Analytical Data
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基因名
GHSR
- Application
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别名
GHRP; GH-releasing peptide receptor; Ghrelin receptor
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种属
Human
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表达系统
E. coli
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标签
N- His & GST
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q92847
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表达区间
Met1~Arg70
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分子量
40kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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Protein Description
GHSR (Growth Hormone Secretagogue Receptor) is a G-protein-coupled receptor (GPCR) that plays a critical role in regulating growth hormone release and energy homeostasis. Its primary ligand, ghrelin, has gained attention for its involvement in appetite regulation, metabolism, and various physiological processes. Research on GHSR recombinant proteins has advanced significantly, driven by the need to understand ghrelin signaling mechanisms in detail, as well as its potential implications in obesity, diabetes, and other metabolic disorders. With the increasing prevalence of these conditions, elucidating the structure and function of GHSR is crucial. Recombinant GHSR proteins facilitate high-throughput screening of novel compounds, allowing for the identification of GHSR modulators that could serve as therapeutic agents. Additionally, the study of GHSR interactions with different ligands and signaling pathways has provided insights into GPCR functional dynamics, which are vital for drug design. Furthermore, investigating the structural biology of GHSR using techniques like X-ray crystallography and cryo-electron microscopy has enhanced our understanding of receptor activation and ligand binding, paving the way for the development of targeted treatments. Overall, the research surrounding GHSR recombinant proteins is vital for unlocking new therapeutic strategies in metabolic and endocrine disorders.












