| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ARL13B |
| Uniprot No | Q3SXY8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-428aa |
| 氨基酸序列 | MFSLMASCCG WFKRWREPVR KVTLLMVGLD NAGKTATAKG IQGEYPEDVA PTVGFSKINL RQGKFEVTIF DLGGGIRIRG IWKNYYAESY GVIFVVDSSD EERMEETKEA MSEMLRHPRI SGKPILVLAN KQDKEGALGE ADVIECLSLE KLVNEHKCLC QIEPCSAISG YGKKIDKSIK KGLYWLLHVI ARDFDALNER IQKETTEQRA LEEQEKQERA ERVRKLREER KQNEQEQAEL DGTSGLAELD PEPTNPFQPI ASVIIENEGK LEREKKNQKM EKDSDGCHLK HKMEHEQIET QGQVNHNGQK NNEFGLVENY KEALTQQLKN EDETDRPSLE SANGKKKTKK LRMKRNHRVE PLNIDDCAPE SPTPPPPPPP VGWGTPKVTR LPKLEPLGET HHNDFYRKPL PPLAVPQRPN SDAHDVIS |
| 分子量 | 48.6 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 冻干粉 |
| 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. **"ARL13B in cilia formation and function"** by Caspary T. et al. (2007)
研究揭示ARL13B突变导致纤毛结构异常，影响Hedgehog信号通路，与Joubert综合征等纤毛病相关，提示其在纤毛发育中的关键作用。
2. **"ARL13B regulates ciliary signaling and neuronal development"** by Duldulao N.A. et al. (2009)
通过斑马鱼模型发现，ARL13B通过调控纤毛膜蛋白定位(如SSTR3)，影响神经管发育及信号传导，缺失引发脑结构异常。
3. **"ARL13B mediates cargo transport in ciliogenesis"** by Higginbotham H. et al. (2012)
提出ARL13B通过结合INPP5E等磷酸酶，调控纤毛膜脂质组成，促进蛋白质运输，缺陷导致纤毛功能失调和疾病。
4. **"Structural insights into ARL13B function in cilia"** by Mariman M. et al. (2020)
通过冷冻电镜解析ARL13B结构，揭示其GTPase结构域与效应蛋白互作机制，为突变相关疾病的分子机制提供新视角。
建议通过PubMed或Google Scholar搜索上述标题获取原文。
ARL13B (ADP-ribosylation factor-like protein 13B) is a small GTPase belonging to the Arf/Arl family, which plays a critical role in regulating cilia structure, function, and signaling. Predominantly localized to primary cilia, it is essential for embryonic development, particularly in neural tube formation and organogenesis. ARL13B facilitates ciliary membrane shaping, protein trafficking, and Hedgehog (Hh) signaling by interacting with other ciliary proteins, such as INPP5E, to maintain lipid composition and signaling pathways. Mutations in ARL13B are linked to ciliopathies, including Joubert syndrome and Meckel-Gruber syndrome, characterized by neurological defects, renal abnormalities, and developmental delays.
Recombinant human ARL13B is engineered for in vitro studies to dissect its molecular mechanisms, ciliary dynamics, and disease-associated dysfunction. Its GTPase activity, regulatory domains (e.g., the C-terminal α-helix), and post-translational modifications (e.g., palmitoylation) are key research focuses. Recombinant forms enable biochemical assays, structural studies, and screening for therapeutic targets. Notably, ARL13B's role in cilia-dependent signaling pathways underscores its potential relevance in cancer and neurodevelopmental disorders. Studies using recombinant ARL13B have advanced insights into cilia biology, offering a tool to model diseases and test interventions targeting ciliary trafficking or signaling defects.
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