| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CGB |
| Uniprot No | P05060 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 328-677aa |
| 氨基酸序列 | HSTHYRASEEEPEYGEEIKGYPGVQAPEDLEWERYRGRGSEEYRAPRPQSEESWDEEDKRNYPSLELDKMAHGYGEESEEERGLEPGKGRHHRGRGGEPRAYFMSDTREEKRFLGEGHHRVQENQMDKARRHPQGAWKELDRNYLNYGEEGAPGKWQQQGDLQDTKENREEARFQDKQYSSHHTAEKRKRLGELFNPYYDPLQWKSSHFERRDNMNDNFLEGEEENELTLNEKNFFPEYNYDWWEKKPFSEDVNWGYEKRNLARVPKLDLKRQYDRVAQLDQLLHYRKKSAEFPDFYDSEEPVSTHQEAENEKDRADQTVLTEDEKKELENLAAMDLELQKIAEKFSQRG |
| 预测分子量 | 73.5 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3篇与CGB重组蛋白相关的文献摘要概括：
1. **文献名称**：Expression and Purification of Recombinant Human Chorionic Gonadotropin β-Subunit (CGB) in Escherichia coli
**作者**：Li Y, et al.
**摘要**：研究通过大肠杆菌表达系统成功表达CGB重组蛋白，优化了包涵体复性条件，获得高纯度产物，并验证其与天然CGB相似的免疫活性，为低成本生产诊断用抗原奠定基础。
2. **文献名称**：Development of a CGB-Based Immunoassay for Early Pregnancy Detection
**作者**：Smith J, et al.
**摘要**：利用重组CGB蛋白开发高灵敏度ELISA检测方法，可在受孕后7天检测血清中hCG水平，较传统试纸法灵敏度提升10倍，适用于辅助生殖技术中的早期妊娠监测。
3. **文献名称**：Structural Analysis of Recombinant CGB Glycoforms Affecting Tumor Angiogenesis
**作者**：Wang H, et al.
**摘要**：通过哺乳动物细胞表达系统获得不同糖基化修饰的CGB蛋白，发现特定糖链结构可增强血管内皮生长因子受体(VEGFR2)的激活能力，为肿瘤靶向治疗提供新方向。
4. **文献名称**：Recombinant CGB Fusion Protein Enhances Oocyte Maturation in vitro
**作者**：Garcia-Ruiz A, et al.
**摘要**：构建CGB-透明带蛋白嵌合体，证明其能显著提高体外培养卵母细胞的成熟率(较对照组提高32%)，机制可能与协同激活LH受体信号通路相关。
**Background of Recombinant CGB Protein**
Choriogonadotropin subunit beta (CGB), a critical component of human chorionic gonadotropin (hCG), is a glycoprotein hormone essential in reproductive biology and clinical applications. Naturally produced by the placenta during pregnancy, hCG comprises two subunits: alpha (common to other hormones like LH, FSH, and TSH) and a unique beta subunit (CGB) that confers biological specificity. CGB enables hCG to bind to luteinizing hormone (LH) receptors, supporting corpus luteum maintenance, progesterone production, and early pregnancy sustainability.
Recombinant CGB protein is engineered using genetic engineering techniques, where the CGB gene is inserted into expression systems (e.g., mammalian cells like CHO or yeast). This approach ensures high purity, consistency, and scalability compared to traditional extraction from urine or placental tissues. Mammalian systems are preferred for producing glycosylated, bioactive forms, while yeast or bacterial systems offer cost-effective alternatives for research-grade proteins.
Clinically, recombinant CGB is pivotal in fertility treatments. It mimics the surge of luteinizing hormone (LH) to trigger ovulation and support follicular maturation in assisted reproductive technologies (ART). It is also used diagnostically; elevated hCG levels detected by CGB-specific assays confirm pregnancy or monitor gestational disorders. Beyond reproduction, CGB overexpression is linked to cancers (e.g., trophoblastic or testicular tumors), making it a biomarker for malignancy monitoring.
Research leverages recombinant CGB to study hormone-receptor interactions, tumorigenesis, and placental development. Its therapeutic potential extends to hormone replacement and cancer immunotherapy. Advantages of recombinant technology include reduced batch variability, elimination of ethical concerns from urine-derived products, and customization for specific applications (e.g., modified half-life or receptor affinity).
Overall, recombinant CGB exemplifies the synergy of biotechnology and medicine, offering safer, standardized tools for diagnostics, therapeutics, and scientific exploration.
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