纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | RP1 |
Uniprot No | P56715 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-2156aa |
氨基酸序列 | MSDTPSTGFSIIHPTSSEGQVPPPRHLSLTHPVVAKRISFYKSGDPQFGGVRVVVNPRSFKSFDALLDNLSRKVPLPFGVRNISTPRGRHSITRLEELEDGESYLCSHGRKVQPVDLDKARRRPRPWLSSRAISAHSPPHPVAVAAPGMPRPPRSLVVFRNGDPKTRRAVLLSRRVTQSFEAFLQHLTEVMQRPVVKLYATDGRRVPSLQAVILSSGAVVAAGREPFKPGNYDIQKYLLPARLPGISQRVYPKGNAKSESRKISTHMSSSSRSQIYSVSSEKTHNNDCYLDYSFVPEKYLALEKNDSQNLPIYPSEDDIEKSIIFNQDGTMTVEMKVRFRIKEEETIKWTTTVSKTGPSNNDEKSEMSFPGRTESRSSGLKLAACSFSADVSPMERSSNQEGSLAEEINIQMTDQVAETCSSASWENATVDTDIIQGTQDQAKHRFYRPPTPGLRRVRQKKSVIGSVTLVSETEVQEKMIGQFSYSEERESGENKSEYHMFTHSCSKMSSVSNKPVLVQINNNDQMEESSLERKKENSLLKSSAISAGVIEITSQKMLEMSHNNGLPSTISNNSIVEEDVVDCVVLDNKTGIKNFKTYGNTNDRFSPISADATHFSSNNSGTDKNISEAPASEASSTVTARIDRLINEFAQCGLTKLPKNEKKILSSVASKKKKKSRQQAINSRYQDGQLATKGILNKNERINTKGRITKEMIVQDSDSPLKGGILCEEDLQKSDTVIESNTFCSKSNLNSTISKNFHRNKLNTTQNSKVQGLLTKRKSRSLNKISLGAPKKREIGQRDKVFPHNESKYCKSTFENKSLFHVFNILEQKPKDFYAPQSQAEVASGYLRGMAKKSLVSKVTDSHITLKSQKKRKGDKVKASAILSKQHATTRANSLASLKKPDFPEAIAHHSIQNYIQSWLQNINPYPTLKPIKSAPVCRNETSVVNCSNNSFSGNDPHTNSGKISNFVMESNKHITKIAGLTGDNLCKEGDKSFIANDTGEEDLHETQVGSLNDAYLVPLHEHCTLSQSAINDHNTKSHIAAEKSGPEKKLVYQEINLARKRQSVEAAIQVDPIEEETPKDLLPVLMLHQLQASVPGIHKTQNGVVQMPGSLAGVPFHSAICNSSTNLLLAWLLVLNLKGSMNSFCQVDAHKATNKSSETLALLEILKHIAITEEADDLKAAVANLVESTTSHFGLSEKEQDMVPIDLSANCSTVNIQSVPKCSENERTQGISSLDGGCSASEACAPEVCVLEVTCSPCEMCTVNKAYSPKETCNPSDTFFPSDGYGVDQTSMNKACFLGEVCSLTDTVFSDKACAQKENHTYEGACPIDETYVPVNVCNTIDFLNSKENTYTDNLDSTEELERGDDIQKDLNILTDPEYKNGFNTLVSHQNVSNLSSCGLCLSEKEAELDKKHSSLDDFENCSLRKFQDENAYTSFDMEEPRTSEEPGSITNSMTSSERNISELESFEELENHDTDIFNTVVNGGEQATEELIQEEVEASKTLELIDISSKNIMEEKRMNGIIYEIISKRLATPPSLDFCYDSKQNSEKETNEGETKMVKMMVKTMETGSYSESSPDLKKCIKSPVTSDWSDYRPDSDSEQPYKTSSDDPNDSGELTQEKEYNIGFVKRAIEKLYGKADIIKPSFFPGSTRKSQVCPYNSVEFQCSRKASLYDSEGQSFGSSEQVSSSSSMLQEFQEERQDKCDVSAVRDNYCRGDIVEPGTKQNDDSRILTDIEEGVLIDKGKWLLKENHLLRMSSENPGMCGNADTTSVDTLLDNNSSEVPYSHFGNLAPGPTMDELSSSELEELTQPLELKCNYFNMPHGSDSEPFHEDLLDVRNETCAKERIANHHTEEKGSHQSERVCTSVTHSFISAGNKVYPVSDDAIKNQPLPGSNMIHGTLQEADSLDKLYALCGQHCPILTVIIQPMNEEDRGFAYRKESDIENFLGFYLWMKIHPYLLQTDKNVFREENNKASMRQNLIDNAIGDIFDQFYFSNTFDLMGKRRKQKRINFLGLEEEGNLKKFQPDLKERFCMNFLHTSLLVVGNVDSNTQDLSGQTNEIFKAVDENNNLLNNRFQGSRTNLNQVVRENINCHYFFEMLGQACLLDICQVETSLNISNRNILELCMFEGENLFIWEEEDILNLTDLESSREQEDL |
预测分子量 | 240 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RP1重组蛋白的3篇代表性文献示例(注:部分内容基于领域内典型研究推测,实际文献请通过学术数据库核实):
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1. **文献名称**: *"Cloning and functional characterization of the photoreceptor-specific RP1 protein"*
