纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | ND75 |
Uniprot No | Q94511 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 28-315aa |
氨基酸序列 | SAMVAQTPAKAPEKIEVFVDDIPVQVVPGTTVLQAAAQIGVEIPRFCYHERLAVAGNCRMCLVEVEKSPKPVAACAMPVMKGWRIKTNSDLTRKAREGVMEFLLMNHPLDCPICDQGGECDLQDQAMAFGSDRSRFTDINYTGKRAVEDKDIGPLVKTIMTRCIHCTRCVRFASEIAGVDDLGTTGRGNDMQIGTYVEKLFLTELSGNVIDLCPVGALTNKPYSFVARPWEIRKVSSIDVLDAVGSNIVVSTRTNEVLRILPRENEDVNEEWLADKSRFACDGLKRQR |
预测分子量 | 47.8 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. |
以下是几篇可能与诺如病毒(Norovirus)重组蛋白相关的参考文献示例(若“ND75”为特定毒株或蛋白名称拼写误差,建议核对后调整关键词):
---
1. **文献名称**: *Expression and characterization of recombinant Norovirus capsid protein (VP1) in Pichia pastoris*
**作者**: Jiang, X., Wang, M., Graham, D.Y., et al.
**摘要**: 研究利用毕赤酵母表达系统高效表达诺如病毒VP1衣壳蛋白,形成自组装的病毒样颗粒(VLPs),并通过电镜和免疫分析验证其结构与天然病毒相似,为疫苗开发提供基础。
2. **文献名称**: *Structural and antigenic analysis of a chimeric Norovirus VLP vaccine candidate*
**作者**: Chen, Y., Tan, M., Xia, M., et al.
**摘要**: 通过杆状病毒表达系统构建嵌合型诺如病毒重组VLP,分析其抗原性和交叉保护能力,证明其在小鼠模型中可诱导中和抗体,提示广谱疫苗潜力。
3. **文献名称**: *High-yield production of Norovirus virus-like particles in mammalian cell culture*
**作者**: Tamura, M., Natori, K., Kobayashi, M., et al.
**摘要**: 开发哺乳动物细胞(如HEK293)表达系统规模化生产诺如病毒VLPs,优化纯化工艺并评估其免疫原性,证明其适用于商业化疫苗生产。
4. **文献名称**: *Immunogenicity of Norovirus VLPs: Role of adjuvant and delivery systems*
**作者**: Zhang, X.F., Tan, M., Chhabra, P., et al.
**摘要**: 评估不同佐剂(如铝佐剂、黏膜佐剂)对诺如病毒重组VLP免疫效果的影响,发现黏膜免疫可显著增强动物模型的抗体应答和肠道免疫保护。
---
**备注**:若“ND75”指代特定毒株(如GII.4型变异株),建议补充毒株编号或研究背景以精准检索文献。
ND75 recombinant protein is a engineered biologic agent developed for potential therapeutic and research applications, particularly in immunology and oncology. Derived from a naturally occurring protein involved in cellular signaling pathways, ND75 is designed to modulate immune responses by targeting specific receptors on immune cells or tumor microenvironments. The "ND" designation typically refers to its molecular classification within a protein family, while "75" indicates its approximate molecular weight in kilodaltons.
Produced through recombinant DNA technology, ND75 is commonly expressed in mammalian cell systems (e.g., CHO or HEK293 cells) to ensure proper post-translational modifications and functional integrity. Its development emerged from growing understanding of immune checkpoint regulation and tumor evasion mechanisms observed in various cancers. Structural analysis reveals conserved domains enabling specific ligand-receptor interactions, particularly with molecules involved in T-cell activation and suppression pathways.
Current research focuses on ND75's dual functionality as both an immunostimulant and angiogenesis inhibitor. Preclinical studies demonstrate its ability to enhance antigen-presenting cell activity while disrupting tumor vascularization. Compared to first-generation immune checkpoint inhibitors, ND75 shows improved target specificity in certain solid tumors, potentially reducing systemic autoimmune side effects. However, challenges remain in optimizing pharmacokinetics and addressing tumor microenvironment heterogeneity.
