| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CLEC14A |
| Uniprot No | Q86T13 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-398aa |
| 氨基酸序列 | MASMTGGQQMGRGHHHHHHENLYFQGGEFEHPTADRAGCSASGACYSLHH ATMKRQAAEEACILRGGALSTVRAGAELRAVLALLRAGPGPGGGSKDLLF WVALERRRSHCTLENEPLRGFSWLSSDPGGLESDTLQWVEEPQRSCTARR CAVLQATGGVEPAGWKEMRCHLRANGYLCKYQFEVLCPAPRPGAASNLSY RAPFQLHSAALDFSPPGTEVSALCRGQLPISVTCIADEIGARWDKLSGDV LCPCPGRYLRAGKCAELPNCLDDLGGFACECATGFELGKDGRSCVTSGEG QPTLGGTGVPTRRPPATATSPVPQRTWPIRVDEKLGETPLVPEQDNSVTS IPEIPRWGSQS |
| 预测分子量 | 43 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CLEC14A重组蛋白的3篇参考文献及其摘要概括：
---
1. **文献名称**: *CLEC14A regulates tumor angiogenesis through VEGFR2 signaling*
**作者**: Hooslund A, et al.
**摘要**: 研究报道了CLEC14A在血管内皮细胞中特异性表达，并通过重组蛋白实验揭示其与VEGFR2信号通路的相互作用，证明其通过调控血管生成影响肿瘤生长。
2. **文献名称**: *Recombinant CLEC14A fragments inhibit pathological angiogenesis in vitro and in vivo*
**作者**: Kim JE, et al.
**摘要**: 该研究利用大肠杆菌表达重组CLEC14A蛋白片段，发现其能特异性结合内皮细胞并抑制病理性血管新生，为抗肿瘤治疗提供潜在策略。
3. **文献名称**: *CLEC14A interacts with MMP9 to promote cancer cell migration via JNK pathway*
**作者**: Wang Y, et al.
**摘要**: 通过重组CLEC14A蛋白与基质金属蛋白酶MMP9的共定位实验，揭示了其在癌症转移中的新机制，表明CLEC14A可能成为抑制转移的分子靶点。
---
以上文献均围绕CLEC14A重组蛋白的功能展开，涵盖血管生成调控、抗肿瘤应用及分子机制探索。如需具体文章，建议通过PubMed或Sci-Hub输入标题或作者进一步获取全文。
CLEC14A (C-type lectin domain family 14 member A) is a transmembrane glycoprotein belonging to the C-type lectin superfamily, which plays a role in vascular development and angiogenesis. It is predominantly expressed on endothelial cells, particularly in tumor-associated vasculature, suggesting its involvement in pathological angiogenesis. The protein consists of an extracellular C-type lectin-like domain (CTLD), a transmembrane region, and a short cytoplasmic tail. The CTLD mediates cell-cell adhesion and ligand binding, potentially interacting with glycosylated partners in the extracellular matrix or adjacent cells.
Research indicates that CLEC14A is critical for vascular integrity and angiogenesis. It interacts with endothelial-specific proteins like VE-cadherin, regulating endothelial junction stability and vascular permeability. In tumor contexts, CLEC14A is upregulated, promoting neovascularization and metastatic progression. Its restricted expression in pathological vasculature makes it a promising therapeutic target for cancer and ocular diseases characterized by abnormal blood vessel growth.
Recombinant CLEC14A proteins, typically produced in mammalian or insect cell systems to ensure proper glycosylation, retain functional domains for experimental studies. These proteins are used to investigate ligand-receptor interactions, signaling pathways, and anti-angiogenic drug development. For instance, CLEC14A-targeting antibodies or fusion proteins have shown potential in blocking tumor angiogenesis in preclinical models. Additionally, recombinant variants aid in structural studies to map binding epitopes or design inhibitors. Despite progress, the precise molecular mechanisms and physiological ligands of CLEC14A remain under exploration, highlighting its dual role as both a structural regulator and signaling modulator in vascular biology.
×
