纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | PL |
Uniprot No | P16233 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-465aa |
氨基酸序列 | MLPLWTLSLL LGAVAGKEVC YERLGCFSDD SPWSGITERP LHILPWSPKD VNTRFLLYTN ENPNNFQEVA ADSSSISGSN FKTNRKTRFI IHGFIDKGEE NWLANVCKNL FKVESVNCIC VDWKGGSRTG YTQASQNIRI VGAEVAYFVE FLQSAFGYSP SNVHVIGHSL GAHAAGEAGR RTNGTIGRIT GLDPAEPCFQ GTPELVRLDP SDAKFVDVIH TDGAPIVPNL GFGMSQVVGH LDFFPNGGVE MPGCKKNILS QIVDIDGIWE GTRDFAACNH LRSYKYYTDS IVNPDGFAGF PCASYNVFTA NKCFPCPSGG CPQMGHYADR YPGKTNDVGQ KFYLDTGDAS NFARWRYKVS VTLSGKKVTG HILVSLFGNK GNSKQYEIFK GTLKPDSTHS NEFDSDVDVG DLQMVKFIWY NNVINPTLPR VGASKIIVET NVGKQFNFCS PETVREEVLL TLTPC |
预测分子量 | 51 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. |
以下为3篇与PL重组蛋白相关的参考文献示例,内容基于典型研究方向整理:
1. **《Optimization of Prolactin-like Protein (PLP) Expression in E. coli for Functional Studies》**
*作者:Smith J, et al.*
摘要:探讨了在大肠杆菌系统中优化PL重组蛋白表达的策略,通过密码子优化和诱导条件调整提高可溶性表达,并验证其生物活性。
2. **《Yeast Secretory Production of Placental Lactogen (PL) for Therapeutic Applications》**
*作者:Li X, et al.*
摘要:研究利用毕赤酵母系统高效分泌表达人胎盘催乳素(PL),分析其糖基化修饰对蛋白稳定性和体内活性的影响,推动其在产科疾病治疗中的应用。
3. **《Structural and Functional Analysis of Recombinant PL Protein in Cancer Immunotherapy》**
*作者:Wang R, et al.*
摘要:通过X射线晶体学解析PL重组蛋白的三维结构,结合体外实验验证其与免疫检查点分子的相互作用,为开发新型肿瘤免疫疗法提供依据。
(注:以上文献标题与内容为示例性质,实际文献需根据具体研究领域在PubMed、Web of Science等平台检索。)
**Background of PL Recombinant Proteins**
Recombinant proteins, including PL (a hypothetical or context-specific designation), are engineered through recombinant DNA technology, enabling the production of specific proteins in heterologous host systems. Since the advent of genetic engineering in the 1970s, this approach has revolutionized biotechnology by allowing precise manipulation of genes to express proteins with tailored functions. PL recombinant proteins, depending on their biological origin or application, may represent therapeutic agents, enzymes, or structural proteins designed for industrial, medical, or research purposes.
The production typically involves cloning a target gene into vectors, transforming host cells (e.g., *E. coli*, yeast, or mammalian cells*), and optimizing conditions for protein expression and purification. Advances in synthetic biology, CRISPR editing, and high-throughput screening have enhanced the efficiency and scalability of recombinant protein synthesis. PL variants might be engineered for improved stability, activity, or reduced immunogenicity, particularly if intended for therapeutic use, such as in vaccines, monoclonal antibodies, or enzyme replacement therapies.
In biomedical research, PL recombinant proteins serve as tools for studying protein interactions, signaling pathways, or disease mechanisms. Industrially, they are applied in biocatalysis, biofuel production, or biodegradable material synthesis. Challenges include ensuring proper post-translational modifications (e.g., glycosylation) in prokaryotic systems, minimizing aggregation, and complying with regulatory standards for clinical applications.
Future directions focus on cell-free systems, AI-driven protein design, and sustainable production platforms. PL recombinant proteins exemplify the intersection of molecular biology and bioengineering, driving innovations across healthcare, agriculture, and environmental science.
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