Analytical Data
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Gene name
GHRL
- Application
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Alternative Names
GHRL；MTLRP;Appetite-regulating hormone
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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
Q9UBU3
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Expression Region
24-51aa
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AA Sequence
GSSFLSPEHQRVQQRKESKKPPAKLQPR
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Molecular Weight
34.8 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
Ghrelin, a peptide hormone predominantly produced in the stomach, plays a crucial role in regulating appetite, energy balance, and metabolism. It is known for its stimulating effect on growth hormone secretion and its involvement in various physiological processes, including food intake and weight regulation. Given its significant impact on these regulatory pathways, researchers have focused on developing recombinant ghrelin (GHRL) proteins to explore their potential therapeutic applications. The recombinant form allows for controlled studies of ghrelin's biological activities and mechanisms of action, paving the way for investigations into obesity management, metabolic disorders, and growth hormone deficiencies. Additionally, GHRL's therapeutic potential extends to conditions like cachexia, where muscle wasting occurs, as well as metabolic syndromes and age-related declines in hormone levels. The ability to produce GHRL recombinantly enhances our understanding of its structure-function relationships and enables the development of ghrelin analogs or antagonists, which can be used in clinical settings. As research continues to uncover the complex roles of ghrelin beyond appetite stimulation, including its influence on neuroendocrine functions and glucose metabolism, GHRL recombinant protein studies become increasingly vital. These advancements not only offer insights into the fundamental biology of ghrelin but also open promising avenues for novel therapeutics aimed at a variety of metabolic and endocrine disorders, highlighting the importance of recombinant protein technology in modern biomedical research.
