纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | DNAL1 |
Uniprot No | Q4LDG9 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-190aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMAKATTI KEALARWEEK TGQRPSEAKE IKLYAQIPPI EKMDASLSML ANCEKLSLST NCIEKIANLN GLKNLRILSL GRNNIKNLNG LEAVGDTLEE LWISYNFIEK LKGIHIMKKL KILYMSNNLV KDWAEFVKLA ELPCLEDLVF VGNPLEEKHS AENNWIEEAT KRVPKLKKLD GTPVIKGDEE EDN |
预测分子量 | 24 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DNAL1重组蛋白的3篇参考文献概览:
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1. **文献名称**: *Characterization of DNAL1 as a ciliary dynein assembly factor in human cells*
**作者**: Smith A, et al.
**摘要**: 本研究通过重组表达人源DNAL1蛋白,验证其与动力蛋白复合体的相互作用,发现DNAL1缺失导致纤毛内动力蛋白组装异常,提示其在纤毛运动功能中的关键调控作用。
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2. **文献名称**: *Recombinant DNAL1 protein rescues motility defects in zebrafish dnal1 mutants*
**作者**: Chen L, et al.
**摘要**: 利用重组DNAL1蛋白在斑马鱼模型中进行功能回补实验,证明外源DNAL1能恢复突变体胚胎的纤毛运动能力,并通过体外结合实验揭示其与Dynein重链的特定结构域相互作用。
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3. **文献名称**: *Expression and purification of human DNAL1 for structural analysis*
**作者**: Gupta R, et al.
**摘要**: 报道了基于大肠杆菌系统的高效重组DNAL1蛋白表达与纯化方案,结合X射线晶体学初步解析其三维结构,为研究其分子机制提供基础。
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注:以上文献为模拟示例,实际研究中建议通过PubMed或Web of Science以关键词“DNAL1 recombinant”检索最新文献。
DNAL1 (Dynein Axonemal Light Chain 1) is a protein component of the dynein motor complex, primarily associated with ciliary and flagellar structures in eukaryotic cells. As a member of the light chain family within axonemal dyneins, it plays a critical role in regulating microtubule-based motility. The protein is encoded by the *DNAL1* gene and is evolutionarily conserved across species, underscoring its functional importance in cellular locomotion and structural organization.
Recombinant DNAL1 protein is produced via heterologous expression systems (e.g., *E. coli* or mammalian cells) for experimental studies. Structurally, it contains conserved domains that facilitate interactions with heavy chain dyneins and other regulatory subunits, enabling ATP-dependent mechanochemical activity. Its function extends beyond motility; DNAL1 is implicated in ciliogenesis, intracellular transport, and maintenance of ciliary architecture. Defects in DNAL1 or its associated pathways are linked to ciliopathies, such as primary ciliary dyskinesia (PCD), characterized by impaired mucociliary clearance and recurrent respiratory infections.
Research on recombinant DNAL1 focuses on elucidating its role in dynein assembly, force transmission, and ciliary beating patterns. It also serves as a tool to study mutations causing ciliary dysfunction, aiding in diagnostic marker development or therapeutic targeting. Additionally, recombinant DNAL1 has applications in structural biology (e.g., cryo-EM studies) to map dynein complex interactions. Its study bridges fundamental cell biology with clinical insights into genetic disorders tied to ciliary defects.
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