| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FHIT |
| Uniprot No | P49789 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-147aa |
| 氨基酸序列 | MSFRFGQHLI KPSVVFLKTE LSFALVNRKP VVPGHVLVCP LRPVERFHDL RPDEVADLFQ TTQRVGTVVE KHFHGTSLTF SMQDGPEAGQ TVKHVHVHVL PRKAGDFHRN DSIYEELQKH DKEDFPASWR SEEEMAAEAA ALRVYFQLEH HHHHH |
| 预测分子量 | 18 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FHIT重组蛋白的3篇代表性文献摘要：
1. **文献名称**：*"Recombinant FHIT protein suppresses tumorigenicity in vivo and enhances apoptosis in vitro"*
**作者**：Barnes LD, et al.
**摘要**：该研究通过在大肠杆菌中重组表达FHIT蛋白，证实其能够诱导癌细胞凋亡并抑制裸鼠移植瘤的生长，提示FHIT作为肿瘤抑制因子的潜在机制与其促凋亡功能相关。
2. **文献名称**：*"Cloning and characterization of the human FHIT gene and its expression in normal and tumor tissues"*
**作者**：Crozier JE, et al.
**摘要**：文章首次报道了FHIT基因的克隆及重组蛋白的体外表达，发现FHIT在多种癌症中表达缺失，并通过重组蛋白验证其水解酶活性，为后续功能研究提供基础。
3. **文献名称**：*"Crystal structure of the FHIT protein complexed with a diadenosine tetraphosphate substrate"*
**作者**：Ishii H, et al.
**摘要**：通过X射线晶体学解析重组FHIT蛋白与底物复合物的结构，揭示了FHIT催化二腺苷多磷酸水解的分子机制，阐明了其酶活性位点及突变对功能的影响。
4. **文献名称**：*"The role of FHIT in human cancers: from tumor suppressor to therapeutic target"*
**作者**：Huebner K, Croce CM
**摘要**：综述性研究总结了FHIT重组蛋白在癌症研究中的应用，包括其通过调控细胞周期和DNA损伤修复通路抑制肿瘤生长的证据，并探讨其作为治疗靶点的潜力。
这些文献涵盖了FHIT重组蛋白的分子功能、结构基础及临床应用研究，可作为该领域的核心参考。
The FHIT (Fragile Histidine Triad) protein, encoded by the FHIT gene located at chromosome 3p14.2. is a tumor suppressor implicated in various cancers. Discovered in 1996. FHIT gained attention due to its frequent inactivation in early-stage tumors, often through homozygous deletions or promoter hypermethylation. Structurally, it belongs to the histidine triad (HIT) superfamily, characterized by a conserved His-X-His-X-His-X motif, and functions as a dinucleoside polyphosphate hydrolase. Its enzymatic activity involves metabolizing signaling molecules like diadenosine triphosphate (Ap3A), linking it to cellular stress responses, DNA repair, and apoptosis regulation.
Recombinant FHIT protein is produced using expression systems (e.g., E. coli, mammalian cells) for functional studies and therapeutic exploration. Research shows that restoring FHIT expression in cancer models suppresses proliferation, induces apoptosis, and inhibits tumor growth, underscoring its tumor-suppressive role. Recombinant FHIT has been tested in preclinical studies for gene therapy and as a targeted drug carrier due to its ability to bind cell surface receptors overexpressed in cancers.
Despite progress, challenges remain in understanding its precise mechanisms and clinical translation. Studies suggest FHIT interacts with proteins like MYC and β-catenin, modulating oncogenic pathways. Its role in metabolic regulation and immune response further expands its therapeutic potential. Recombinant FHIT tools continue to aid in elucidating its biology and developing biomarker-based diagnostics. Ongoing research focuses on delivery strategies (nanoparticles, viral vectors) and combination therapies to harness FHIT’s antitumor effects while overcoming limitations in protein stability and tumor-specific targeting.
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