| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Cenpa |
| Uniprot No | P49450 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-114aa |
| 氨基酸序列 | MGPRRRSRKP EAPRRRSPSP TPTPGPSRRG PSLGASSHQH SRRRQGWLKE IRKLQKSTHL LIRKLPFSRL AAEAFLVHLF EDAYLLTLHA GRVTLFPKDV QLARRIRGLE EGLG |
| 预测分子量 | 16 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Cenpa重组蛋白的3篇参考文献及其摘要概述：
1. **"Human CENP-A contains a histone H3 related histone fold domain that is required for targeting to chromosomes"**
*作者：Yoda K, Ando S, Okuda A, et al. (2004)*
摘要：该研究首次报道了人源Cenpa重组蛋白的表达与功能，发现其N端结构域对染色体定位至关重要，并在体外验证了其与组蛋白H4的相互作用，为理解着丝粒组装奠定了基础。
2. **"Crystal structure of the human centromeric nucleosome containing CENP-A"**
*作者：Tachiwana H, Kagawa W, Shiga T, et al. (2011)*
摘要：通过重组表达Cenpa蛋白与组蛋白H4/H2A/H2B复合体，解析了Cenpa核小体的晶体结构，揭示了其独特的DNA缠绕方式及与其他着丝粒蛋白的结合界面。
3. **"Recombinant CENP-A nucleosomes reconstitute a functional centromere in vivo"**
*作者：Sekulic N, Black BE. (2018)*
摘要：研究利用重组Cenpa蛋白在体外组装核小体，并证明其能在人类细胞中重建功能性着丝粒，验证了重组蛋白在维持染色体分离中的生物学活性。
Cenpa (Centromere Protein-A) is a histone H3 variant critical for centromere specification and chromosome segregation during cell division. As a core component of centromeric chromatin, it replaces canonical histone H3 in nucleosomes at centromeres, forming a unique epigenetic signature essential for kinetochore assembly. Unlike standard histones, Cenpa-containing nucleosomes exhibit a heterotypic tetrameric structure, conferring structural stability and serving as a platform for recruiting other centromere-associated proteins. Its incorporation into chromatin is tightly regulated, ensuring centromere function is maintained through cell cycles. Dysregulation of Cenpa is linked to genomic instability, chromosomal missegregation, and diseases such as cancer.
Recombinant Cenpa proteins are engineered in vitro using expression systems (e.g., E. coli, mammalian cells) to study its biochemical and functional properties. These proteins retain the ability to form nucleosome-like particles and interact with binding partners like HJURP (Holiday Junction Recognition Protein), which chaperones Cenpa deposition. Recombinant Cenpa enables in vitro reconstitution of centromeric chromatin, facilitating studies on centromere assembly, epigenetic inheritance, and mitotic regulation. It is widely used in structural analyses (e.g., cryo-EM), binding assays, and functional screens to dissect centromere biology.
Research on recombinant Cenpa has advanced understanding of centromere evolution, particularly in holocentric organisms, and its role in cancer progression. Overexpression of Cenpa in tumors correlates with poor prognosis, making it a potential therapeutic target. Additionally, recombinant Cenpa tools aid in developing synthetic chromosomes and gene delivery systems. By enabling precise manipulation of centromeric processes, these proteins remain pivotal in exploring cell division mechanisms and developing strategies to address chromosomal disorders.
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