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Recombinant Human TRIP13 protein

  • 中文名: 粗线期检查点蛋白2同源物(TRIP13)重组蛋白
  • 别    名: TRIP13;PCH2;Pachytene checkpoint protein 2 homolog
货号: PA2000-4660
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点TRIP13
Uniprot No Q15645
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 1-432aa
氨基酸序列MDEAVGDLKQALPCVAESPTVHVEVHQRGSSTAKKEDINLSVRKLLNRHNIVFGDYTWTEFDEPFLTRNVQSVSIIDTELKVKDSQPIDLSACTVALHIFQLNEDGPSSENLEEETENIIAANHWVLPAAEFHGLWDSLVYDVEVKSHLLDYVMTTLLFSDKNVNSNLITWNRVVLLHGPPGTGKTSLCKALAQKLTIRLSSRYRYGQLIEINSHSLFSKWFSESGKLVTKMFQKIQDLIDDKDALVFVLIDEVESLTAARNACRAGTEPSDAIRVVNAVLTQIDQIKRHSNVVILTTSNITEKIDVAFVDRADIKQYIGPPSAAAIFKIYLSCLEELMKCQIIYPRQQLLTLRELEMIGFIENNVSKLSLLLNDISRKSEGLSGRVLRKLPFLAHALYVQAPTVTIEGFLQALSLAVDKQFEERKKLAAYI
预测分子量 54.6 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.

参考文献

以下是3篇关于TRIP13重组蛋白的简要文献信息及内容概括:

1. **文献名称**: "Structure and function of the AAA+ ATPase TRIP13 in mitotic checkpoint control"

**作者**: Yost S, et al.

**摘要**: 本研究解析了TRIP13重组蛋白的晶体结构,揭示其通过ATP酶活性调控纺锤体检查点蛋白MAD2的构象变化,促进染色体正确分离的分子机制。

2. **文献名称**: "TRIP13 reshapes recombination machinery for DNA repair in human cells"

**作者**: Wojtasz L, et al.

**摘要**: 通过体外重组实验发现TRIP13与HORMAD1协同作用,重塑DNA同源重组修复复合体结构,影响乳腺癌细胞对PARP抑制剂的敏感性。

3. **文献名称**: "Recombinant TRIP13 exhibits ATP-dependent modulation of meiotic crossover formation"

**作者**: Qiao H, et al.

**摘要**: 利用重组TRIP13蛋白进行生化实验,证明其通过水解ATP调控减数分裂中交叉重组频率,揭示其在生殖细胞基因组稳定性中的关键作用。

4. **文献名称**: "TRIP13 promotes cancer stemness via the Wnt/β-catenin pathway in hepatocellular carcinoma"

**作者**: Chen X, et al.

**摘要**: 研究通过重组TRIP13过表达模型,发现其通过激活Wnt信号通路增强肝癌干细胞自我更新能力,提示其作为治疗靶点的潜力。

注:以上文献标题及作者为示例性内容,实际文献需通过PubMed(https://pubmed.ncbi.nlm.nih.gov)等数据库检索确认。

背景信息

**Background of TRIP13 Recombinant Protein**

TRIP13 (Thyroid hormone Receptor Interactor Protein 13) is a member of the AAA+ ATPase family, known for its critical role in regulating mitotic and meiotic processes, particularly chromosome recombination and DNA repair. It functions as a key mediator in the spindle assembly checkpoint (SAC) by facilitating the structural remodeling of proteins involved in cell cycle progression. TRIP13 interacts with MAD2. a component of the SAC, to promote the conversion of inactive MAD2 conformers, thereby ensuring accurate chromosome segregation during cell division. Additionally, it plays a role in resolving recombination intermediates during meiosis by processing Holliday junctions in collaboration with the Shugoshin protein complex.

Structurally, TRIP13 forms a hexameric ring and utilizes ATP hydrolysis to drive conformational changes in its substrates, enabling substrate recognition and remodeling. This ATP-dependent activity is essential for its function in both mitotic checkpoints and meiotic recombination. Dysregulation of TRIP13 has been implicated in chromosomal instability, which is a hallmark of various cancers. Overexpression of TRIP13 is observed in ovarian, breast, and prostate cancers, correlating with poor prognosis and chemoresistance. Conversely, mutations in TRIP13 are linked to developmental disorders, such as female-limited gonadal dysgenesis, highlighting its importance in reproductive health.

Recombinant TRIP13 protein, produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), is widely used to study its biochemical properties, ATPase activity, and interactions with partner proteins. It also serves as a tool for screening inhibitors targeting its ATPase function, offering potential therapeutic avenues for cancer treatment. Research continues to unravel its multifaceted roles in genome stability and disease pathogenesis.

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