纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | CEL |
Uniprot No | P19835 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 21-753aa |
氨基酸序列 | AKLGAVYTEG GFVEGVNKKL GLLGDSVDIF KGIPFAAPTK ALENPQPHPG WQGTLKAKNF KKRCLQATIT QDSTYGDEDC LYLNIWVPQG RKQVSRDLPV MIWIYGGAFL MGSGHGANFL NNYLYDGEEI ATRGNVIVVT FNYRVGPLGF LSTGDANLPG NYGLRDQHMA IAWVKRNIAA FGGDPNNITL FGESAGGASV SLQTLSPYNK GLIRRAISQS GVALSPWVIQ KNPLFWAKKV AEKVGCPVGD AARMAQCLKV TDPRALTLAY KVPLAGLEYP MLHYVGFVPV IDGDFIPADP INLYANAADI DYIAGTNNMD GHIFASIDMP AINKGNKKVT EEDFYKLVSE FTITKGLRGA KTTFDVYTES WAQDPSQENK KKTVVDFETD VLFLVPTEIA LAQHRANAKS AKTYAYLFSH PSRMPVYPKW VGADHADDIQ YVFGKPFATP TGYRPQDRTV SKAMIAYWTN FAKTGDPNMG DSAVPTHWEP YTTENSGYLE ITKKMGSSSM KRSLRTNFLR YWTLTYLALP TVTDQEATPV PPTGDSEATP VPPTGDSETA PVPPTGDSGA PPVPPTGDSG APPVPPTGDS GAPPVPPTGD SGAPPVPPTG DSGAPPVPPT GDSGAPPVPP TGDSGAPPVP PTGDSGAPPV PPTGDAGPPP VPPTGDSGAP PVPPTGDSGA PPVTPTGDSE TAPVPPTGDS GAPPVPPTGD SEAAPVPPTD DSKEAQMPAV IRF |
预测分子量 | 79,3 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CEL(羧酸酯酶)重组蛋白研究的文献示例,包含标题、作者及摘要概括:
1. **标题**:*"High-level expression and characterization of a novel recombinant human carboxylesterase 1 (rhCE1) in Pichia pastoris"*
**作者**:Li Y, et al.
**摘要**:研究报道了在毕赤酵母系统中高效表达重组人羧酸酯酶1(rhCE1),通过优化密码子和发酵条件显著提升酶活性,并验证其在药物前体水解中的应用潜力。
2. **标题**:*"Functional characterization of recombinant carboxylesterase from Pseudomonas aeruginosa for biodegradation of plasticizers"*
**作者**:Wang X, et al.
**摘要**:该研究克隆并表达了铜绿假单胞菌来源的CEL重组蛋白,证实其对邻苯二甲酸酯类增塑剂的高效降解能力,为环境污染修复提供新策略。
3. **标题**:*"Structural and kinetic analysis of a recombinant carboxylesterase from marine microbial metagenome"*
**作者**:Kim S, et al.
**摘要**:通过宏基因组学筛选得到海洋微生物CEL基因,重组表达后解析其三维结构,揭示其低温高催化活性的分子机制,拓展工业酶应用场景。
注:上述文献为模拟示例,实际引用时需核对真实数据库(如PubMed、Web of Science)获取准确信息。
CEL recombinant protein, derived from the carboxyl ester lipase (CEL) gene, is a key focus in metabolic and pancreatic disease research. CEL, also known as bile salt-dependent carboxyl ester hydrolase or cholesterol esterase, is a digestive enzyme primarily synthesized in the pancreatic acinar cells and secreted into the intestinal lumen. It plays a critical role in hydrolyzing dietary cholesterol esters, lipid-soluble vitamins, and other esterified substrates, contributing to lipid absorption and metabolism. The CEL gene’s polymorphisms and mutations have been linked to pancreatic disorders (e.g., chronic pancreatitis) and diabetes (e.g., maturity-onset diabetes of the young type 8. MODY8), driving interest in its recombinant form for functional studies.
Recombinant CEL is produced using genetic engineering techniques, often expressed in microbial (e.g., *E. coli*) or mammalian cell systems to ensure proper post-translational modifications. This allows large-scale production of highly pure, bioactive protein for research and therapeutic applications. Its applications span enzymology, drug discovery, and disease mechanism studies. For instance, recombinant CEL aids in elucidating how specific mutations disrupt enzyme activity or promote pathogenic protein aggregation in pancreatic tissue. It also serves as a tool for screening enzyme inhibitors or stabilizers for metabolic disease therapy.
Additionally, recombinant CEL is explored as a biologics candidate for enzyme replacement in pancreatic insufficiency and as an antigen in autoimmune diabetes research. Its pathogen-free production and scalability make it advantageous over animal-derived counterparts. Recent studies also investigate its role in lipid-mediated signaling and potential use in drug delivery systems. Overall, CEL recombinant protein bridges basic science and translational medicine, offering insights into digestive disorders, diabetes pathogenesis, and therapeutic innovation.
在生物科技领域,蛋白研发与生产是前沿探索的关键支撑。艾普蒂作为行业内的创新者,凭借自身卓越的研发实力,每年能成功研发 1000 多种全新蛋白,在重组蛋白领域不断突破。 在重组蛋白生产过程中,艾普蒂积累了丰富且成熟的经验。从结构复杂的跨膜蛋白,到具有特定催化功能的酶、参与信号传导的激酶,再到用于免疫研究的病毒抗原,艾普蒂都能实现高效且稳定的生产。 这一成就离不开艾普蒂强大的技术平台。我们构建了多元化的重组蛋白表达系统,昆虫细胞、哺乳动物细胞以及原核蛋白表达系统协同运作。不同的表达系统各有优势,能够满足不同客户对重组蛋白的活性、产量、成本等多样化的需求,从而提供高品质、低成本的活性重组蛋白。 艾普蒂提供的不只是产品,更是从源头到终端的一站式解决方案。从最初的基因合成,精准地构建出符合要求的基因序列,到载体构建,为蛋白表达创造适宜的环境,再到蛋白质表达和纯化,每一个环节都严格把控。我们充分尊重客户的个性化需求,在表达 / 纯化标签的选择、表达宿主的确定等方面,为客户量身定制专属方案。 同时,艾普蒂还配备了多种纯化体系,能够应对不同特性蛋白的纯化需求。这种灵活性和专业性,极大地提高了蛋白表达和纯化的成功率,让客户的研究项目得以顺利推进,在生物科技的探索道路上助力每一位科研工作者迈向成功。
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艾普蒂生物在重组蛋白和天然蛋白开发领域经验十分丰富,拥有超过 2 万种重组蛋白的开发案例。在四大重组蛋白表达平台的运用上,艾普蒂生物不仅经验老到,还积累了详实的成功案例。针对客户的工业化生产需求,我们能够定制并优化实验方案。通过小试探索、工艺放大以及条件优化等环节,对重组蛋白基因序列进行优化,全面探索多种条件,精准找出最契合客户需求的生产方法。 此外,公司还配备了自有下游验证平台,可对重组蛋白展开系统的质量检测与性能测试,涵盖蛋白互作检测、活性验证、内毒素验证等,全方位保障产品质量。 卡梅德生物同样重视蛋白工艺开发,确保生产出的蛋白质具备所需的纯度、稳定性与生物活性,这对于保障药物的安全性和有效性起着关键作用 ,与艾普蒂生物共同推动着行业的发展。
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