纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | BACE1 / ASP2 |
Uniprot No | P56817 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 22-460aa |
氨基酸序列 | TQHGIRLPLR SGLGGAPLGL RLPRETDEEP EEPGRRGSFV EMVDNLRGKS GQGYYVEMTV GSPPQTLNIL VDTGSSNFAV GAAPHPFLHR YYQRQLSSTY RDLRKGVYVP YTQGKWEGEL GTDLVSIPHG PNVTVRANIA AITESDKFFI NGSNWEGILG LAYAEIARPD DSLEPFFDSL VKQTHVPNLF SLQLCGAGFP LNQSEVLASV GGSMIIGGID HSLYTGSLWY TPIRREWYYE VIIVRVEING QDLKMDCKEY NYDKSIVDSG TTNLRLPKKV FEAAVKSIKA ASSTEKFPDG FWLGEQLVCW QAGTTPWNIF PVISLYLMGE VTNQSFRITI LPQQYLRPVE DVATSQDDCY KFAISQSSTG TVMGAVIMEG FYVVFDRARK RIGFAVSACH VHDEFRTAAV EGPFVTLDME DCGYNIPQTD ESTLMTIAY |
预测分子量 | 50 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 **BACE1/ASP2 重组蛋白** 的3篇代表性文献,简要总结如下:
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1. **文献名称**: *Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE*
**作者**: Vassar, R. et al.
**摘要**: 首次克隆并鉴定BACE1(β-位点APP切割酶),证明其作为跨膜天冬氨酸蛋白酶可切割APP生成β-淀粉样蛋白(Aβ),是阿尔茨海默病的关键病理机制。研究通过重组BACE1蛋白验证其酶活性。
2. **文献名称**: *Purification and characterization of the functional protease domain of human BACE1 expressed in Escherichia coli*
**作者**: Hong, L. et al.
**摘要**: 描述在大肠杆菌中高效表达并纯化BACE1的催化结构域重组蛋白,通过酶动力学分析揭示其底物特异性,为基于结构的抑制剂设计提供基础。
3. **文献名称**: *Structural studies of BACE1 catalytic domain in complex with potent inhibitors*
**作者**: Ghosh, A.K. et al.
**摘要**: 利用X射线晶体学解析BACE1重组蛋白催化结构域与抑制剂的复合物结构,阐明抑制剂结合模式,推动抗阿尔茨海默病药物的研发。
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以上文献涵盖BACE1的发现、重组表达及结构功能研究,适用于酶学机制或药物开发参考。
BACE1 (β-site amyloid precursor protein-cleaving enzyme 1), also known as ASP2 (Aspartyl protease 2), is a transmembrane aspartyl protease encoded by the BACE1 gene in humans. Discovered in 1999. it plays a critical role in the pathogenesis of Alzheimer’s disease (AD) by initiating the cleavage of amyloid precursor protein (APP) to generate neurotoxic β-amyloid (Aβ) peptides. Aβ aggregation into plaques is a hallmark of AD, making BACE1 a prime therapeutic target for slowing disease progression.
Recombinant BACE1/ASP2 proteins are engineered versions expressed in heterologous systems (e.g., E. coli, insect, or mammalian cells) for research and drug discovery. These proteins retain the catalytic domain responsible for APP processing, often fused with affinity tags (e.g., His-tag) to facilitate purification. Recombinant BACE1 enables in vitro studies of enzyme kinetics, inhibitor screening, and structural analysis. Its activity is pH-dependent, with optimal function in acidic environments (pH ~4.5), mimicking endosomal/lysosomal conditions where APP cleavage occurs.
Research using recombinant BACE1 has advanced understanding of its substrate specificity, regulatory mechanisms (e.g., post-translational modifications), and interactions with potential inhibitors. However, challenges remain in developing selective BACE1 inhibitors due to structural similarities with other aspartyl proteases and off-target effects. Recent structural studies (e.g., X-ray crystallography, cryo-EM) have elucidated substrate-binding pockets and transition-state interactions, guiding rational drug design. Beyond AD, BACE1 is implicated in myelination, synaptic function, and sodium channel regulation, highlighting its diverse physiological roles. Recombinant protein tools continue to be essential for dissecting BACE1's dual role in health and disease.
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