Analytical Data
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Gene name
DRD1
- Application
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Alternative Names
DRD1；D(1A) dopamine receptor
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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
P21728
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Expression Region
338-446aa
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AA Sequence
RKAFSTLLGCYRLCPATNNAIETVSINNNGAAMFSSHHEPRGSISKECNLVYLIPHAVGSSEDLKKEEAAGIARPLEKLSPALSVILDYDTDVSLEKIQPITQNGQHPT
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Molecular Weight
17.8 kDa
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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
Dopamine receptor D1 (DRD1) is a critical G protein-coupled receptor (GPCR) primarily involved in mediating dopaminergic signaling pathways that influence various neurological and psychiatric functions. Its role in the central nervous system has made it a focal point for research related to neurological disorders such as schizophrenia, depression, and Parkinson's disease. The reconstitution and study of DRD1 as a recombinant protein allow researchers to elucidate its structural properties, ligand-binding affinities, and downstream signaling mechanisms. Producing DRD1 in a recombinant form often involves the use of cellular expression systems, such as bacteria, yeast, or mammalian cells, enabling scientists to obtain sufficient quantities of the protein for functional assays and biophysical characterization. The study of DRD1 not only aids in understanding its normal physiological functions but also provides insights into potential therapeutic targets for the development of pharmacological agents. Furthermore, the exploration of DRD1 interactions with various compounds can pave the way for novel drug design strategies that could lead to improved treatments for dopamine-related disorders. Advances in recombinant protein technology and techniques such as cryo-electron microscopy and X-ray crystallography have been instrumental in revealing the intricate details of DRD1 structure and function, thus enriching our understanding of its pivotal role in neurotransmission and behavior.
