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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GCSF |
| Uniprot No | P09919 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 31-207aa |
| 氨基酸序列 | TPLGPASSLPQSFLLKCLEQVRKIQGDGAALQEKLVSECATYKLCHPEEL VLLGHSLGIPWAPLSSCPSQALQLAGCLSQLHSGLFLYQGLLQALEGISP ELGPTLDTLQLDVADFATTIWQQMEELGMAPALQPTQGAMPAFASAFQRR AGGVLVASHLQSFLEVSYRVLRHLAQP |
| 预测分子量 | 19 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. |
1. **"Recombinant human granulocyte colony-stimulating factor: effects on normal and leukemic myeloid cells"**
*作者：Morstyn G, et al.*
**摘要**：该研究评估了重组人G-CSF在健康志愿者和白血病患者中的安全性与疗效，证实其能显著促进中性粒细胞增殖，缩短化疗后中性粒细胞减少的持续时间。
2. **"Phase I study of recombinant human granulocyte colony-stimulating factor in patients receiving intensive chemotherapy"**
*作者：Bronchud MH, et al.*
**摘要**：首次临床试验表明，重组G-CSF可安全用于接受高剂量化疗的癌症患者，有效减少中性粒细胞减少症的发生率并加速恢复。
3. **"Expression of the human gene encoding granulocyte colony-stimulating factor (G-CSF) in Escherichia coli"**
*作者：Nagata S, et al.*
**摘要**：报道了通过大肠杆菌表达系统高效生产重组人G-CSF的方法，并验证其生物活性与天然蛋白一致，为大规模生产奠定基础。
4. **"Pegylated recombinant human granulocyte colony-stimulating factor (PEG-rhG-CSF): a review of its use in chemotherapy-induced neutropenia"**
*作者：Molineux G.*
**摘要**：探讨聚乙二醇化修饰的长效G-CSF的药代动力学优势，证明其单次给药即可维持疗效，减少化疗患者的注射频率。
**Background of Recombinant G-CSF Protein**
Granulocyte Colony-Stimulating Factor (G-CSF) is a hematopoietic growth factor that regulates the production, differentiation, and survival of neutrophils, a critical type of white blood cell. Naturally produced by endothelial cells, macrophages, and other immune cells, G-CSF binds to specific receptors on myeloid progenitor cells, activating signaling pathways (e.g., JAK/STAT) to stimulate neutrophil proliferation and maturation.
The recombinant form of G-CSF (rG-CSF), first developed in the 1980s, is synthesized using genetic engineering techniques. By inserting the human *CSF3* gene into expression systems like *E. coli* (for non-glycosylated versions, e.g., filgrastim) or mammalian cells (for glycosylated forms, e.g., pegfilgrastim), large-scale production became feasible. This innovation addressed limitations in natural G-CSF availability and purity.
Clinically, rG-CSF is pivotal in managing chemotherapy-induced neutropenia, reducing infection risks by accelerating neutrophil recovery. It also aids in hematopoietic stem cell mobilization for transplantation and treats congenital neutropenia. Pegfilgrastim, a PEGylated variant, offers prolonged activity due to reduced renal clearance, enabling single-dose administration per chemotherapy cycle.
Safety profiles are generally favorable, though mild side effects (bone pain, fever) and rare complications (splenomegaly, capillary leak syndrome) are noted. Ongoing research explores its role in immunomodulation, tissue repair, and combination therapies.
Overall, recombinant G-CSF exemplifies the successful translation of molecular biology into therapeutic applications, significantly improving outcomes in oncology and hematology.
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