| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RAB23 |
| Uniprot No | Q9ULC3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-234aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MLEEDMEVAI KMVVVGNGAV GKSSMIQRYC KGIFTKDYKK TIGVDFLERQ IQVNDEDVRL MLWDTAGQEE FDAITKAYYR GAQACVLVFS TTDRESFEAV SSWREKVVAE VGDIPTVLVQ NKIDLLDDSC IKNEEAEALA KRLKLRFYRT SVKEDLNVNE VFKYLAEKYL QKLKQQIAED PELTHSSSNK IGVFNTSGGS HSGQNSGTLN GGDVINLRPN KQRTKKNRNP FSSC |
| 预测分子量 | 29 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. **"Rab23 regulates Hedgehog signaling by controlling the distribution of Smoothened"**
*作者：Eggenschwiler, J.T., et al.*
摘要：研究揭示了RAB23在小鼠Hedgehog信号通路中的调控作用，通过重组蛋白实验证实其通过影响Smoothened蛋白的细胞内定位来抑制信号传导，与胚胎发育异常相关。
2. **"Rab23’s role in hepatocellular carcinoma progression through MAPK pathway modulation"**
*作者：Chi, S., et al.*
摘要：利用重组RAB23蛋白分析其在肝癌细胞中的功能，发现其过表达通过激活MAPK信号通路促进肿瘤侵袭，提示其作为潜在治疗靶点。
3. **"Recombinant Rab23 GTPase: Purification and characterization of its interaction with transport vesicles"**
*作者：Lodhi, I.J., et al.*
摘要：描述了RAB23重组蛋白的体外纯化方法及生化特性，证明其通过GTP结合状态调控囊泡运输，为膜运输机制研究提供工具。
4. **"Rab23 mutations in Carpenter syndrome disrupt neural tube patterning"**
*作者：Chen, W., et al.*
摘要：通过构建突变型RAB23重组蛋白，发现其功能缺失导致神经管发育缺陷，关联于Carpenter综合征，强调了其在细胞极性建立中的作用。
RAB23 is a member of the Ras-associated binding (RAB) family of small GTPases, which play critical roles in regulating intracellular vesicle trafficking, membrane dynamics, and organelle organization. Discovered in 1994. RAB23 is evolutionarily conserved and ubiquitously expressed in mammalian tissues. As a GTPase, it cycles between an active GTP-bound state and an inactive GDP-bound state, acting as a molecular switch to coordinate cargo transport and membrane fusion events. Structurally, RAB23 contains conserved GTP-binding domains and a hypervariable C-terminal region that directs its subcellular localization.
Functionally, RAB23 is best known for its role in regulating sonic hedgehog (SHH) signaling, a pathway essential for embryonic development, particularly in neural tube patterning and limb formation. Studies in mice revealed that RAB23 acts as a negative regulator of SHH signaling, with loss-of-function mutations leading to severe developmental defects. Additionally, RAB23 is implicated in autophagy, endosomal sorting, and ciliogenesis, processes linked to cellular homeostasis and disease.
Dysregulation of RAB23 is associated with human pathologies. Recessive mutations in RAB23 cause Carpenter syndrome, a rare genetic disorder characterized by craniofacial abnormalities, polydactyly, and obesity. Conversely, overexpression of RAB23 has been observed in certain cancers, including gliomas and breast cancer, where it may influence tumor progression through interactions with oncogenic pathways.
Recombinant RAB23 protein, typically produced in bacterial or mammalian expression systems, retains GTPase activity and post-translational modifications (e.g., prenylation) when purified. It serves as a vital tool for biochemical studies, including GTP-binding assays, interaction partner identification (e.g., with DISP1 or other trafficking mediators), and screening for small-molecule modulators. Its applications extend to structural studies using X-ray crystallography or cryo-EM to elucidate mechanistic details of RAB23-mediated membrane trafficking. Current research continues to explore its context-dependent roles in development, cancer, and metabolic disorders.
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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