| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ITGA5 |
| Uniprot No | P08648 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 42-995aa |
| 氨基酸序列 | FNLDAEAPAVLSGPPGSFFGFSVEFYRPGTDGVSVLVGAPKANTSQPGVL QGGAVYLCPWGASPTQCTPIEFDSKGSRLLESSLSSSEGEEPVEYKSLQW FGATVRAHGSSILACAPLYSWRTEKEPLSDPVGTCYLSTDNFTRILEYAP CRSDFSWAAGQGYCQGGFSAEFTKTGRVVLGGPGSYFWQGQILSATQEQI AESYYPEYLINLVQGQLQTRQASSIYDDSYLGYSVAVGEFSGDDTEDFVA GVPKGNLTYGYVTILNGSDIRSLYNFSGEQMASYFGYAVAATDVNGDGLD DLLVGAPLLMDRTPDGRPQEVGRVYVYLQHPAGIEPTPTLTLTGHDEFGR FGSSLTPLGDLDQDGYNDVAIGAPFGGETQQGVVFVFPGGPGGLGSKPSQ VLQPLWAASHTPDFFGSALRGGRDLDGNGYPDLIVGSFGVDKAVVYRGRP IVSASASLTIFPAMFNPEERSCSLEGNPVACINLSFCLNASGKHVADSIG FTVELQLDWQKQKGGVRRALFLASRQATLTQTLLIQNGAREDCREMKIYL RNESEFRDKLSPIHIALNFSLDPQAPVDSHGLRPALHYQSKSRIEDKAQI LLDCGEDNICVPDLQLEVFGEQNHVYLGDKNALNLTFHAQNVGEGGAYEA ELRVTAPPEAEYSGLVRHPGNFSSLSCDYFAVNQSRLLVCDLGNPMKAGA SLWGGLRFTVPHLRDTKKTIQFDFQILSKNLNNSQSDVVSFRLSVEAQAQ VTLNGVSKPEAVLFPVSDWHPRDQPQKEEDLGPAVHHVYELINQGPSSIS QGVLELSCPQALEGQQLLYVTRVTGLNCTTNHPINPKGLELDPEGSLHHQ QKREAPSRSSASSGPQILKCPEAECFRLRCELGPLHQQESQSLQLHFRVW AKTFLQREHQPFSLQCEAVYKALKMPYRILPRQLPQKERQVATAVQWTKA EGSYVDHHHHHH |
| 预测分子量 | 105 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ITGA5重组蛋白的模拟参考文献示例(非真实文献，仅供格式参考)：
1. **文献名称**：*Expression and Functional Characterization of Recombinant Human ITGA5 in Mammalian Cells*
**作者**：Smith J, et al.
**摘要**：本研究在HEK293细胞中成功表达并纯化了具有生物活性的ITGA5重组蛋白，优化了表达条件以提高产量，并通过细胞粘附实验证实其与纤连蛋白(FN1)的特异性结合能力。
2. **文献名称**：*ITGA5 Recombinant Protein Promotes Tumor Cell Migration via FAK Signaling Pathway*
**作者**：Zhang L, et al.
**摘要**：通过体外实验证明，重组ITGA5蛋白可显著增强乳腺癌细胞的迁移能力，并激活黏着斑激酶(FAK)信号通路，提示其在癌症转移中的潜在作用。
3. **文献名称**：*Structural Insights into ITGA5-Fibronectin Interaction Using Cryo-EM*
**作者**：Jones R, et al.
**摘要**：利用冷冻电镜技术解析了ITGA5重组蛋白与纤连蛋白RGD结构域的复合物结构，揭示了其结合界面的关键氨基酸残基，为靶向药物设计提供依据。
4. **文献名称**：*High-Throughput Screening of ITGA5 Inhibitors Using Recombinant Protein-Based Assays*
**作者**：Lee H, et al.
**摘要**：开发了一种基于ITGA5重组蛋白的高通量筛选平台，鉴定出多个小分子抑制剂，可有效阻断ITGA5/β1整合素介导的细胞黏附，具有抗纤维化治疗潜力。
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如需真实文献，建议通过PubMed或Google Scholar检索关键词：“ITGA5 recombinant protein”、“integrin alpha 5 expression”等。
ITGA5 (Integrin Alpha-5) is a critical subunit of the heterodimeric transmembrane receptor integrin α5β1. which plays a pivotal role in mediating cell-extracellular matrix (ECM) interactions. As part of the integrin family, ITGA5 pairs exclusively with the β1 subunit to form the α5β1 integrin, also known as the fibronectin receptor. This receptor primarily binds to fibronectin through its Arg-Gly-Asp (RGD) motif, facilitating cell adhesion, migration, and signaling processes essential for embryonic development, tissue repair, angiogenesis, and cancer metastasis. Dysregulation of ITGA5 expression or function is associated with pathological conditions, including fibrosis, inflammation, and tumor progression.
Recombinant ITGA5 protein is engineered for in vitro studies to dissect its biological roles and therapeutic potential. Produced using expression systems like mammalian cells or insect cells, the recombinant protein typically includes the extracellular domain of ITGA5. preserving its ligand-binding capacity while excluding transmembrane and cytoplasmic regions for solubility. Purification tags (e.g., His, Fc) are often added to facilitate isolation and detection. Researchers utilize recombinant ITGA5 to investigate integrin-mediated signaling pathways, screen for inhibitory compounds, or develop targeted therapies. In cancer research, blocking ITGA5-ECM interactions may suppress metastasis, while in regenerative medicine, enhancing its activity could promote wound healing. Its structural and functional versatility makes it a valuable tool for both basic and applied biomedical studies.
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