| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TLL1 |
| Uniprot No | O43897-2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-392aa |
| 氨基酸序列 | MGLGTLSPRMLVWLVASGIVFYGELWVCAGLDYDYTFDGNEEDKTETIDY KDPCKAAVFWGDIALDDEDLNIFQIDRTIDLTQNPFGNLGHTTGGLGDHA MSKKRGALYQLIDRIRRIGFGLEQNNTVKGKVPLQFSGQNEKNRVPRAAT SRTERIWPGGVIPYVIGGNFTGSQRAMFKQAMRHWEKHTCVTFIERSDEE SYIVFTYRPCGCCSYVGRRGNGPQAISIGKNCDKFGIVVHELGHVIGFWH EHTRPDRDNHVTIIRENIQPGQEYNFLKMEPGEVNSLGERYDFDSIMHYA RNTFSRGMFLDTILPSRDDNGIRPAIGQRTRLSKGDIAQARKLYRCPACG ETLQESNGNLSSPGFPNGYPSYTHCIWRVSVTPGEKVVFSLC |
| 预测分子量 | 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3篇涉及TLL1(Tolloid-like 1)重组蛋白研究的文献摘要信息：
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1. **文献名称**：*"Recombinant expression and functional analysis of human TLL1 in extracellular matrix remodeling"*
**作者**：Smith A, et al.
**摘要**：研究报道了人源TLL1重组蛋白在大肠杆菌中的表达与纯化，验证其金属蛋白酶活性，并证明其能切割细胞外基质蛋白如原纤维蛋白，调节TGF-β信号通路。
2. **文献名称**：*"TLL1-mediated proteolytic activation of pro-BMP1 in zebrafish development"*
**作者**：Chen L, et al.
**摘要**：通过重组TLL1蛋白体外实验，揭示了TLL1在斑马鱼胚胎发育中激活前体BMP1(骨形态发生蛋白1)的分子机制，表明其对组织形态发生的关键作用。
3. **文献名称**：*"Characterization of TLL1 as a potential therapeutic target in fibrosis"*
**作者**：Garcia-Reyes B, et al.
**摘要**：研究利用重组TLL1蛋白分析其在纤维化模型中的作用，发现抑制TLL1活性可减少胶原沉积，提示其作为抗纤维化治疗靶点的潜力。
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注：以上文献信息为示例性质，实际文献需通过PubMed或学术数据库检索确认。若需具体文献链接或DOI，请提供更详细的关键词或年份范围。
Tolloid-like protein 1 (TLL1) is a member of the tolloid-like family of metalloproteases, which belong to the astacin subfamily of zinc-dependent endopeptidases. Initially identified through homology with the Drosophila tolloid gene, TLL1 plays critical roles in extracellular matrix (ECM) remodeling and tissue morphogenesis by modulating key signaling pathways, particularly the bone morphogenetic protein (BMP) and transforming growth factor-beta (TGF-β) pathways. It functions as a type I transmembrane protein or can be processed into a soluble form, exerting enzymatic activity to cleave specific substrates, including pro-collagen C-propeptides and latent BMP-binding proteins, thereby regulating collagen fibrillogenesis and BMP bioavailability.
TLL1 is essential during embryonic development, particularly in cardiovascular and skeletal systems. Studies in animal models have demonstrated its involvement in heart valve formation, septal development, and bone mineralization. Dysregulation of TLL1 has been implicated in human pathologies such as fibrosis, cardiomyopathy, and connective tissue disorders. For instance, elevated TLL1 expression correlates with excessive collagen deposition in fibrotic tissues, while genetic variants are linked to Marfan syndrome and other ECM-related diseases.
Recombinant TLL1 protein is produced using heterologous expression systems (e.g., mammalian or insect cells) to ensure proper post-translational modifications. This engineered protein retains enzymatic activity, enabling its use in mechanistic studies, drug screening, and therapeutic exploration. Researchers employ recombinant TLL1 to investigate its substrate specificity, regulatory mechanisms in ECM dynamics, and potential as a biomarker or therapeutic target in fibrosis and cardiovascular diseases. Its role in modulating BMP signaling also makes it relevant for regenerative medicine applications.
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