| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | MYOC |
| Uniprot No | Q99972 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 33-504aa |
| 氨基酸序列 | RTAQLRKA NDQSGRCQYT FSVASPNESS CPEQSQAMSV IHNLQRDSST QRLDLEATKA RLSSLESLLH QLTLDQAARP QETQEGLQRE LGTLRRERDQ LETQTRELET AYSNLLRDKS VLEEEKKRLR QENENLARRL ESSSQEVARL RRGQCPQTRD TARAVPPGSR EVSTWNLDTL AFQELKSELT EVPASRILKE SPSGYLRSGE GDTGCGELVW VGEPLTLRTA ETITGKYGVW MRDPKPTYPY TQETTWRIDT VGTDVRQVFE YDLISQFMQG YPSKVHILPR PLESTGAVVY SGSLYFQGAE SRTVIRYELN TETVKAEKEI PGAGYHGQFP YSWGGYTDID LAVDEAGLWV IYSTDEAKGA IVLSKLNPEN LELEQTWETN IRKQSVANAF IICGTLYTVS SYTSADATVN FAYDTGTGIS KTLTIPFKNR YKYSSMIDYN PLEKKLFAWD NLNMVTYDIK LSKM |
| 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. |
以下是关于MYOC重组蛋白的3篇参考文献概览：
1. **文献名称**: "Expression and purification of recombinant human myocilin"
**作者**: Clark AF, et al.
**摘要**: 该研究建立了高效表达和纯化重组人MYOC蛋白的方法，利用哺乳动物细胞系统进行分泌表达，纯化后的蛋白用于结构分析和抗体生成，为后续功能研究奠定基础。
2. **文献名称**: "Aggregation properties of recombinant myocilin mutants in glaucoma"
**作者**: Joe MK, et al.
**摘要**: 文章通过比较野生型与青光眼相关突变型重组MYOC的聚集特性，发现突变体在细胞内异常聚集并引发内质网应激，揭示了MYOC突变导致青光眼的潜在分子机制。
3. **文献名称**: "Interaction of recombinant myocilin with extracellular matrix components"
**作者**: Filla MS, et al.
**摘要**: 研究利用重组MYOC蛋白分析其与纤连蛋白、胶原IV等细胞外基质成分的相互作用，发现MYOC可能通过调控细胞黏附参与小梁网功能，提示其在房水流出通路中的作用。
*注：以上文献为示例性质，实际文献需通过学术数据库检索确认。建议使用PubMed/Google Scholar以关键词“recombinant myocilin”或“MYOC expression”查找最新研究。*
MYOC (myocilin) is a secreted glycoprotein encoded by the MYOC gene, first identified in 1997 through genetic linkage studies in families with primary open-angle glaucoma (POAG), a leading cause of irreversible blindness. Predominantly expressed in ocular tissues, particularly the trabecular meshwork (TM) and ciliary body, MYOC is implicated in regulating intraocular pressure (IOP) by influencing aqueous humor outflow. Structurally, it contains an N-terminal coiled-coil domain, facilitating protein-protein interactions, and a C-terminal olfactomedin-like domain, which harbors most glaucoma-associated mutations (e.g., Pro370Leu).
While MYOC’s precise physiological role remains unclear, studies suggest involvement in cell adhesion, cytoskeletal organization, and extracellular matrix remodeling. Over 70 MYOC mutations are linked to POAG, often causing protein misfolding and aggregation within the endoplasmic reticulum (ER) of TM cells. This triggers ER stress, aberrant autophagy, and TM dysfunction, ultimately elevating IOP and damaging the optic nerve.
Recombinant MYOC proteins, produced via bacterial (e.g., E. coli) or mammalian (e.g., HEK293) expression systems, are critical tools for studying these mechanisms. Bacterial systems yield non-glycosylated proteins suitable for structural analyses, while mammalian-expressed MYOC mimics native post-translational modifications. Recombinant MYOC enables in vitro studies on mutation-induced aggregation, stress pathways, and interactions with extracellular components (e.g., fibronectin). It also aids in drug screening for compounds that stabilize MYOC or enhance its secretion, offering therapeutic potential. Challenges include optimizing solubility and stability due to aggregation tendencies. Current research focuses on elucidating MYOC’s native function, mutation-specific pathogenicity, and gene therapy strategies to mitigate its toxic effects in glaucoma.
×
