| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CHERP |
| Uniprot No | Q8IWX8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-916aa |
| 氨基酸序列 | MEMPLPPDDQELRNVIDKLAQFVARNGPEFEKMTMEKQKDNPKFSFLFGGEFYSYYKCKLALEQQQLICKQQTPELEPAATMPPLPQPPLAPAAPIPPAQGAPSMDELIQQSQWNLQQQEQHLLALRQEQVTAAVAHAVEQQMQKLLEETQLDMNEFDNLLQPIIDTCTKDAISAGKNWMFSNAKSPPHCELMAGHLRNRITADGAHFELRLHLIYLINDVLHHCQRKQARELLAALQKVVVPIYCTSFLAVEEDKQQKIARLLQLWEKNGYFDDSIIQQLQSPALGLGQYQATLINEYSSVVQPVQLAFQQQIQTLKTQHEEFVTSLAQQQQQQQQQQQQLQMPQMEAEVKATPPPPAPPPAPAPAPAIPPTTQPDDSKPPIQMPGSSEYEAPGGVQDPAAAGPRGPGPHDQIPPNKPPWFDQPHPVAPWGQQQPPEQPPYPHHQGGPPHCPPWNNSHEGMWGEQRGDPGWNGQRDAPWNNQPDAAWNSQFEGPWNSQHEQPPWGGGQREPPFRMQRPPHFRGPFPPHQQHPQFNQPPHPHNFNRFPPRFMQDDFPPRHPFERPPYPHRFDYPQGDFPAEMGPPHHHPGHRMPHPGINEHPPWAGPQHPDFGPPPHGFNGQPPHMRRQGPPHINHDDPSLVPNVPYFDLPAGLMAPLVKLEDHEYKPLDPKDIRLPPPMPPSERLLAAVEAFYSPPSHDRPRNSEGWEQNGLYEFFRAKMRARRRKGQEKRNSGPSRSRSRSKSRGRSSSRSNSRSSKSSGSYSRSRSRSCSRSYSRSRSRSRSRSRSSRSRSRSQSRSRSKSYSPGRRRRSRSRSPTPPSSAGLGSNSAPPIPDSRLGEENKGHQMLVKMGWSGSGGLGAKEQGIQDPIKGGDVRDKWDQYKGVGVALDDPYENYRRNKSYSFIARMKARDECK |
| 预测分子量 | 103,7 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CHERP重组蛋白的模拟参考文献(虚构内容，仅供示例)：
1. **文献名称**：*CHERP蛋白在钙信号调控中的功能研究*
**作者**：Zhang L, et al.
**摘要**：研究揭示了CHERP(Calcium Homeostasis Endoplasmic Reticulum Protein)通过与内质网钙离子通道IP3R相互作用，调节细胞内钙稳态的分子机制，并利用重组蛋白技术验证其结合活性。
2. **文献名称**：*重组CHERP蛋白的高效表达与纯化*
**作者**：Wang Y, et al.
**摘要**：开发了一种基于大肠杆菌表达系统的重组CHERP蛋白制备方法，通过优化诱导条件和亲和层析技术获得高纯度蛋白，为后续功能研究提供材料基础。
3. **文献名称**：*CHERP缺失对心血管疾病模型的影响*
**作者**：Chen R, et al.
**摘要**：利用CRISPR/Cas9技术构建CHERP敲除细胞系，发现其缺失导致心肌细胞钙信号异常，提示CHERP在心脏病理生理中的潜在作用。
4. **文献名称**：*CHERP蛋白结构与功能域分析*
**作者**：Kim S, et al.
**摘要**：通过X射线晶体学解析重组CHERP蛋白的三维结构，确定其关键功能域，并揭示其与DNA损伤修复通路相关蛋白的相互作用。
注：以上内容为模拟生成，实际文献需通过学术数据库(如PubMed、Web of Science)检索关键词"CHERP recombinant protein"或"CHERP protein function"获取。
CHERP (Calcium Homeostasis Endoplasmic Reticulum Protein) is a ubiquitously expressed protein implicated in cellular calcium regulation and transcriptional processes. Initially identified through its interaction with the inositol 1.4.5-trisphosphate receptor (IP3R), CHERP facilitates calcium release from the endoplasmic reticulum (ER), a critical step in intracellular signaling pathways. Structurally, it contains dual N-terminal EF-hand motifs for calcium sensing and a C-terminal domain involved in protein-protein interactions, enabling its role as a molecular scaffold.
Beyond calcium homeostasis, CHERP participates in pre-mRNA splicing by associating with the U5 small nuclear ribonucleoprotein (snRNP) complex, linking calcium signaling to gene expression regulation. Dysregulation of CHERP has been correlated with pathological conditions, including cardiovascular diseases and cancer, where altered calcium signaling and aberrant splicing contribute to disease progression. For instance, reduced CHERP expression in hepatocellular carcinoma correlates with enhanced tumor growth and metastasis.
Recombinant CHERP protein is typically produced using bacterial or mammalian expression systems to study its biochemical properties, interaction networks, and therapeutic potential. Its purification often involves affinity tags (e.g., His-tag) followed by chromatography techniques. Researchers utilize recombinant CHERP to investigate calcium-dependent signaling mechanisms, screen drug candidates targeting calcium dysregulation, and develop splice-modulating therapies. Recent studies also explore its potential in neurodegenerative diseases where calcium imbalance and RNA splicing defects are prominent. As a multifunctional protein bridging calcium dynamics and genetic regulation, CHERP represents a compelling target for both basic research and translational applications.
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