| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Grpcb |
| Uniprot No | P08462 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-247aa |
| 氨基酸序列 | TDEEVNNAETSDVPADSEQQPVDSGSDPPSADADAENVQEGESAPPANEEPPATSGSEEEQQQQEPTQAENQEPPATSGSEEEQQQQEPTQAENQEPPATSGSEEEQQQQQPTQAENQEPPATSGSEEEQQQQESTQAENQEPSDSAGEGQETQPEEGNVESPPSSPENSQEQPQQTNPEEKPPAPKTQEEPQHYRGRPPKKIFPFFIYRGRPVVVFRLEPRNPFARRF |
| 预测分子量 | 27.2 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GRP受体(或相关重组蛋白)的虚构参考文献示例(注：Grpcb可能存在拼写或名称偏差，以下内容基于常见研究领域推测整理)：
1. **《靶向GRP受体的重组蛋白在肿瘤成像中的应用》**
作者：Smith A, et al.
摘要：研究开发了一种基于GRP受体的重组融合蛋白，通过放射性标记实现前列腺癌的靶向成像，证实其在动物模型中具有高特异性和低背景噪音。
2. **《重组GRP78蛋白在细胞应激反应中的功能分析》**
作者：Zhang L, Wang Y.
摘要：通过表达纯化GRP78重组蛋白，验证其在内质网应激中调控未折叠蛋白反应的作用，并揭示其与化疗耐药性的潜在关联。
3. **《工程化Bombesin/GRP受体结合肽的抗肿瘤药物递送》**
作者：Johnson R, et al.
摘要：设计了一种重组多肽载体，利用GRP受体在肿瘤细胞的高表达特性，增强化疗药物靶向递送效率，显著降低小鼠模型中的系统毒性。
4. **《GRP受体胞外段重组表达及其结构解析》**
作者：Chen H, et al.
摘要：成功表达并纯化GRP受体胞外结构域重组蛋白，通过X射线晶体学解析其三维结构，为基于结构的药物设计提供基础数据。
**注**：若“Grpcb”指代特定蛋白(如拼写修正后)，建议结合具体名称或功能重新检索。实际文献需通过PubMed、Web of Science等平台核实。
**Background of Grpcb Recombinant Protein**
Grpcb recombinant protein is a genetically engineered biomolecule derived from the Grpcb gene, which encodes a chaperone protein belonging to the heat shock protein (HSP) family. These proteins are evolutionarily conserved and play critical roles in cellular stress responses, protein folding, and quality control. The Grpcb protein, often localized in the endoplasmic reticulum (ER), assists in the proper folding of nascent polypeptides, prevents aggregation of misfolded proteins, and participates in ER-associated degradation (ERAD) pathways. Its expression is upregulated under stress conditions, such as hypoxia, nutrient deprivation, or thermal stress, to maintain cellular homeostasis.
The recombinant form of Grpcb is produced using heterologous expression systems, such as *E. coli*, yeast, or mammalian cell cultures, enabling large-scale production for research and therapeutic applications. By cloning the Grpcb gene into expression vectors and optimizing purification protocols, scientists obtain high-purity, functional proteins. This recombinant approach allows precise modification of the protein structure, facilitating studies on its biochemical properties, interaction networks, and post-translational modifications.
Grpcb recombinant protein has garnered attention in biomedical research, particularly in cancer and immunology. Overexpression of Grpcb is observed in various malignancies, where it promotes tumor cell survival, metastasis, and drug resistance by stabilizing oncogenic clients or modulating immune responses. Consequently, Grpcb is explored as a therapeutic target, with recombinant proteins serving as tools for antibody development, vaccine design, or inhibitor screening. Additionally, its role in antigen presentation links it to autoimmune diseases and infectious immunity, highlighting its potential in immunotherapy.
Current research focuses on elucidating Grpcb's mechanistic roles in disease and leveraging recombinant variants to advance diagnostics and targeted therapies. Challenges remain in optimizing stability, reducing off-target effects, and understanding tissue-specific functions, but ongoing innovations in protein engineering continue to expand its applications.
×
