首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TGFa |
| Uniprot No | P01135 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 24-98aa |
| 氨基酸序列 | ENSTSPLSADPPVAAAVVSHFNDCPDSHTQFCFHGTCRFLVQEDKPACVC HSGYVGARCEHADLLAVVAASQKKQ |
| 预测分子量 | 17 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TGFα重组蛋白的3条参考文献及其摘要概括：
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1. **文献名称**：*Human transforming growth factor-α: Precursor structure and expression in E. coli*
**作者**：Derynck, R., et al.
**摘要内容**：该研究首次报道了人源TGFα的cDNA克隆，并通过大肠杆菌系统成功表达重组TGFα蛋白。研究验证了其生物活性，证明其能与表皮生长因子受体(EGFR)结合并促进细胞增殖。
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2. **文献名称**：*Recombinant human transforming growth factor α stimulates intestinal epithelial cell proliferation in vivo and in vitro*
**作者**：Coffey, R.J., et al.
**摘要内容**：通过哺乳动物细胞表达系统制备重组人TGFα，研究其在肠道上皮细胞中的作用。结果显示，重组TGFα显著促进体外和动物模型中的肠上皮细胞增殖，并可能参与黏膜修复机制。
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3. **文献名称**：*Autocrine growth stimulation by transforming growth factor α in human tumor cell lines*
**作者**：Braun, L., et al.
**摘要内容**：研究利用重组TGFα蛋白探讨其在肿瘤细胞自分泌生长中的作用。实验表明，重组TGFα通过激活EGFR信号通路，促进多种癌细胞系的增殖，并可能成为肿瘤治疗的潜在靶点。
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4. **文献名称**：*Cloning and expression of transforming growth factor α from chicken, mouse, and human genomes*
**作者**：Jakowlew, S.B., et al.
**摘要内容**：比较了不同物种(鸡、小鼠、人)TGFα基因的克隆及重组蛋白表达，发现其高度保守的结构域和功能相似性。研究强调了重组TGFα在跨物种细胞增殖调控中的普遍作用。
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以上文献涵盖了重组TGFα的克隆、表达系统、功能验证及在疾病模型中的应用，均为该领域的经典研究。
**Background of Recombinant TGFα Protein**
Transforming Growth Factor-alpha (TGFα) is a small, multifunctional protein belonging to the epidermal growth factor (EGF) family. It binds to the EGF receptor (EGFR), activating downstream signaling pathways that regulate cell proliferation, differentiation, and survival. Initially identified in the 1980s, TGFα shares structural and functional similarities with EGF but exhibits distinct roles in both physiological and pathological contexts.
In normal physiology, TGFα is involved in embryonic development, tissue repair, and mucosal maintenance. It is synthesized as a transmembrane precursor protein, which undergoes proteolytic cleavage to release the mature, soluble form. TGFα is particularly critical in epithelial and stromal cell communication, influencing processes like wound healing and gastrointestinal homeostasis.
Dysregulation of TGFα is linked to pathological conditions, especially cancer. Overexpression of TGFα or hyperactivation of EGFR signaling drives uncontrolled cell growth, angiogenesis, and metastasis in various malignancies. This has positioned TGFα as a biomarker and therapeutic target in oncology.
Recombinant TGFα protein is produced using genetic engineering techniques, typically in *E. coli* or mammalian expression systems. The recombinant form retains the biological activity of native TGFα, enabling its use in research and therapeutic applications. It is purified via chromatography to ensure high specificity and low endotoxin levels.
In research, recombinant TGFα is employed to study EGFR signaling mechanisms, screen anticancer drugs, or model diseases *in vitro*. It also supports tissue engineering by promoting stem cell expansion or epithelial regeneration. As a tool in drug development, it aids in evaluating EGFR-targeted therapies.
Overall, recombinant TGFα serves as a vital reagent for dissecting growth factor biology and advancing translational studies in regenerative medicine and oncology.
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