Analytical Data
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Gene name
GHSR
- Application
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Alternative Names
GHSR；Growth hormone secretagogue receptor type 1
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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
Q92847
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Expression Region
1-366aa
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AA Sequence
MWNATPSEEPGFNLTLADLDWDASPGNDSLGDELLQLFPAPLLAGVTATCVALFVVGIAGNLLTMLVVSRFRELRTTTNLYLSSMAFSDLLIFLCMPLDLVRLWQYRPWNFGDLLCKLFQFVSESCTYATVLTITALSVERYFAICFPLRAKVVVTKGRVKLVIFVIWAVAFCSAGPIFVLVGVEHENGTDPWDTNECRPTEFAVRSGLLTVMVWVSSIFFFLPVFCLTVLYSLIGRKLWRRRRGDAVVGASLRDQNHKQTVKMLAVVVFAFILCWLPFHVGRYLFSKSFEPGSLEIAQISQYCNLVSFVLFYLSAAINPILYNIMSKKYRVAVFRLLGFEPFSQRKLSTLKDESSRAWTESSINT
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Molecular Weight
41.3 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
GHSR (Growth Hormone Secretagogue Receptor) is a G-protein coupled receptor primarily responsible for mediating the effects of ghrelin, a peptide hormone implicated in various physiological processes, including appetite regulation, growth hormone release, and energy homeostasis. The interest in GHSR research has significantly increased due to its potential therapeutic implications in obesity, metabolic disorders, and growth-related diseases. Recombinant GHSR proteins have been developed to study their structure-function relationships, signaling pathways, and the molecular mechanisms by which ghrelin influences physiological responses. These proteins facilitate high-throughput screenings for drugs that can modulate GHSR activity, offering potential interventions for disorders linked to energy balance and metabolic dysregulation. Given the rising prevalence of obesity and metabolic syndrome globally, understanding GHSR biology through recombinant protein studies is critical for the development of innovative treatments aimed at promoting healthier metabolic pathways and overall well-being. Furthermore, the knowledge gained from these studies may open up new avenues in endocrinology and therapeutic strategies targeting GHSR-related pathways.