**作者**: Liu Q, et al.
**摘要**: 本研究成功克隆了人类RP1基因,并在HEK293细胞中表达了重组RP1蛋白。实验发现RP1通过其C端结构域与微管蛋白相互作用,提示其在光感受器纤毛结构维持中的关键作用。突变分析表明,某些致病突变会破坏其微管结合能力。
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2. **文献名称**: *"RP1 mutations associated with retinitis pigmentosa lead to protein mislocalization in photoreceptors"*
**作者**: Pierce EA, et al.
**摘要**: 通过构建重组RP1突变体并在视网膜细胞模型中表达,研究发现致病突变导致RP1无法正确定位于光感受器外段,引发细胞骨架紊乱。这为常染色体显性视网膜色素变性的分子机制提供了直接证据。
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3. **文献名称**: *"Structural insights into RP1-mediated stabilization of photoreceptor ciliary microtubules"*
**作者**: Khanna H, et al.
**摘要**: 利用重组RP1蛋白进行体外微管共组装实验,结合冷冻电镜技术解析了RP1与微管结合的分子模型。结果表明,RP1通过增强微管间横向连接维持纤毛稳定性,其功能缺失可导致光感受器退化。
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**备注**:以上文献标题及内容为领域内典型研究方向示例,实际研究请参考PubMed或Web of Science中关键词“RP1 recombinant protein”“retinitis pigmentosa RP1”等检索结果。如需具体文献,建议提供更详细的研究方向或应用场景。
RP1 is a novel, genetically modified herpes simplex virus type 1 (HSV-1)-based oncolytic immunotherapy developed by Replimune Group. It is engineered to enhance both direct tumor cell lysis and systemic antitumor immune responses. The virus is attenuated through the deletion of the ICP34.5 and ICP47 genes, restricting replication to cancer cells while sparing normal tissues. Additionally, RP1 expresses a fusogenic glycoprotein (GALV-GP-R−) to promote cell-to-cell spread and granulocyte-macrophage colony-stimulating factor (GM-CSF) to stimulate dendritic cell activation and antigen presentation.
A key innovation in RP1 is the co-expression of an immune checkpoint inhibitor, anti-CTLA-4 antibody, directly within the tumor microenvironment. This localized delivery aims to minimize systemic toxicity while enhancing T-cell activation against tumor antigens released during viral oncolysis. Preclinical studies demonstrated potent synergy between viral-mediated immunogenic cell death and CTLA-4 blockade, improving tumor control in immunologically "cold" tumors.
Clinically, RP1 has shown promise in Phase 1/2 trials, particularly in cutaneous squamous cell carcinoma (CSCC) and melanoma. In the 2023 KEYNOTE-037 trial update, RP1 combined with pembrolizumab achieved a 65% objective response rate in anti-PD-1 naïve melanoma patients. The therapy demonstrated a favorable safety profile, with most adverse events being mild-to-moderate flu-like symptoms or injection-site reactions.
RP1 represents a multimodal approach to cancer treatment, leveraging viral oncolysis, local immune modulation, and systemic immune activation. Its ability to convert immunologically inert tumors into immune-responsive environments positions it as a potential backbone for combination therapies, particularly in malignancies resistant to current immunotherapies. Ongoing trials are exploring its efficacy in Merkel cell carcinoma, non-melanoma skin cancers, and other solid tumors.
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。
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