纯度 | > 90 % SDS-PAGE. |
种属 | Human |
靶点 | ASRGL1 |
Uniprot No | Q7L266 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-308aa |
氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMNPIVVV HGGGAGPISK DRKERVHQGM VRAATVGYGI LREGGSAVDA VEGAVVALED DPEFNAGCGS VLNTNGEVEM DASIMDGKDL SAGAVSAVQC IANPIKLARL VMEKTPHCFL TDQGAAQFAA AMGVPEIPGE KLVTERNKKR LEKEKHEKGA QKTDCQKNLG TVGAVALDCK GNVAYATSTG GIVNKMVGRV GDSPCLGAGG YADNDIGAVS TTGHGESILK VNLARLTLFH IEQGKTVEEA ADLSLGYMKS RVKGLGGLIV VSKTGDWVAK WTSTSMPWAA AKDGKLHFGI DPDDTTITDL P |
预测分子量 | 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3篇关于ASRGL1重组蛋白的参考文献摘要概括,基于现有研究主题的合理推测(部分文献名称及作者为虚拟示例,建议通过学术数据库核实):
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1. **文献名称**:*"Recombinant ASRGL1 Expression in E. coli: Purification and Enzymatic Activity Analysis"*
**作者**:Chen L, et al.
**摘要**:本研究成功在大肠杆菌中表达并纯化了带有His标签的重组ASRGL1蛋白,证实其具有天冬酰胺酶活性,并揭示了pH和温度对酶活性的影响,为后续功能研究提供工具。
2. **文献名称**:*"ASRGL1 Recombinant Protein Suppresses Ovarian Cancer Cell Proliferation via Degrading Asparagine"*
**作者**:Wang Y, et al.
**摘要**:通过哺乳动物细胞系统表达ASRGL1重组蛋白,发现其通过消耗细胞外天冬酰胺抑制卵巢癌细胞生长,提示其作为潜在肿瘤治疗靶点的价值。
3. **文献名称**:*"Crystal Structure of Human ASRGL1 Reveals Unique Substrate-Binding Motifs"*
**作者**:Kimura T, et al.
**摘要**:利用重组ASRGL1蛋白进行X射线晶体学分析,解析了其三维结构,发现特异性底物结合域,为设计靶向抑制剂奠定结构基础。
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**注意**:以上内容为示例,实际文献需通过PubMed、Web of Science等平台检索。建议使用关键词“ASRGL1 recombinant”“ASRGL1 purification”或结合具体研究领域(如癌症、酶学)进一步筛选。
ASRGL1 (Asparaginase-like protein 1) is a conserved eukaryotic enzyme belonging to the asparaginase family, with dual enzymatic activities: asparaginase and isoaspartyl peptidase. It catalyzes the hydrolysis of asparagine to aspartate and ammonia, and repairs protein damage by cleaving isoaspartyl residues formed through spontaneous deamidation or isomerization. These functions position ASRGL1 as a critical player in maintaining protein homeostasis and amino acid metabolism. Structurally, it shares homology with bacterial asparaginases but contains a unique N-terminal domain proposed to regulate substrate specificity or cellular localization.
The enzyme is ubiquitously expressed, with high levels in the liver, brain, and reproductive tissues. Its physiological roles extend to cell cycle regulation, neuronal health, and reproductive system function. Notably, ASRGL1 has been implicated in multiple pathologies. In ovarian and endometrial cancers, reduced ASRGL1 expression correlates with poor prognosis and chemoresistance, potentially through dysregulation of asparagine metabolism. In neurodegenerative disorders like Alzheimer's and tauopathies, ASRGL1 mislocalization from microtubules may contribute to pathological tau accumulation.
Recombinant ASRGL1 protein, typically produced in E. coli or mammalian expression systems, serves as a vital tool for studying its structure-function relationships and enzymatic mechanisms. Purification often involves affinity chromatography tags (e.g., His-tag) followed by enzymatic activity validation. Current research leverages recombinant ASRGL1 to explore its therapeutic potential, including enzyme replacement strategies for asparagine-related disorders and targeted cancer therapies. However, challenges persist in understanding its substrate preference regulation and developing small-molecule modulators. As an emerging biomarker and drug target, ASRGL1 continues to bridge fundamental biochemistry with translational medical applications.
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