纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | ACR |
Uniprot No | P10323 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 20-343aa |
氨基酸序列 | KDNATCDGPCGLRFRQNPQGGVRIVGGKAAQHGAWPWMVSLQIFTYNSHRYHTCGGSLLNSRWVLTAAHCFVGKNNVHDWRLVFGAKEITYGNNKPVKAPLQERYVEKIIIHEKYNSATEGNDIALVEITPPISCGRFIGPGCLPHFKAGLPRGSQSCWVAGWGYIEEKAPRPSSILMEARVDLIDLDLCNSTQWYNGRVQPTNVCAGYPVGKIDTCQGDSGGPLMCKDSKESAYVVVGITSWGVGCARAKRPGIYTATWPYLNWIASKIGSNALRMIQSATPPPPTTRPPPIRPPFSHPISAHLPWYFQPPPRPLPPRPPAAQ |
预测分子量 | 39.3 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ACR重组蛋白的3篇虚构参考文献示例(基于常见研究方向模拟):
1. **文献名称**:*Structural insights into the AcrAB-TolC multidrug efflux pump using recombinant protein expression*
**作者**:Murakami S, et al.
**摘要**:本研究通过重组技术在大肠杆菌中表达并纯化AcrAB-TolC复合物,利用冷冻电镜解析其三维结构,揭示其抗生素外排机制,为克服细菌耐药性提供理论依据。
2. **文献名称**:*Recombinant ACR protein suppresses tumor growth by modulating immune checkpoint pathways*
**作者**:Zhang Y, et al.
**摘要**:通过哺乳动物细胞系统表达重组ACR蛋白,证实其通过抑制PD-1/PD-L1信号通路增强T细胞活性,在黑色素瘤小鼠模型中显著抑制肿瘤进展。
3. **文献名称**:*Functional characterization of a novel ACR recombinant enzyme in environmental toxin degradation*
**作者**:Li H, et al.
**摘要**:从极端微生物中克隆ACR基因,构建重组表达体系,证明该酶可高效降解有机磷农药,为环境污染修复提供潜在生物催化剂。
4. **文献名称**:*Optimization of recombinant ACR production in Pichia pastoris for therapeutic applications*
**作者**:Wang Q, et al.
**摘要**:通过毕赤酵母表达系统优化ACR重组蛋白的分泌表达,提高产量并验证其抗炎活性,为类风湿性关节炎的蛋白药物开发奠定基础。
(注:以上文献为模拟内容,实际研究需查询具体数据库如PubMed、Web of Science。)
**Background of ACR Recombinant Proteins**
ACR (Antibody-Cytokine Recombinant) proteins represent a class of engineered biologics designed to synergize targeted antibody therapy with cytokine-mediated immune modulation. Emerging in the late 1990s, their development was propelled by advances in genetic engineering and immunology, aiming to overcome limitations of traditional cytokine therapies, such as systemic toxicity and short half-life. By fusing cytokines (e.g., interleukins, interferons) to tumor-specific antibodies or antibody fragments, ACR proteins enable localized delivery of immune-stimulating molecules to diseased tissues, enhancing therapeutic precision.
The concept leverages the targeting capability of monoclonal antibodies (mAbs) to direct cytokines to specific microenvironments, such as tumors or inflamed sites. For instance, interleukin-2 (IL-2) or interferon-alpha (IFN-α), when fused to tumor-targeting antibodies, can activate immune cells within the tumor while minimizing off-target effects. Early models, like immunocytokines, demonstrated proof-of-concept in preclinical cancer studies, showing improved efficacy over standalone cytokines or antibodies.
ACR platforms have since expanded to address diverse diseases, including autoimmune disorders and chronic infections. Innovations in protein engineering, such as optimizing linker sequences, modulating cytokine receptor affinity, and incorporating half-life extension domains (e.g., Fc fusion), have refined their stability and activity. Challenges remain, including balancing potency with safety, managing immune-mediated adverse events, and ensuring scalable production. Despite these hurdles, ACR proteins exemplify the convergence of immunotherapy and precision medicine, offering adaptable frameworks for next-generation therapeutics. Ongoing research focuses on combinatorial regimens, personalized designs, and novel cytokine-antibody pairings to unlock broader clinical potential.
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