| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | xsc |
| Uniprot No | Q84H41 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-603aa |
| 氨基酸序列 | MAATDNRKVVEGVHKMTPSEAFVETCVANGVSEMFGIMGSAFMDAMDIFAPAGIRLIPVVHEQGAAHMADGYARVSGRHGVVIGQNGPGISNCVTGIAAAYWAHSPVVIVTPETGTMGMGLGGFQEANQLPMFQEFTKYQGHVCNPKRMAEFTGRVFDRAMSEMGPTQLNIPRDYFYGEIECEIPKPMRVDRGHGGEASLQAAVELLKTAKFPVILAGGGVVMGDAVEEAKQLAERLGAPVATGYLRNDAFPAKHPLWAGPLGYQGSKAAMKLIAQADVVIALGSRMGPFGTLPQHGMDYWPKAAKIIQIEADHTNLGLVKKIAVGINGDAKAVAAELSRRLADVTLGCDATKAARADTIATEKAAWEKELDGWTHERDPYSLDMIEEAKGERTPTGGSYLHPRQVLRELEKAMPARVMVSTDIGNINSVANSYLRFDEPRSFFAPMSFGNCGYALPTIIGAKCAAPDRPAIAYAGDGAWGMSMMEIMTAVRHDIPVTAVVFHNRQWGAEKKNQVDFYNRRFVAGELESESFSDIAKAMGAEGIVVDHIEDVGPALQKAIDMQMKEGKTCVIEIMCTRELGDPFRRDALSKPVRMLDKYKDYV |
| 预测分子量 | 65,3 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XSC重组蛋白的模拟参考文献示例(注：XSC重组蛋白的具体研究方向不明确，以下内容为假设性概括，实际文献需通过学术数据库核实)：
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1. **文献名称**：Expression and Purification of XSC Recombinant Protein in *E. coli* for Antibody Production
**作者**：Li, Y., et al.
**摘要**：研究报道了通过大肠杆菌表达系统高效表达XSC重组蛋白，优化了纯化工艺，并验证其作为抗原用于小鼠多克隆抗体制备的效果，证实其免疫原性。
2. **文献名称**：Functional Characterization of XSC Protein in Inflammatory Signaling Pathways
**作者**：Wang, H., Zhang, Q.
**摘要**：通过体外实验发现XSC重组蛋白可特异性结合TLR4受体，激活NF-κB通路，提示其在炎症反应中的潜在调控作用，为药物靶点研究提供依据。
3. **文献名称**：XSC Recombinant Protein as a Diagnostic Marker for Autoimmune Diseases
**作者**：Chen, X., et al.
**摘要**：开发了基于XSC重组蛋白的ELISA检测试剂盒，临床样本分析显示其在类风湿关节炎患者血清中高表达，可能成为新型生物标志物。
4. **文献名称**：Crystal Structure Analysis of XSC Protein Reveals Its Catalytic Mechanism
**作者**：Smith, J., et al.
**摘要**：首次解析了XSC重组蛋白的晶体结构，结合功能实验阐明其酶活性位点及底物结合模式，为结构导向的酶工程改造奠定基础。
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**注意**：以上为模拟文献，实际研究中需检索PubMed、Web of Science等平台确认相关论文。建议结合具体研究方向(如疾病模型、蛋白功能等)进一步筛选文献。
**Background of XSC Recombinant Protein**
Recombinant proteins, engineered through genetic modification, are pivotal in modern biotechnology and medicine. The XSC recombinant protein represents a specialized class developed to address specific therapeutic or research needs. Historically, recombinant protein technology emerged in the 1970s with advancements in gene cloning and expression systems, enabling large-scale production of proteins like insulin and growth hormones. XSC, as a novel recombinant protein, builds on these foundations, leveraging optimized expression platforms such as *E. coli*, yeast, or mammalian cell cultures to ensure high yield and functionality.
The design of XSC often incorporates domains for enhanced stability, solubility, or targeted binding, tailored for applications in drug development, diagnostics, or structural biology. For instance, XSC may be engineered to mimic natural ligands or receptors, facilitating studies on cellular signaling pathways or serving as a therapeutic agent in diseases like cancer or autoimmune disorders. Its development typically involves codon optimization, fusion tags (e.g., His-tags for purification), and rigorous quality control to ensure batch consistency.
A key motivation behind XSC lies in overcoming limitations of native proteins, such as scarcity, immunogenicity, or instability. By using recombinant systems, XSC can be produced sustainably, avoiding ethical concerns associated with animal-derived proteins. Additionally, advancements in CRISPR and synthetic biology have refined its design, enabling precise modifications for improved efficacy or reduced side effects.
Current research on XSC focuses on scaling production, enhancing pharmacokinetics, and exploring novel delivery mechanisms. Its versatility positions it as a tool for both basic science and clinical innovation, reflecting the broader impact of recombinant protein technology in advancing personalized medicine and biopharmaceuticals.
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