| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CAPN7 |
| Uniprot No | Q9Y6W3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-813aa |
| 氨基酸序列 | MDATALERDAVQFARLAVQRDHEGRYSEAVFYYKEAAQALIYAEMAGSSLENIQEKITEYLERVQALHSAVQSKSADPLKSKHQLDLERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKTSYETADKVLQNKLKQLARQALDRAEALSEPLTKPVGKISSTSVKPKPPPVRAHFPLGANPFLERPQSFISPQSCDAQGQRYTAEEIEVLRTTSKINGIEYVPFMNVDLRERFAYPMPFCDRWGKLPLSPKQKTTFSKWVRPEDLTNNPTMIYTVSSFSIKQTIVSDCSFVASLAISAAYERRFNKKLITGIIYPQNKDGEPEYNPCGKYMVKLHLNGVPRKVIIDDQLPVDHKGELLCSYSNNKSELWVSLIEKAYMKVMGGYDFPGSNSNIDLHALTGWIPERIAMHSDSQTFSKDNSFRMLYQRFHKGDVLITASTGMMTEAEGEKWGLVPTHAYAVLDIREFKGLRFIQLKNPWSHLRWKGRYSENDVKNWTPELQKYLNFDPRTAQKIDNGIFWISWDDLCQYYDVIYLSWNPGLFKESTCIHSTWDAKQGPVKDAYSLANNPQYKLEVQCPQGGAAVWVLLSRHITDKDDFANNREFITMVVYKTDGKKVYYPADPPPYIDGIRINSPHYLTKIKLTTPGTHTFTLVVSQYEKQNTIHYTVRVYSACSFTFSKIPSPYTLSKRINGKWSGQSAGGCGNFQETHKNNPIYQFHIEKTGPLLIELRGPRQYSVGFEVVTVSTLGDPGPHGFLRKSSGDYRCGFCYLELENIPSGIFNIIPSTFLPKQEGPFFLDFNSIIPIKITQLQ |
| 预测分子量 | 92,6 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. |
以下是基于CAPN7相关研究方向的模拟参考文献示例(请注意文献信息为假设性概括，实际文献需通过数据库核实)：
1. **文献名称**：*"Functional characterization of recombinant human CAPN7 and its role in autophagic regulation"*
**作者**：Tamura K, et al.
**摘要**：本研究通过昆虫细胞表达系统成功纯化CAPN7重组蛋白，发现其钙依赖性蛋白酶活性对自噬相关蛋白LC3的切割具有调控作用，提示CAPN7可能参与细胞自噬通路。
2. **文献名称**：*"Structural insights into CAPN7 protease domain: Crystallographic analysis of a recombinant mutant"*
**作者**：Chen L, et al.
**摘要**：利用X射线晶体学解析了CAPN7催化结构域的重组蛋白三维结构，揭示了其独特的钙离子结合位点，为设计特异性抑制剂提供了结构基础。
3. **文献名称**：*"CAPN7 interacts with ESCRT-III proteins through its microtubule-interacting domain"*
**作者**：Suzuki M, et al.
**摘要**：通过体外pull-down实验证明重组CAPN7蛋白能与ESCRT-III复合物成员CHMP4B直接结合，表明其在膜修复过程中的潜在功能。
4. **文献名称**：*"Development of a high-yield CAPN7 recombinant expression system in mammalian cells for neurodegenerative disease modeling"*
**作者**：Wang Y, et al.
**摘要**：优化HEK293细胞中CAPN7重组蛋白的分泌表达条件，并验证其在神经元中的异常活性与tau蛋白病理性剪切的相关性。
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**提示**：实际文献需通过PubMed/Google Scholar检索关键词"CAPN7 recombinant"、"Calpain-7 expression"等，建议关注近五年内《Journal of Biological Chemistry》《Cell Reports》等期刊的相关研究。
**Background of CAPN7 Recombinant Protein**
CAPN7. also known as calpain-7 or hepatocyte growth factor-regulated tyrosine kinase substrate (HGS)-associated tyrosine kinase substrate (Hakai), is a member of the calpain family of calcium-dependent cysteine proteases. Unlike classical calpains (e.g., CAPN1/CAPN2), CAPN7 lacks a calcium-binding domain and exhibits unique structural features, including a tandem repeat of cysteine protease domains. It is evolutionarily conserved and implicated in intracellular processes such as membrane trafficking, protein degradation, and autophagy.
CAPN7 is ubiquitously expressed, with higher levels in tissues like the brain, liver, and kidney. Its biological role remains partially understood, but studies suggest it interacts with endosomal sorting complexes (ESCRT) to regulate vesicle formation and lysosomal degradation. CAPN7 also participates in epidermal growth factor receptor (EGFR) trafficking and may influence cell adhesion by modulating cadherin-based junctions. Dysregulation of CAPN7 has been linked to pathological conditions, including cancer metastasis and neurodegenerative disorders.
Recombinant CAPN7 protein is produced via heterologous expression systems (e.g., *E. coli* or mammalian cells) for functional studies. Purified CAPN7 enables *in vitro* analysis of its protease activity, substrate specificity, and interaction partners. Researchers utilize this tool to explore its enzymatic regulation, particularly its calcium-independent activation mechanism, which distinguishes it from traditional calpains. Additionally, recombinant CAPN7 aids in structural studies to resolve its unique domain architecture and catalytic mechanism.
Current research focuses on clarifying CAPN7's physiological substrates, signaling pathways, and therapeutic potential in diseases linked to proteostasis imbalance. Its recombinant form remains critical for advancing mechanistic insights into non-classical calpain functions.
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