit
  • Hypoxia-inducible factor 1-beta
  • TANGO

Background

Aryl hydrocarbon nuclear translocator (ARNT), also commonly known as Hypoxia-inducible factor 1-beta (HIF-1 beta), is a ubiquitously expressed transcription factor that is part of the basic-helix-loop-helix (bHLH)-Per-ARNT-Sim (PAS) family (1, 2). Human arnt is located on chromosome 1q21 and encodes a protein 789 amino acids (aa) in length with a theoretical molecular weight of 87 kDa (1). Structurally, ARNT has a DNA binding bHLH domain, two PAS domains required for dimerization, and a transactivation domain/PAC region (1). ARNT belongs to the Class II bHLH-PAS proteins and is able to homodimerize or heterodimerize with the Class I proteins including AHA, AHRR, HIF-1 alpha, HIF-2 alpha, NPAS1, and SIM1 (2). Dimerization allows for efficient DNA binding and regulation of their target genes (2).

ARNT has an important role in two specific signaling pathways - the aryl hydrocarbon receptor (AhR) and the hypoxia inducible factor (HIF) pathway (1). In the AhR pathway, AhR in the cytosol is typically inactive and bound to heat shock protein 90 (hsp90) (3). Upon activation and ligand binding by environmental pollutants such as dioxins, AhR is translocated to the nucleus, dissociates from hsp90, and dimerizes with ARNT, leading to binding to response elements and expression of target genes including monooxygenases (1, 3). In the HIF pathway, under hypoxia (low oxygen) conditions prolylhydroxylase domain (PHD) enzymes and factor inhibiting HIF (FIH) are inhibited. HIF-1 alpha (or HIF-2 alpha) accumulates and is transported to the nucleus where it heterodimerizes with ARNT, allowing for binding to target gene's hypoxia response element (HRE), recruitment of coactivators, and transcription (1, 3). HIF-induced gene transcription plays a large role in tumor progression by promoting invasion, metastasis, de-differentiation and altered metabolism, and angiogenesis (1). While HIF-1 alpha's stability is dependent upon oxygen conditions, HIF-1 beta is stable in both normoxia and hypoxia (1-3).

The bHLH-PAS family and ARNT have been linked with a variety of pathologies and diseases including cancer, metabolic diseases, autoimmune diseases, and psychiatric disorders (2). ARNT/AHR is expressed in the skin and its pathway activation enhances skin barrier function and epidermal terminal differentiation, thus AHR agonists are currently being used as therapeutics for atopic dermatitis and psoriasis (4). Accordingly, studies of Arnt-deficient mice show profound abnormalities in skin barrier function and keratinization (4). Additionally, studies suggest that ARNT plays an important role in diabetes and beta-cell function (5). Islets from patients with type 2 diabetes have a significantly decreased ARNT expression compared to glucose-tolerant control donors (5). Modulation and stimulation of the HIF pathway may be a potential therapeutic strategy for treating type 2 diabetes and metabolic syndrome (5).

Alternate names for ARNT/HIF-1 beta include aryl hydrocarbon receptor nuclear translocator, BHLHE2, class E basic helix-loop-helix protein 2, Dixon receptor nuclear translocator, Hypoxia-inducible factor 1-beta, nuclear translocator, and TANGO.

References

1. Mandl, M., & Depping, R. (2014). Hypoxia-inducible aryl hydrocarbon receptor nuclear translocator (ARNT) (HIF-1beta): is it a rare exception?. Molecular medicine (Cambridge, Mass.). https://doi.org/10.2119/molmed.2014.00032

2. Wu, D., & Rastinejad, F. (2017). Structural characterization of mammalian bHLH-PAS transcription factors. Current opinion in structural biology. https://doi.org/10.1016/j.sbi.2016.09.011

3. Esser, C., & Rannug, A. (2015). The aryl hydrocarbon receptor in barrier organ physiology, immunology, and toxicology. Pharmacological reviews.https://doi.org/10.1124/pr.114.009001

4. Furue, M., Hashimoto-Hachiya, A., & Tsuji, G. (2019). Aryl Hydrocarbon Receptor in Atopic Dermatitis and Psoriasis. International journal of molecular sciences. https://doi.org/10.3390/ijms20215424

5. Girgis, C. M., Cheng, K., Scott, C. H., & Gunton, J. E. (2012). Novel links between HIFs, type 2 diabetes, and metabolic syndrome. Trends in endocrinology and metabolism: TEM, https://doi.org/10.1016/j.tem.2012.05.003

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.

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FAQs for ARNT/HIF-1 beta Partial Recombinant Protein (H00000405-Q01). (Showing 1 - 3 of 3 FAQ).

  1. Is this target appropriate for use in Chromatin Research?
    • Yes; here is a list of research areas that we have deemed appropriate for the target "ARNT/HIF-1 beta": Angiogenesis, Autophagy, Cancer, Cellular Markers, Chromatin Research, HIF Target Genes, Hypoxia, Transcription Factors and Regulators, Cardiovascular Biology, Lipid and Metabolism.
  2. For use in Western Blot with HIF-1 beta antibodies, what molecular weight of the band should I expect to see?
    • The theoretical molecular weight determined by our technical team for ARNT/HIF-1 beta antibodies is 86.6 kDa.
  3. If this product is used in an application or species as a part of a customer review, will that validate this product in the application/species?
    • If any of our primary antibodes are used in an untested application or species and it is shown to work through images from customer reviews or through publications, this validates the application/species for this product, allowing the tested application/species to fall under our 100% guarantee. Please check out our Innovator's Reward Program if you decide to test a primary antibody with a species or application that is not currently listed. Please note that the Innovator's Reward Program only applies to our primary antibodies.

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HIF-2 alpha: HIF1A's Homologue with Similar and Divergent Functions
HIF-2 alpha is a member of the heterodimeric hypoxia-inducible factors/HIFs family (HIF-1, HIF-2, and HIF-3) which contains a common beta subunit but differ in their alpha subunits. Also called as EPAS1 or Mop2, HIF-2 alpha regulates cellular adapt...  Read full blog post.

HIF-3 alpha: a versatile target with hypoxia dependent and independent functions
By: Subhash GangarHIF-3 alpha (hypoxia-inducible factor 3-alpha/ HIF3A) represents an isoform of HIF-alpha subunits which heterodimerize with stable beta subunit (HIF-beta) for the regulation of HIF target genes through binding to hypoxia respon...  Read full blog post.

HIF-1 beta - activating gene transcription in response to hypoxia
Hypoxia-inducible factor 1 (HIF-1) is a heterodimeric transcription factor consisting of alpha and beta subunits. The levels of functional HIF-1 in the cell depends on the level of oxygen allowing cells to respond to hypoxic conditions. HIF-1a is a...  Read full blog post.

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Bioinformatics

Gene Symbol ARNT