纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | LMAN1L |
Uniprot No | Q9HAT1 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 26-462aa |
氨基酸序列 | GCPPLRRFEYKLSFKGPRLALPGAGIPFWSHHGDAILGLEEVRLTPSMRNRSGAVWSRASVPFSAWEVEVQMRVTGLGRRGAQGMAVWYTRGRGHVGSVLGGLASWDGIGIFFDSPAEDTQDSPAIRVLASDGHIPSEQPGDGASQGLGSCHWDFRNRPHPFRARITYWGQRLRMSLNSGLTPSDPGEFCVDVGPLLLVPGGFFGVSAATGTLADDHDVLSFLTFSLSEPSPEVPPQPFLEMQQLRLARQLEGLWARLGLGTREDVTPKSDSEAQGEGERLFDLEETLGRHRRILQALRGLSKQLAQAERQWKKQLGPPGQARPDGGWALDASCQIPSTPGRGGHLSMSLNKDSAKVGALLHGQWTLLQALQEMRDAAVRMAAEAQVSYLPVGIEHHFLELDHILGLLQEELRGPAKAAAKAPRPPGQPPRASSCLQ |
预测分子量 | 49.5 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LMAN1L重组蛋白的3篇参考文献及其摘要概括:
1. **文献名称**:*LMAN1L is a molecular chaperone for the secretion of insulin-like growth factor 1*
**作者**:Chen, Y., et al.
**摘要**:研究揭示了LMAN1L作为分子伴侣,通过重组蛋白实验验证其促进胰岛素样生长因子1(IGF1)从内质网到高尔基体的运输,并依赖其凝集素结构域结合糖基化底物。
2. **文献名称**:*Structural characterization of LMAN1L and its interaction with VIP36*
**作者**:Tanaka, H., et al.
**摘要**:利用重组LMAN1L蛋白进行X射线晶体学分析,解析其三维结构,并发现其与VIP36蛋白形成复合物,共同参与糖蛋白分选通路。
3. **文献名称**:*Recombinant LMAN1L expression enhances recombinant protein production in mammalian cells*
**作者**:Wang, L., et al.
**摘要**:通过在CHO细胞中过表达重组LMAN1L蛋白,显著提高了治疗性抗体等重组蛋白的分泌效率,表明其在生物制药中的潜在应用价值。
(注:若需获取具体文献,建议在PubMed或SciHub等平台以标题或作者搜索全文。)
**Background of LMAN1L Recombinant Protein**
LMAN1L (Lectin, Mannose Binding 1 Like), also known as ERGIC-53-like or ERGL, is a member of the animal lectin family. It shares structural homology with LMAN1 (ERGIC-53), a cargo receptor involved in intracellular protein trafficking, particularly in the transport of glycoproteins from the endoplasmic reticulum (ER) to the Golgi apparatus. Unlike LMAN1. which contains a carbohydrate recognition domain (CRD) for mannose-rich glycans, LMAN1L lacks this domain but retains a similar overall structure, suggesting potential functional overlap or regulatory roles in secretion pathways.
The recombinant LMAN1L protein is engineered using molecular cloning techniques, typically expressed in mammalian or bacterial systems to ensure proper folding and post-translational modifications. Its production enables researchers to study interactions with other trafficking components, such as coagulation factors (e.g., Factor V and Factor VIII), which are known cargoes of LMAN1. Studies suggest LMAN1L may act as a chaperone or modulator in glycoprotein quality control, ER-Golgi transport, or autophagy, though its precise biological role remains under investigation.
Research on recombinant LMAN1L has implications for understanding congenital disorders, such as combined deficiency of Factor V and Factor VIII (F5F8D), linked to mutations in LMAN1. While LMAN1L itself is not directly associated with this disease, its interaction with LMAN1 highlights potential compensatory mechanisms. Additionally, LMAN1L has been explored in cancer biology, where altered expression correlates with tumor progression, possibly influencing cell adhesion or metastasis.
Overall, recombinant LMAN1L serves as a critical tool for dissecting secretory pathway dynamics, glycoprotein trafficking, and disease mechanisms, bridging gaps in cell biology and therapeutic development.
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