| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TIEG1 |
| Uniprot No | Q13118 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-480aa |
| 氨基酸序列 | MLNFGASLQQ TAEERMEMIS ERPKESMYSW NKTAEKSDFE AVEALMSMSC SWKSDFKKYV ENRPVTPVSD LSEEENLLPG TPDFHTIPAF CLTPPYSPSD FEPSQVSNLM APAPSTVHFK SLSDTAKPHI AAPFKEEEKS PVSAPKLPKA QATSVIRHTA DAQLCNHQTC PMKAASILNY QNNSFRRRTH LNVEAARKNI PCAAVSPNRS KCERNTVADV DEKASAALYD FSVPSSETVI CRSQPAPVSP QQKSVLVSPP AVSAGGVPPM PVICQMVPLP ANNPVVTTVV PSTPPSQPPA VCPPVVFMGT QVPKGAVMFV VPQPVVQSSK PPVVSPNGTR LSPIAPAPGF SPSAAKVTPQ IDSSRIRSHI CSHPGCGKTY FKSSHLKAHT RTHTGEKPFS CSWKGCERRF ARSDELSRHR RTHTGEKKFA CPMCDRRFMR SDHLTKHARR HLSAKKLPNW QMEVSKLNDI ALPPTPAPTQ |
| 预测分子量 | 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TIEG1重组蛋白的参考文献示例，涵盖其功能机制及疾病相关研究：
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1. **文献名称**：*TIEG1 Recombinant Protein Modulates TGF-β Signaling in Pancreatic Cancer Cells*
**作者**：Zhang L, et al.
**摘要**：该研究通过大肠杆菌表达系统制备了重组TIEG1蛋白，并证明其可增强胰腺癌细胞中TGF-β/Smad通路的活性，抑制癌细胞增殖并诱导凋亡，提示其在靶向治疗中的潜在应用。
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2. **文献名称**：*Structural and Functional Characterization of TIEG1 KRAB Domain via Recombinant Protein Expression*
**作者**：Johnson RB, et al.
**摘要**：作者解析了TIEG1重组蛋白的KRAB结构域晶体结构，发现其通过与染色质修饰酶相互作用抑制靶基因转录，为设计调控TIEG1活性的小分子奠定基础。
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3. **文献名称**：*Recombinant TIEG1 Attenuates Renal Fibrosis by Suppressing EMT in Diabetic Nephropathy Models*
**作者**：Wang Y, et al.
**摘要**：研究利用腺病毒递送重组TIEG1蛋白至糖尿病肾病小鼠，结果显示其通过抑制上皮-间质转化(EMT)减轻肾纤维化，机制涉及下调Fibronectin和α-SMA表达。
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4. **文献名称**：*TIEG1 Recombinant Protein Enhances Osteogenic Differentiation via BMP-2 Pathway Activation*
**作者**：Chen H, et al.
**摘要**：实验证明重组TIEG1蛋白通过激活BMP-2信号通路促进间充质干细胞的成骨分化，为骨再生治疗提供了新策略。
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注：上述文献为示例性质，实际引用时需核实真实出版物信息。建议通过PubMed或Google Scholar以“TIEG1 recombinant protein”为关键词检索最新研究。
TIEG1 (TGF-β Inducible Early Gene-1), also known as KLF10 (Kruppel-like factor 10), is a transcription factor belonging to the Sp1/KLF family. It was first identified in 1995 as an early-response gene induced by TGF-β signaling in osteoblasts. Structurally, TIEG1 contains three C-terminal C2H2 zinc finger domains for DNA binding and N-terminal repression domains that recruit co-regulators. It functions primarily as a transcriptional repressor, regulating genes involved in cell differentiation, apoptosis, and extracellular matrix remodeling.
TIEG1 plays critical roles in bone metabolism, immune regulation, and cellular responses to growth factors. Studies highlight its importance in osteoblast/osteoclast differentiation, BMP/TGF-β signaling pathways, and maintaining skeletal homeostasis. Dysregulation of TIEG1 is linked to pathologies such as osteoporosis, cancer metastasis, cardiovascular diseases, and fibrosis. For instance, reduced TIEG1 expression correlates with impaired osteoblast function, while its overexpression suppresses tumor cell proliferation.
Recombinant TIEG1 protein, typically produced in *E. coli* or mammalian expression systems, retains the functional domains required for DNA binding and protein interactions. It is purified using affinity tags (e.g., His-tag) and validated for activity through electrophoretic mobility shift assays (EMSAs) or luciferase reporter assays. Researchers use recombinant TIEG1 to study its molecular mechanisms, screen for interacting partners, or modulate target gene expression in cell cultures.
Its therapeutic potential is being explored, particularly in bone disorders and diseases driven by TGF-β pathway imbalances. However, challenges remain in delivering functional TIEG1 protein *in vivo* due to stability and tissue-targeting limitations. Current research focuses on optimizing its structure-activity relationships and developing TIEG1-based gene therapies.
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