| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CST7 |
| Uniprot No | O76096 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-145aa |
| 氨基酸序列 | GPSPDTCSQDLNSRVKPGFPKTIKTNDPGVLQAARYSVEKFNNCTNDMFL FKESRITRALVQIVKGLKYMLEVEIGRTTCKKNQHLRLDDCDFQTNHTLK QTLSCYSEVWVVPWLQHFEVPVLRCHVDHHHHHH |
| 预测分子量 | 16 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CST7重组蛋白的3篇文献示例(注：文献为示例性内容，实际引用时请核实准确性)：
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1. **标题**: *Recombinant Human Cystatin F Suppresses NK Cell Cytotoxicity via Inhibition of Cathepsin C Activity*
**作者**: Hamilton, G., et al.
**摘要**: 本研究通过重组表达人胱抑素F(CST7)，发现其通过抑制组织蛋白酶C的活性，显著降低自然杀伤(NK)细胞的细胞毒性，揭示了其在免疫调节中的潜在作用机制。
2. **标题**: *Cystatin F as a Regulator of Immune Response: Production and Functional Analysis of Recombinant Protein*
**作者**: Magister, Š., et al.
**摘要**: 作者成功在大肠杆菌中表达并纯化重组CST7蛋白，证明其可抑制T淋巴细胞中的半胱氨酸蛋白酶活性，提示其在自身免疫性疾病或癌症治疗中的潜在应用价值。
3. **标题**: *Cloning and Characterization of Recombinant Cystatin F for Antiviral Research*
**作者**: Langerholc, T., et al.
**摘要**: 该研究克隆并表达了重组CST7蛋白，发现其能够抑制某些病毒蛋白酶活性，为开发基于胱抑素F的抗病毒疗法提供了实验依据。
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如需查找真实文献，建议在PubMed或Google Scholar中检索关键词：**"recombinant cystatin F"** 或 **"CST7 protein expression"**，并筛选近年研究。
Cystatin F (CST7), a member of the cystatin superfamily of cysteine protease inhibitors, plays a critical role in regulating proteolytic activity within intracellular and extracellular environments. Encoded by the CST7 gene in humans, this protein is distinguished by its ability to inhibit cathepsins—lysosomal cysteine proteases involved in protein degradation, antigen processing, and immune response modulation. Unlike other cystatins, CST7 is synthesized as an inactive proform requiring proteolytic cleavage for activation, a feature that allows precise control over its inhibitory function in specific physiological contexts.
Research highlights its expression in immune cells, particularly cytotoxic T lymphocytes and natural killer cells, where it modulates immune synapse formation and cytotoxic granule secretion. Dysregulation of CST7 has been implicated in pathological conditions, including cancer, neurodegenerative diseases, and viral infections. For instance, elevated CST7 levels in tumor microenvironments may suppress immune cell activity, facilitating immune evasion, while its deficiency has been linked to uncontrolled proteolysis in neurodegenerative processes.
Recombinant CST7 protein, produced via heterologous expression systems (e.g., E. coli or mammalian cells), enables detailed studies of its structure-function relationships and therapeutic potential. Engineered variants with optimized stability or modified inhibitory profiles are being explored for applications in immunotherapy, biomarker development, and targeted drug delivery. Its role as a dual regulator of protease activity and immune signaling continues to drive interest in both basic research and translational medicine, positioning recombinant CST7 as a versatile tool for understanding disease mechanisms and developing precision therapies.
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