| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GHR |
| Uniprot No | P10912 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-264aa |
| 氨基酸序列 | AILSRAPWSLQSVNPGLKTNSSKEPKFTKCRSPERETFSCHWTDEVHHGTKNLGPIQLFYTRRNTQEWTQEWKECPDYVSAGENSCYFNSSFTSIWIPYCIKLTSNGGTVDEKCFSVDEIVQPDPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVLEYELQYKEVNETKWKMMDPILTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLYVTLPQMSQFTCEEDFY |
| 预测分子量 | 58.8 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GHR(生长激素受体)重组蛋白的3篇文献示例，包含名称、作者及摘要概括：
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1. **文献名称**：*Expression and Purification of Recombinant Human Growth Hormone Receptor Extracellular Domain*
**作者**：Smith A, et al.
**摘要**：该研究利用哺乳动物细胞表达系统成功表达并纯化了人源GHR胞外结构域重组蛋白，优化了纯化流程以获得高纯度蛋白，并验证其与生长激素(GH)的结合活性，为后续结构功能研究奠定基础。
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2. **文献名称**：*Crystal Structure of the GH-GHR Complex Reveals Ligand-Induced Conformational Changes*
**作者**：Li J, Souza DH.
**摘要**：通过X射线晶体学解析了重组GHR胞外区与生长激素的复合物结构，揭示了GH结合诱导的受体二聚化机制及关键相互作用位点，为开发靶向GHR的分子药物提供了结构依据。
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3. **文献名称**：*Functional Characterization of a Recombinant GHR Mutant in Laron Syndrome*
**作者**：Wang Y, et al.
**摘要**：构建了Laron综合征相关的GHR点突变重组蛋白，发现其导致GH信号通路下游STAT5磷酸化水平显著降低，阐明该突变致病的分子机制，为基因治疗策略提供实验证据。
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注：以上文献信息为示例性内容，实际引用时需以真实发表的论文为准。建议通过PubMed或Web of Science等数据库检索关键词“recombinant GHR protein”获取具体文献。
**Background of GHR Recombinant Protein**
The Growth Hormone Receptor (GHR) is a transmembrane protein belonging to the cytokine receptor superfamily, playing a pivotal role in mediating the physiological effects of growth hormone (GH). GHR is critical for postnatal growth, metabolism regulation, and cellular processes such as proliferation and differentiation. Structurally, it consists of an extracellular domain for GH binding, a single transmembrane helix, and an intracellular domain responsible for signal transduction via JAK-STAT pathways. Dysregulation of GHR signaling is linked to disorders like growth hormone insensitivity (Laron syndrome), acromegaly, and certain cancers.
Recombinant GHR proteins are engineered using biotechnological platforms (e.g., mammalian, insect, or bacterial expression systems) to produce soluble, functional forms of the receptor, often focusing on the extracellular domain. These proteins retain high affinity for GH and are purified via techniques like affinity chromatography. Their development has enabled detailed studies of GH-GHR interactions, aiding in structural analyses (e.g., X-ray crystallography) and the design of GH antagonists or mimetics.
Clinically, GHR recombinant proteins serve as therapeutic tools. For example, pegvisomant, a modified recombinant GHR extracellular domain, acts as a competitive antagonist to treat acromegaly. Additionally, they are utilized in diagnostic assays to measure GH levels or detect GHR autoantibodies. Research applications include investigating metabolic diseases, aging, and cancer mechanisms, where altered GH signaling is implicated.
Despite advancements, challenges remain in optimizing stability, bioavailability, and cost-effective production. Ongoing studies focus on engineering hybrid receptors, improving half-life via PEGylation, and exploring gene therapy approaches. As a bridge between basic research and clinical translation, GHR recombinant proteins continue to offer insights into endocrine regulation and therapeutic innovation.
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