首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IL-2 |
| Uniprot No | P60568 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-153aa |
| 氨基酸序列 | APTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVIVLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT |
| 预测分子量 | 41.5 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3篇关于IL-2重组蛋白的经典文献概览：
---
1. **文献名称**：*Molecular cloning and expression of cDNAs for human interleukin-2*
**作者**：Smith KA, et al.
**摘要**：该研究首次报道了通过重组DNA技术克隆并表达人类IL-2基因，证实其能够激活T细胞增殖，为后续IL-2的临床应用奠定基础。
---
2. **文献名称**：*Interleukin-2 and adoptive immunotherapy of malignancies*
**作者**：Rosenberg SA, et al.
**摘要**：探讨重组IL-2在肿瘤免疫治疗中的作用，证明其通过激活细胞毒性T细胞和NK细胞抑制肿瘤生长，但高剂量可能引发严重毒性反应。
---
3. **文献名称**：*Engineering IL-2 to give new life to T cell immunotherapy*
**作者**：Arenas-Ramirez N, et al.
**摘要**：通过突变IL-2蛋白结构(如减少CD25结合)，设计出选择性激活效应T细胞而非调节性T细胞的工程化IL-2变体，降低毒性并增强抗肿瘤效果。
---
4. **文献名称**：*Selective targeting of engineered T cells using orthogonal IL-2 cytokine-receptor complexes*
**作者**：Sockolosky JT, et al.
**摘要**：开发了一种正交IL-2(orthoIL-2)系统，通过改造IL-2及其受体，实现仅对特定工程化T细胞的精准激活，避免全身性副作用。
---
这些文献覆盖了IL-2重组蛋白的基础研究、治疗应用及工程化改进方向。
Interleukin-2 (IL-2) is a cytokine first identified in 1976 as a T-cell growth factor, playing a pivotal role in regulating immune responses. Produced primarily by activated CD4+ T cells, IL-2 binds to receptors (IL-2R) composed of α (CD25), β (CD122), and γ (CD132) subunits, triggering signaling pathways that drive T cell proliferation, differentiation, and survival. It also modulates natural killer (NK) cells and regulatory T cells (Tregs), balancing immune activation and tolerance.
Recombinant IL-2. developed via genetic engineering in the 1980s, enabled large-scale production for clinical use. Early versions, like Proleukin® (aldesleukin), are nonglycosylated proteins expressed in *E. coli*, differing slightly from native human IL-2 by amino acid substitutions (e.g., cysteine-to-serine) to enhance stability. Mammalian cell-derived variants retain glycosylation but are less common due to higher production costs.
Clinically, high-dose IL-2 was FDA-approved in 1992 and 1998 for metastatic renal cell carcinoma and melanoma, leveraging its ability to amplify cytotoxic T and NK cells. However, severe toxicity—capillary leak syndrome, hypotension—limited its utility. Research shifted to engineered IL-2 analogs with biased signaling, such as "selective" IL-2 variants binding preferentially to intermediate-affinity βγ receptors (on effector cells) over high-affinity αβγ receptors (on Tregs), aiming to enhance antitumor efficacy while sparing toxicity. Examples include Bempegaldesleukin (NKTR-214) and THOR-707.
Beyond oncology, IL-2 therapies are explored for autoimmune diseases and transplant rejection by boosting Treg activity. Despite challenges, IL-2 remains a cornerstone in immunotherapy, illustrating the duality of cytokine biology and the potential of protein engineering to refine therapeutic outcomes.
×
