纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | GHRH |
Uniprot No | P01286 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 19-108aa |
氨基酸序列 | CSPPPPLTLRMRRYADAIFTNSYRKVLGQLSARKLLQDIMSRQQGESNQE RGARARLGRQVDSMWAEQKQMELESILVALLQKHSRNSQG |
预测分子量 | 40 kDa |
蛋白标签 | His tag N-Terminus |
缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于GHRH(生长激素释放激素)重组蛋白的3篇代表性文献示例(部分信息基于研究方向整合,非真实文献):
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1. **文献名称**:*Cloning and Expression of Human Growth Hormone-Releasing Hormone in Escherichia coli*
**作者**:Schally AV, et al.
**摘要**:该研究通过基因工程技术成功克隆了人源GHRH基因,并利用大肠杆菌表达系统高效表达重组GHRH蛋白。纯化后的蛋白在体外实验中显示出刺激垂体细胞释放生长激素的活性,为大规模生产GHRH提供了基础。
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2. **文献名称**:*Recombinant GHRH Enhances Growth Performance in Swine Models*
**作者**:Kovacs M, et al.
**摘要**:本研究将重组猪GHRH蛋白注射至生长迟缓的猪模型中,观察到显著提高血浆GH水平和体重增长率。结果表明重组GHRH在畜牧业中具有促进动物生长的潜在应用价值。
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3. **文献名称**:*PEGylated GHRH Analog Improves Stability and Prolongs Hormone Release in Rats*
**作者**:Zhang L, et al.
**摘要**:通过聚乙二醇(PEG)修饰重组GHRH蛋白,开发了一种长效化GHRH类似物。实验显示修饰后的蛋白在小鼠体内半衰期延长了3倍,并持续刺激GH分泌,为治疗生长激素缺乏症提供了新策略。
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注:以上文献为示例性内容,实际研究中建议通过PubMed、Google Scholar等平台以关键词“recombinant GHRH”或“GHRH protein expression”检索真实文献。
Growth hormone-releasing hormone (GHRH) is a hypothalamic peptide critical for regulating growth hormone (GH) synthesis and secretion in the anterior pituitary. Discovered in the 1980s, native GHRH is a 44-amino acid neuropeptide that binds to pituitary receptors, activating cAMP pathways to stimulate GH release. GH itself plays essential roles in growth, metabolism, and tissue repair. Dysregulation of the GHRH-GH axis is linked to disorders like growth hormone deficiency (GHD), acromegaly, or age-related metabolic decline.
Recombinant GHRH proteins are engineered using genetic modification techniques, typically expressed in bacterial (E. coli), yeast, or mammalian cell systems. These bioengineered versions replicate the functional domain of native GHRH while improving stability and bioavailability. For therapeutic use, recombinant GHRH offers advantages over direct GH administration by preserving the body’s natural pulsatile GH secretion rhythm, potentially reducing side effects like insulin resistance.
Research applications include studying GH regulation mechanisms and developing treatments for GHD, particularly in cases where pituitary function remains intact. Modified analogs, such as sermorelin (a 29-amino acid fragment), were developed to enhance receptor specificity and plasma stability. Clinical trials have explored their efficacy in pediatric growth disorders, muscle-wasting conditions, and metabolic syndromes.
Beyond therapeutics, recombinant GHRH serves as a tool in endocrinology research, enabling precise modulation of GH pathways. Challenges remain in optimizing delivery methods (e.g., subcutaneous injections) and prolonging half-life through PEGylation or fusion proteins. Ongoing studies also investigate its role in aging, immune function, and tissue regeneration, highlighting its multifaceted potential in both clinical and experimental contexts.
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