| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GSPT1 |
| Uniprot No | P15170 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-499aa |
| 氨基酸序列 | MELSEPIVENGETEMSPEESWEHKEEISEAEPGGGSLGDGRPPEESAHEMMEEEEEIPKPKSVVAPPGAPKKEHVNVVFIGHVDAGKSTIGGQIMYLTGMVDKRTLEKYEREAKEKNRETWYLSWALDTNQEERDKGKTVEVGRAYFETEKKHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFETGFEKGGQTREHAMLAKTAGVKHLIVLINKMDDPTVNWSNERYEECKEKLVPFLKKVGFNPKKDIHFMPCSGLTGANLKEQSDFCPWYIGLPFIPYLDNLPNFNRSVDGPIRLPIVDKYKDMGTVVLGKLESGSICKGQQLVMMPNKHNVEVLGILSDDVETDTVAPGENLKIRLKGIEEEEILPGFILCDPNNLCHSGRTFDAQIVIIEHKSIICPGYNAVLHIHTCIEEVEITALICLVDKKSGEKSKTRPRFVKQDQVCIARLRTAGTICLETFKDFPQMGRFTLRDEGKTIAIGKVLKLVPEKD |
| 预测分子量 | 59.8 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GSPT1重组蛋白的虚构参考文献示例(内容基于常见研究方向模拟，非真实文献)：
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1. **文献名称**：Structural Insights into Human GSPT1 Protein and Its Role in Translation Termination
**作者**：T. Nakamura et al.
**摘要**：本研究通过冷冻电镜解析了人源GSPT1重组蛋白的晶体结构，揭示了其与真核释放因子eRF3的相互作用机制，证明GSPT1通过调控翻译终止复合物的构象变化影响蛋白质合成效率，为靶向GSPT1的药物设计提供结构基础。
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2. **文献名称**：GSPT1 Degradation as a Therapeutic Strategy in Myeloid Leukemia
**作者**：L. Zhang et al.
**摘要**：文章报道了利用重组GSPT1蛋白筛选小分子降解剂(如CC-90009)，通过CRISPR-Cas9验证GSPT1缺失可选择性诱导AML细胞凋亡，证实GSPT1是髓系恶性肿瘤的潜在治疗靶点。
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3. **文献名称**：Functional Characterization of GSPT1 Mutants in Drug-Resistant Cancers
**作者**：M. Gupta & R. Schmidt
**摘要**：通过表达不同突变体重组GSPT1蛋白，发现C-terminal结构域的点突变(如R632L)可导致蛋白稳定性改变，并降低靶向降解药物的敏感性，揭示了临床耐药性的分子机制。
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4. **文献名称**：Yeast-Based Assay for High-Throughput Screening of GSPT1 Inhibitors
**作者**：K. Park et al.
**摘要**：开发基于重组GSPT1蛋白的酵母生长抑制模型，用于高通量筛选靶向GSPT1的化合物，成功鉴定出多个可阻断GSPT1-eRF1相互作用的新型抑制剂。
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注：以上文献为示例性内容，实际研究中建议通过PubMed或Google Scholar检索真实文献(关键词：GSPT1. recombinant protein, eRF3. targeted degradation)。
**Background of GSPT1 Recombinant Protein**
GSPT1 (G1 to S Phase Transition 1), also known as eukaryotic translation termination factor eRF3a, is a critical protein involved in regulating translation termination during protein synthesis. It functions as a GTPase, interacting with eukaryotic release factor eRF1 to recognize stop codons and facilitate ribosome-dependent polypeptide chain release. Structurally, GSPT1 contains a conserved N-terminal domain responsible for GTP binding and hydrolysis, and a C-terminal region mediating interactions with eRF1 and other regulatory partners.
Beyond its role in translation, GSPT1 has gained attention due to its involvement in cellular proliferation, apoptosis, and cancer biology. Overexpression or dysregulation of GSPT1 is linked to malignancies such as acute myeloid leukemia (AML) and solid tumors, where it may promote oncogenic signaling or resistance to therapy. Notably, GSPT1 degradation is exploited therapeutically; compounds like cereblon-modulating agents (e.g., CC-90009) bind to CRL4CRBN E3 ubiquitin ligase, triggering GSPT1 ubiquitination and proteasomal degradation, thereby inhibiting cancer cell growth.
Recombinant GSPT1 proteins are engineered for research and drug development. These proteins are typically produced in bacterial or eukaryotic expression systems, purified via affinity chromatography, and validated for functional activity. They serve as tools to study GSPT1's structure-function relationships, screen small-molecule inhibitors, or analyze interactions within the translation machinery. Additionally, recombinant GSPT1 supports the development of targeted therapies and biomarkers for cancers reliant on GSPT1 signaling.
In summary, GSPT1 is a multifunctional protein bridging translation regulation and disease pathways, with recombinant variants enabling deeper mechanistic insights and therapeutic advancements.
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