Analytical Data
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Gene name
ARNT
- Application
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Alternative Names
ARNT；BHLHE2；Aryl hydrocarbon receptor nuclear translocator
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P27540
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Expression Region
1-474aa
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AA Sequence
MAATTANPEMTSDVPSLGPAIASGNSGPGIQGGGAIVQRAIKRRPGLDFDDDGEGNSKFLRCDDDQMSNDKERFARSDDEQSSADKERLARENHSEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVSHMKSLRGTGNTSTDGSYKPSFLTDQELKHLILEAADGFLFIVSCETGRVVYVSDSVTPVLNQPQSEWFGSTLYDQVHPDDVDKLREQLSTSENALTGRILDLKTGTVKKEGQQSSMRMCMGSRRSFICRMRCGSSSVDPVSVNRLSFVRNRCRNGLGSVKDGEPHFVVVHCTGYIKAWPPAGVSLPDDDPEAGQGSKFCLVAIGRLQVTSSPNCTDMSNVCQPTEFISRHNIEGIFTFVDHRCVATVGYQPQELLGKNIVEFCHPEDQQLLRDSFQQVVKLKGQVLSVMFRFRSKNQEWLWMRTSSFTFQNPYSDEIEYIICTNTNVKNSSQEPRPT
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Molecular Weight
54.8kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The research on ARNT (Aryl Hydrocarbon Receptor Nuclear Translocator) recombinant proteins has garnered significant interest in the fields of molecular biology and pharmacology due to their pivotal role in mediating cellular responses to various environmental and endogenous signals. ARNT is a critical partner for several basic helix-loop-helix (bHLH) transcription factors, particularly in the context of the aryl hydrocarbon receptor (AhR) pathway, which is fundamental for the regulation of genes involved in detoxification processes, circadian rhythm, and development. Aberrations in ARNT function have been implicated in various pathological conditions, including cancer, metabolic diseases, and neurodegenerative disorders. The production and study of recombinant ARNT proteins enable researchers to investigate their biochemical properties, interaction dynamics with ligands and other proteins, and their functional roles in signal transduction pathways. Moreover, understanding the structure-function relationships of ARNT can aid in the development of therapeutic strategies that target its pathways for disease intervention. Recent advancements in recombinant DNA technology and protein expression systems have greatly enhanced the ability to produce high-yield, functional ARNT proteins for detailed studies. This research is crucial, not only for unraveling the mechanism of action of ARNT in health and disease but also for providing insights into the design of small molecules or biotherapeutics that can modulate its activity, thereby opening new avenues for innovative treatments.
