首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FS |
| Uniprot No | P19883 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 35-283aa |
| 氨基酸序列 | RQAKNGRCQVLYKTELSKEECCSTGRLSTSWTEEDVNDNTLFKWMIFNGG APNCIPCKETCENVDCGPGKKCRMNKKNKPRCVCAPDCSNITWKGPVCGL DGKTYRNECALLKARCKEQPELEVQYQGRCKKTCRDVFCPGSSTCVVDQT NNAYCVTCNRICPEPASSEQYLCGNDGVTYSSACHLRKATCLLGRSIGLA YEGKCIKAKSCEDIQCTGGKKCLWDFKVGRGRCSLCDELCPDSKSDEPV |
| 预测分子量 | 33 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. |
以下是关于重组蛋白(假设“FS重组蛋白”指某种功能性重组蛋白)的3篇参考文献示例，包含文献名称、作者及摘要概括：
---
1. **文献名称**：*Optimization of Recombinant FS Protein Expression in E. coli for Enhanced Stability*
**作者**：Zhang L, et al.
**摘要**：该研究通过优化大肠杆菌表达系统的培养条件(如温度、诱导剂浓度)，成功提高了FS重组蛋白的可溶性和产量，并通过质谱和圆二色谱验证了其正确折叠，为工业化生产提供了参考。
---
2. **文献名称**：*Structural and Functional Analysis of FS Recombinant Protein in Tissue Regeneration*
**作者**：Smith J, et al.
**摘要**：文章解析了FS重组蛋白的三维结构，发现其通过激活特定生长因子通路(如TGF-β)促进细胞增殖和损伤修复，动物实验显示其可加速皮肤伤口愈合，具有潜在治疗价值。
---
3. **文献名称**：*A Novel Chromatography Strategy for High-Purity FS Recombinant Protein Purification*
**作者**：Wang Y, et al.
**摘要**：研究者开发了一种结合亲和层析和离子交换的两步纯化法，显著提升了FS重组蛋白的纯度(>98%)，并降低了内毒素含量，满足药物开发的质量标准。
---
(注：以上文献为虚构示例，实际引用需检索PubMed、ScienceDirect等数据库，以“recombinant protein”“expression/purification/application”等关键词筛选。)
**Background of FS Recombinant Protein**
Recombinant FS protein, often associated with fusion proteins or specific functional domains, is a bioengineered molecule designed to address challenges in therapeutic and research applications. The term "FS" may refer to a particular fusion construct or a functionally optimized protein variant, depending on context. Recombinant proteins like FS are typically produced using genetic engineering techniques, where target genes are inserted into host systems (e.g., *E. coli*, yeast, or mammalian cells*) for expression. This approach allows large-scale production of proteins with tailored properties, such as enhanced stability, solubility, or bioactivity.
The development of FS recombinant proteins aligns with advancements in structural biology and protein engineering. For instance, fusion tags (e.g., His-tags, Fc domains) or linker sequences are often incorporated to improve purification efficiency or functional performance. In therapeutics, FS proteins might serve as biologics targeting diseases like cancer, autoimmune disorders, or infectious diseases. For example, fusion proteins combining cytokine domains with antibody fragments (immunocytokines) have been explored to enhance targeted drug delivery.
In research, FS recombinant proteins are critical tools for studying protein interactions, signaling pathways, or cellular mechanisms. They enable precise manipulation of biological systems, such as activating or inhibiting specific receptors. Challenges in their development include ensuring proper folding, post-translational modifications, and minimizing immunogenicity in clinical applications.
The FS protein concept reflects the broader trend toward precision biomedicine, where engineered proteins bridge gaps between natural molecules and therapeutic needs. Ongoing innovations in CRISPR, computational modeling, and high-throughput screening continue to refine recombinant protein design, expanding their potential in diagnostics, therapeutics, and industrial biotechnology.
×
