| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TIF1b |
| Uniprot No | Q13263 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-291aa |
| 氨基酸序列 | PGEGSAGGEKRSTAPSAAASASASAAASSPAGGGAEALELLEHCGVCRERLRPEREPRLLPCLHSACSACLGPAAPAAANSSGDGGAAGDGTVVDCPVCKQQCFSKDIVENYFMRDSGSKAATDAQDANQCCTSCEDNAPATSYCVECSEPLCETCVEAHQRVKYTKDHTVRSTGPAKSRDGERTVYCNVHKHEPLVLFCESCDTLTCRDCQLNAHKDHQYQFLEDAVRNQRKLLASLVKRLGDKHATLQKSTKEVRSSIRQVSDVQKRV |
| 预测分子量 | 55.8 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TIF1β(TRIM28/KAP1)重组蛋白的3篇参考文献，包括文献名称、作者及摘要概括：
---
1. **文献名称**: *KAP-1. a novel corepressor for the highly conserved KRAB repression domain*
**作者**: Friedman, J.R., Fredericks, W.J., Jensen, D.E. et al.
**摘要**: 该研究首次克隆并鉴定了KAP1(TIF1β)作为KRAB结构域锌指蛋白的核辅阻遏物。通过重组蛋白实验，揭示了KAP1与染色质修饰复合物(如HP1和SETDB1)的相互作用，并证明其在转录沉默中的核心作用。
2. **文献名称**: *The TIF1β homolog KAP1 regulates murine retrovirus expression and innate immunity through SUMO modification*
**作者**: Ivanov, A.V., Peng, H., Yurchenko, V. et al.
**摘要**: 本研究利用重组TIF1β蛋白，阐明了其SUMO化修饰在调控逆转录病毒沉默和先天免疫应答中的机制。实验表明，TIF1β通过SUMO依赖的途径招募组蛋白甲基转移酶SETDB1.介导异染色质形成。
3. **文献名称**: *Structural and functional analysis of the TRIM28/KAP1 coiled-coil domain*
**作者**: Ecco, G., Cassano, M., Cucurachi, T. et al.
**摘要**: 通过重组表达纯化的TIF1β蛋白，解析了其卷曲螺旋结构域的三维结构，并验证了该结构域在介导多聚体形成及与其他辅因子(如HP1)结合中的关键作用。
---
以上文献涵盖了TIF1β重组蛋白在转录调控、表观遗传修饰及结构功能分析中的核心研究，均涉及重组蛋白技术的应用。
TIF1β (Transcriptional Intermediary Factor 1 beta), also known as TRIM28 or KAP1. is a member of the tripartite motif (TRIM) protein family involved in transcriptional regulation, epigenetic modification, and genome stability. Initially identified as a co-repressor for Kruppel-associated box (KRAB) domain-containing zinc finger proteins, it plays a central role in mediating heterochromatin formation, genomic imprinting, and cellular responses to DNA damage. Structurally, TIF1β contains a RING finger domain, B-box motifs, a coiled-coil region (characteristic of TRIM proteins), and a C-terminal PHD-bromodomain module that facilitates chromatin interaction and histone modification recognition.
Recombinant TIF1β protein is engineered for in vitro studies to dissect its molecular functions, including its role in recruiting chromatin-modifying complexes like the SETDB1 histone methyltransferase and the NuRD deacetylase complex. Its ability to regulate pluripotency in stem cells and suppress retrotransposons has made it a focus in developmental biology and cancer research. Dysregulation of TIF1β is linked to oncogenesis, immune evasion, and neurodegenerative disorders.
The recombinant protein is typically produced in bacterial or mammalian expression systems, often tagged with affinity markers (e.g., His-tag, GST) for purification and interaction studies. Researchers utilize it to investigate post-translational modifications (e.g., phosphorylation, SUMOylation) that modulate its activity, as well as its interplay with viral proteins or therapeutic agents. Its conserved role in epigenetic silencing mechanisms and DNA repair pathways underscores its relevance in understanding disease mechanisms and developing targeted therapies.
×
