纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | ITGa3 |
Uniprot No | P26006 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-1051aa |
氨基酸序列 | MGPGPSRAPRAPRLMLCALALMVAAGGCVVSAFNLDTRFLVVKEAGNPGSLFGYSVALHRQTERQQRYLLLAGAPRELAVPDGYTNRTGAVYLCPLTAHKDDCERMNITVKNDPGHHIIEDMWLGVTVASQGPAGRVLVCAHRYTQVLWSGSEDQRRMVGKCYVRGNDLELDSSDDWQTYHNEMCNSNTDYLETGMCQLGTSGGFTQNTVYFGAPGAYNWKGNSYMIQRKEWDLSEYSYKDPEDQGNLYIGYTMQVGSFILHPKNITIVTGAPRHRHMGAVFLLSQEAGGDLRRRQVLEGSQVGAYFGSAIALADLNNDGWQDLLVGAPYYFERKEEVGGAIYVFMNQAGTSFPAHPSLLLHGPSGSAFGLSVASIGDINQDGFQDIAVGAPFEGLGKVYIYHSSSKGLLRQPQQVIHGEKLGLPGLATFGYSLSGQMDVDENFYPDLLVGSLSDHIVLLRARPVINIVHKTLVPRPAVLDPALCTATSCVQVELCFAYNQSAGNPNYRRNITLAYTLEADRDRRPPRLRFAGSESAVFHGFFSMPEMRCQKLELLLMDNLRDKLRPIIISMNYSLPLRMPDRPRLGLRSLDAYPILNQAQALENHTEVQFQKECGPDNKCESNLQMRAAFVSEQQQKLSRLQYSRDVRKLLLSINVTNTRTSERSGEDAHEALLTLVVPPALLLSSVRPPGACQANETIFCELGNPFKRNQRMELLIAFEVIGVTLHTRDLQVQLQLSTSSHQDNLWPMILTLLVDYTLQTSLSMVNHRLQSFFGGTVMGESGMKTVEDVGSPLKYEFQVGPMGEGLVGLGTLVLGLEWPYEVSNGKWLLYPTEITVHGNGSWPCRPPGDLINPLNLTLSDPGDRPSSPQRRRRQLDPGGGQGPPPVTLAAAKKAKSETVLTCATGRAHCVWLECPIPDAPVVTNVTVKARVWNSTFIEDYRDFDRVRVNGWATLFLRTSIPTINMENKTTWFSVDIDSELVEELPAEIELWLVLVAVGAGLLLLGLIILLLWKCGFFKRARTRALYEAKRQKAEMKSQPSETERLTDDY |
预测分子量 | 116,6 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ITGa3重组蛋白的3篇参考文献示例(注:以下内容为示例性概括,具体文献需通过学术数据库核实):
1. **文献名称**: "Expression and Functional Characterization of Recombinant Integrin α3β1 in Mammalian Cells"
**作者**: Smith J, et al.
**摘要**: 该研究描述了在HEK293细胞中重组表达ITGa3(整合素α3β1异源二聚体)的方法,并验证其与层粘连蛋白-5的结合活性,证实重组蛋白在细胞粘附实验中的功能作用。
2. **文献名称**: "Structural Insights into ITGa3 Extracellular Domain by Cryo-EM Using Recombinant Protein"
**作者**: Li X, et al.
**摘要**: 通过冷冻电镜解析重组ITGa3胞外域的结构,揭示其与配体相互作用的分子机制,为靶向ITGa3的药物设计提供结构基础。
3. **文献名称**: "Role of Recombinant ITGa3 in Cancer Cell Invasion and Metastasis"
**作者**: Tanaka M, et al.
**摘要**: 利用重组ITGa3蛋白进行体外实验,证明其通过激活FAK信号通路促进肿瘤细胞侵袭,提示ITGa3在癌症转移中的潜在治疗靶点价值。
建议通过PubMed或Google Scholar以关键词“ITGa3 recombinant protein”或“integrin alpha 3 recombinant expression”检索最新文献以获取准确信息。
**Background of ITGa3 Recombinant Protein**
Integrin alpha-3 (ITGa3) is a subunit of the α3β1 heterodimeric transmembrane receptor, part of the integrin family involved in cell-cell and cell-extracellular matrix (ECM) interactions. ITGa3 pairs with the β1 subunit (ITGB1) to form a receptor that primarily binds laminin, fibronectin, and other ECM components, mediating cellular adhesion, migration, and signaling. This protein plays critical roles in tissue development, wound healing, and epithelial integrity.
The *ITGA3* gene, located on chromosome 17 in humans, encodes a protein with a large extracellular domain, a transmembrane region, and a short cytoplasmic tail. Dysregulation of ITGa3 is linked to pathological conditions, including cancer metastasis, chronic inflammation, and skin disorders like epidermolysis bullosa. Its involvement in tumor progression, particularly in modulating invasion and angiogenesis, has made it a focus in oncology research.
Recombinant ITGa3 protein is engineered using mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications, such as glycosylation, which are essential for ligand-binding activity. Purification typically involves affinity chromatography, yielding high-purity, functional protein.
In research, recombinant ITGa3 is utilized to study integrin-mediated signaling pathways, screen therapeutic agents targeting integrin-associated diseases, or develop biomaterials for regenerative medicine. Its applications extend to elucidating mechanisms of cell-ECM interactions in physiological and disease contexts, offering insights for novel therapeutic strategies.
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