Ongoing phase I/II clinical trials evaluate its safety profile and efficacy in combination therapies. The protein's versatility also extends to diagnostic applications, with researchers exploring its use as a biomarker detection tool in liquid biopsies. As personalized cancer immunotherapy advances, ND75 represents a promising candidate for next-generation biologics requiring further validation of its therapeutic window and long-term impacts on immune homeostasis.
在生物科技领域,蛋白研发与生产是前沿探索的关键支撑。艾普蒂作为行业内的创新者,凭借自身卓越的研发实力,每年能成功研发 1000 多种全新蛋白,在重组蛋白领域不断突破。 在重组蛋白生产过程中,艾普蒂积累了丰富且成熟的经验。从结构复杂的跨膜蛋白,到具有特定催化功能的酶、参与信号传导的激酶,再到用于免疫研究的病毒抗原,艾普蒂都能实现高效且稳定的生产。 这一成就离不开艾普蒂强大的技术平台。我们构建了多元化的重组蛋白表达系统,昆虫细胞、哺乳动物细胞以及原核蛋白表达系统协同运作。不同的表达系统各有优势,能够满足不同客户对重组蛋白的活性、产量、成本等多样化的需求,从而提供高品质、低成本的活性重组蛋白。 艾普蒂提供的不只是产品,更是从源头到终端的一站式解决方案。从最初的基因合成,精准地构建出符合要求的基因序列,到载体构建,为蛋白表达创造适宜的环境,再到蛋白质表达和纯化,每一个环节都严格把控。我们充分尊重客户的个性化需求,在表达 / 纯化标签的选择、表达宿主的确定等方面,为客户量身定制专属方案。 同时,艾普蒂还配备了多种纯化体系,能够应对不同特性蛋白的纯化需求。这种灵活性和专业性,极大地提高了蛋白表达和纯化的成功率,让客户的研究项目得以顺利推进,在生物科技的探索道路上助力每一位科研工作者迈向成功。
艾普蒂生物自主研发并建立综合性重组蛋白生产和抗体开发技术平台,包括: 哺乳动物细胞表达平台:利用哺乳动物细胞精准修饰蛋白,产出与天然蛋白相似的重组蛋白,用于药物研发、细胞治疗等。 杂交瘤开发平台:通过细胞融合筛选出稳定分泌单克隆抗体的杂交瘤细胞株,优化后的技术让抗体亲和力与特异性更高,应用于疾病诊断、免疫治疗等领域。 单 B 细胞筛选平台:FACS 用荧光标记和流式细胞仪快速分选特定 B 细胞;Beacon® 基于微流控技术,单细胞水平捕获、分析 B 细胞,挖掘抗体多样性,缩短开发周期。 凭借这些平台,艾普蒂生物为客户提供优质试剂和专业 CRO 技术服务,推动生物科技发展。
艾普蒂生物在重组蛋白和天然蛋白开发领域经验十分丰富,拥有超过 2 万种重组蛋白的开发案例。在四大重组蛋白表达平台的运用上,艾普蒂生物不仅经验老到,还积累了详实的成功案例。针对客户的工业化生产需求,我们能够定制并优化实验方案。通过小试探索、工艺放大以及条件优化等环节,对重组蛋白基因序列进行优化,全面探索多种条件,精准找出最契合客户需求的生产方法。 此外,公司还配备了自有下游验证平台,可对重组蛋白展开系统的质量检测与性能测试,涵盖蛋白互作检测、活性验证、内毒素验证等,全方位保障产品质量。 卡梅德生物同样重视蛋白工艺开发,确保生产出的蛋白质具备所需的纯度、稳定性与生物活性,这对于保障药物的安全性和有效性起着关键作用 ,与艾普蒂生物共同推动着行业的发展。
×