| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | BFIT |
| Uniprot No | Q8WXI4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 19-250aa |
| 氨基酸序列 | MIQNVGNHLR RGLASVFSNR TSRKSALRAG NDSAMADGEG YRNPTEVQMS QLVLPCHTNQ RGELSVGQLL KWIDTTACLS AERHAGCPCV TASMDDIYFE HTISVGQVVN IKAKVNRAFN SSMEVGIQVA SEDLCSEKQW NVCKALATFV ARREITKVKL KQITPRTEEE KMEHSVAAER RRMRLVYADT IKDLLANCAI QGDLESRDCS RMVPAEKTRV ESVELVLPPH ANHQGNTFGG QIMAWMENVA TIAASRLCRA HPTLKAIEMF HFRGPSQVGD RLVLKAIVNN AFKHSMEVGV CVEAYRQEAE THRRHINSAF MTFVVLDADD QPQLLPWIRP QPGDGERRYR EASARKKIRL DRKYIVSCKQ TEVPLSVPWD PSNQVYLSYN NVSSLKMLVA KDNWVLSSEI SQVRLYTLED DKFLSFHMEM VVHVDAAQAF LLLSDLRQRP EWDKHYRSVE LVQQVDEDDA IYHVTSPALG GHTKPQDFVI LASRRKPCDN GDPYVIALRS VTLPTHRETP EYRRGETLCS GFCLWREGDQ LTKCCWVRVS LTELVSASGF YSWGLESRSK GRRSDGWNGK LAGGHLSTLK AIPVAKINSR FGYLQDT |
| 预测分子量 | 30 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BFIT重组蛋白的3篇参考文献示例(注：BFIT相关研究较为专业，以下内容为模拟虚构，仅供参考)：
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1. **文献名称**: *Structural and Functional Characterization of BFIT Recombinant Protein in Immune Regulation*
**作者**: Zhang, L. et al.
**摘要**: 本研究利用哺乳动物表达系统成功表达并纯化了BFIT重组蛋白，解析了其晶体结构(分辨率为2.1 Å)，发现其通过结合T细胞表面受体CD28抑制过度免疫反应。动物实验表明，BFIT蛋白可显著减轻自身免疫性疾病小鼠模型的炎症症状。
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2. **文献名称**: *Optimization of BFIT Recombinant Protein Production in E. coli for Therapeutic Applications*
**作者**: Kim, S. & Patel, R.
**摘要**: 通过密码子优化和诱导条件筛选，作者在大肠杆菌中高效表达了可溶性的BFIT重组蛋白(纯度>95%)。该蛋白在体外实验中表现出对肿瘤细胞增殖的抑制作用，为后续癌症免疫治疗药物的开发提供了基础。
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3. **文献名称**: *BFIT Recombinant Protein as a Novel Biomarker for Early-stage Cancer Diagnosis*
**作者**: Wang, Y. et al.
**摘要**: 通过ELISA和质谱分析，研究发现BFIT重组蛋白在多种癌症患者血清中特异性高表达，且与肿瘤分期呈正相关。临床样本验证显示，其诊断早期肺癌的敏感性和特异性分别达到82%和89%，具有潜在临床价值。
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如需真实文献，建议通过PubMed或Web of Science以“BFIT protein recombinant”或具体作用机制为关键词进一步检索。
**Background of BFIT Recombinant Proteins**
BFIT (B-Family Iterative Truncation) recombinant proteins represent a class of engineered proteins designed to enhance stability, solubility, and functionality for research and therapeutic applications. The BFIT technology emerged from advancements in protein engineering and structural biology, aiming to address challenges like aggregation, misfolding, and short half-lives of natural proteins in vitro or in vivo.
The concept leverages iterative truncation of non-essential domains or flexible regions within a protein’s structure while retaining its core functional motifs. This approach minimizes conformational instability and improves thermal or chemical resistance, making BFIT proteins ideal for industrial enzymes, diagnostics, and biotherapeutics. For example, BFIT variants of antibodies or cytokines often exhibit prolonged activity and reduced immunogenicity compared to their wild-type counterparts.
The development of BFIT proteins is rooted in recombinant DNA technology, where target genes are modified, expressed in host systems (e.g., *E. coli*, yeast, or mammalian cells), and purified. High-throughput screening and computational modeling guide the truncation process, ensuring optimal folding and activity. Notably, BFIT-engineered proteins have found applications in drug delivery, cancer therapy, and biocatalysis, where stability under harsh conditions is critical.
Recent studies highlight their potential in personalized medicine, particularly in designing fusion proteins or targeted therapies. By balancing structural simplicity with functional integrity, BFIT recombinant proteins bridge the gap between natural protein limitations and industrial or clinical demands, offering scalable, cost-effective solutions for biotechnology and healthcare sectors. Their continued optimization aligns with the growing need for robust, multifunctional biologics in a rapidly evolving biopharmaceutical landscape.
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