| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ADAM9 |
| Uniprot No | Q13443 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 29-697aa |
| 氨基酸序列 | AARPGFQQTSHLSSYEIITPWRLTRERREAPRPYSKQVSYVIQAEGKEHIIHLERNKDLLPEDFVVYTYNKEGTLITDHPNIQNHCHYRGYVEGVHNSSIALSDCFGLRGLLHLENASYGIEPLQNSSHFEHIIYRMDDVYKEPLKCGVSNKDIEKETAKDEEEEPPSMTQLLRRRRAVLPQTRYVELFIVVDKERYDMMGRNQTAVREEMILLANYLDSMYIMLNIRIVLVGLEIWTNGNLINIVGGAGDVLGNFVQWREKFLITRRRHDSAQLVLKKGFGGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGRDCSCGAKSCIMNSGASGSRNFSSCSAEDFEKLTLNKGGNCLLNIPKPDEAYSAPSCGNKLVDAGEECDCGTPKECELDPCCEGSTCKLKSFAECAYGDCCKDCRFLPGGTLCRGKTSECDVPEYCNGSSQFCQPDVFIQNGYPCQNNKAYCYNGMCQYYDAQCQVIFGSKAKAAPKDCFIEVNSKGDRFGNCGFSGNEYKKCATGNALCGKLQCENVQEIPVFGIVPAIIQTPSRGTKCWGVDFQLGSDVPDPGMVNEGTKCGAGKICRNFQCVDASVLNYDCDVQKKCHGHGVCNSNKNCHCENGWAPPNCETKGYGGSVDSGPTYNEMNTALRD |
| 预测分子量 | 75.3 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ADAM9重组蛋白的3篇参考文献示例(注：内容为模拟概括，建议通过学术数据库核实最新文献)：
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1. **文献名称**：*"Recombinant expression and functional characterization of ADAM9 in cancer cell invasion"*
**作者**：Smith J, et al.
**摘要**：研究通过哺乳动物表达系统成功获得ADAM9重组蛋白，证实其在肿瘤细胞迁移和侵袭中通过降解细胞外基质蛋白(如纤连蛋白)促进转移。
2. **文献名称**：*"Structural insights into ADAM9 protease domain via recombinant protein crystallography"*
**作者**：Li H, Wang Y.
**摘要**：报道ADAM9催化结构域的重组表达与纯化，通过X射线晶体学解析其三维结构，揭示底物结合位点特征，为抑制剂设计提供依据。
3. **文献名称**：*"ADAM9 interacts with integrin β1 in endothelial cells: Role in angiogenesis studied via recombinant protein assays"*
**作者**：Garcia-Rojas P, et al.
**摘要**：利用重组ADAM9蛋白进行体外结合实验，发现其与整合素β1直接互作，调控血管内皮细胞黏附和血管生成过程。
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建议通过PubMed或Google Scholar搜索关键词“ADAM9 recombinant protein”获取最新实证研究。
ADAM9 (A Disintegrin And Metalloproteinase 9) is a member of the ADAM family of transmembrane proteins, which are characterized by their dual roles in cell adhesion and proteolytic processing. As a multidomain protein, ADAM9 consists of a prodomain, metalloproteinase domain, disintegrin domain, cysteine-rich region, transmembrane domain, and cytoplasmic tail. This structural complexity enables its involvement in diverse cellular processes, including cell signaling, migration, and extracellular matrix remodeling. Recombinant ADAM9 proteins are engineered to study its biochemical functions, therapeutic potential, and pathological roles in diseases such as cancer, inflammation, and neurodegenerative disorders.
In physiological contexts, ADAM9 regulates cell-cell and cell-matrix interactions by cleaving substrates like growth factors (e.g., HB-EGF) and adhesion molecules (e.g., E-cadherin). However, its dysregulation is linked to pathological conditions. Overexpression of ADAM9 in cancers (e.g., prostate, breast, pancreatic) correlates with tumor progression, metastasis, and drug resistance, partly through activation of oncogenic pathways like EGFR and Notch. In neurodegenerative diseases, aberrant ADAM9 activity may contribute to amyloid precursor protein processing, influencing Alzheimer’s pathology.
Recombinant ADAM9 is typically produced in mammalian or insect expression systems to ensure proper post-translational modifications and functional activity. These proteins are utilized to investigate substrate specificity, develop inhibitory antibodies or small molecules, and model disease mechanisms. Tagged versions (e.g., His, Fc, or FLAG tags) facilitate purification and detection in assays. Structural studies of recombinant ADAM9 domains, particularly the catalytic metalloproteinase region, provide insights into inhibitor design. Despite challenges in maintaining its native conformation *in vitro*, recombinant ADAM9 remains a critical tool for unraveling its dual roles in health and disease.
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