| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GNLY |
| Uniprot No | P22749 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-145aa |
| 氨基酸序列 | RLSPEYYDLARAHLRDEEKSCPCLAQEGPQGDLLTKTQELGRDYRTCLTI VQKLKKMVDKPTQRSVSNAATRVCRTGRSRWRDVCRNFMRRYQSRVTQGL VAGETAQQICEDLRLCIPSTGPL |
| 预测分子量 | 14 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GNLY(Granulysin)重组蛋白的3篇参考文献示例(基于真实研究领域背景，具体作者和年份可能有调整)：
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1. **标题**: *"Granulysin, a novel antimicrobial protein of cytotoxic T cells and natural killer cells, activates apoptosis in target cells"*
**作者**: Krensky, A.M., Clayberger, C.
**摘要**: 研究揭示了重组GNLY蛋白的抗菌和促凋亡功能，发现其能通过破坏细胞膜完整性诱导靶细胞(如感染结核杆菌的巨噬细胞)凋亡，并与穿孔素协同作用增强细胞毒性。
2. **标题**: *"Structural and functional analysis of recombinant human granulysin"*
**作者**: Deng, H., et al.
**摘要**: 通过大肠杆菌表达系统成功纯化重组GNLY蛋白，解析其晶体结构，发现其α-螺旋结构域对抗微生物活性至关重要，并验证其对多种病原体的体外杀伤效果。
3. **标题**: *"Recombinant granulysin exhibits antitumor activity in vitro and in vivo"*
**作者**: Okada, S., et al.
**摘要**: 实验证明重组GNLY蛋白能选择性杀伤肿瘤细胞，并通过激活凋亡通路抑制小鼠模型中的肿瘤生长，提示其在癌症免疫治疗中的潜在应用价值。
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**备注**：以上文献为示例，实际引用时建议通过PubMed或Google Scholar检索最新研究，关键词如“recombinant granulysin”或“GNLY protein expression”。
GNLY (Granulysin) is a cytolytic protein primarily produced by human natural killer (NK) cells and cytotoxic T lymphocytes (CTLs). Discovered in the late 1980s, it is a member of the saposin-like protein (SAPLIP) family and plays a critical role in innate and adaptive immunity. GNLY is stored in cytotoxic granules alongside perforin and granzymes, which are released upon immune cell activation to eliminate infected or malignant cells. Its unique structure comprises two distinct domains: a saposin-like domain responsible for membrane interaction and a unstructured cationic domain enabling broad pathogen targeting.
Functionally, GNLY exhibits dual antimicrobial and antitumor activities. It disrupts microbial membranes (bacteria, fungi, parasites) through electrostatic interactions with negatively charged lipid components, while also inducing apoptosis in cancer cells via both membrane disruption and intracellular pathways. Notably, GNLY can penetrate host cells to target intracellular pathogens without damaging the host cell membrane, a feature distinguishing it from other cytotoxic proteins.
Recombinant GNLY production, typically using E. coli or mammalian expression systems, enables research into its therapeutic potential. The 9 kDa and 15 kDa isoforms (post-translational processing variants) are commonly studied. Purified recombinant GNLY has shown promise in preclinical studies for treating multidrug-resistant infections, enhancing cancer immunotherapy, and modulating immune responses. Its ability to synergize with conventional antibiotics and chemotherapeutic agents while maintaining selectivity for pathogenic cells has generated significant interest in therapeutic development. Current research focuses on optimizing its stability, delivery mechanisms, and combination therapies for clinical applications.
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