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Recombinant Human PLPL protein

  • 中文名: 髓鞘蛋白脂蛋白样蛋白(PLPL)重组蛋白
  • 别    名: PLPL;Omega-hydroxyceramide transacylase
货号: PA1000-9189
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点PLPL
Uniprot NoQ96AD5
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-504aa
氨基酸序列MFPREKTWNISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGA LTATALVTGVCLGEAGAKFIEVSKEARKRFLGPLHPSFNLVKIIRSFLLK VLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPV YCGLIPPSLQGVRYVDGGISDNLPLYELKNTITVSPFSGESDICPQDSST NIHELRVTNTSIQFNLRNLYRLSKALFPPEPLVLREMCKQGYRDGLRFLQ RNGLLNRPNPLLALPPARPHGPEDKDQAVESAQAEDYSQLPGEDHILEHL PARLNEALLEACVEPTDLLTTLSNMLPVRLATAMMVPYTLPLESALSFTI RLLEWLPDVPEDIRWMKEQTGSICQYLVMRAKRKLGRHLPSRLPEQVELR RVQSLPSVPLSCAAYREALPGWMRNNLSLGDALAKWEECQRQLLLGLFCT NVAFPPEALRMRAPADPAPAPADPASPQHQLAGPAPLLSTPAPEARPVIG ALGL
预测分子量71 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.

参考文献

以下是基于假设的模拟参考文献示例(请注意,PLPL重组蛋白的具体信息可能需要进一步核实术语准确性):

1. **《高效表达PLPL重组蛋白的大肠杆菌系统构建》- 作者:张伟等**

摘要:研究利用大肠杆菌表达系统成功表达PLPL重组蛋白,优化了诱导条件及纯化工艺,获得高纯度蛋白,为后续功能研究奠定基础。

2. **《PLPL重组蛋白在肿瘤靶向治疗中的应用评估》- 作者:Chen, L. et al.**

摘要:探讨PLPL重组蛋白作为药物载体的可行性,通过体外实验证实其能特异性结合肿瘤细胞并增强化疗药物递送效率。

3. **《PLPL重组蛋白的晶体结构解析及功能位点鉴定》- 作者:Kim, S. et al.**

摘要:采用X射线衍射技术解析PLPL蛋白的三维结构,发现其活性中心的关键氨基酸,为酶活性调控提供结构依据。

4. **《PLPL重组蛋白在植物抗逆反应中的功能研究》- 作者:Martinez, R. et al.**

摘要:通过转基因技术验证PLPL蛋白在植物耐旱性中的作用,揭示其通过调节脂质代谢增强细胞膜稳定性。

**注意事项**:

- 上述文献为模拟示例,实际研究中“PLPL”可能需替换为准确术语(如PLpro、PLGA相关蛋白等)。

- 建议通过PubMed或Google Scholar以“PLPL recombinant protein”或相关关键词检索真实文献,或确认蛋白全称/研究领域以获取精准信息。

背景信息

**Background of PLPL Recombinant Proteins**

Recombinant proteins, engineered through genetic modification, are pivotal in modern biotechnology and therapeutic development. PLPL (example designation; specifics may vary by context) recombinant proteins typically refer to engineered variants designed to mimic or enhance native protein functions. These proteins are synthesized by inserting target gene sequences into expression vectors, which are then transfected into host systems (e.g., *E. coli*, yeast, or mammalian cells*) for large-scale production.

PLPL proteins may belong to specific functional classes, such as enzymes, signaling molecules, or structural proteins, depending on their native counterparts. For instance, if PLPL denotes a phospholipase-like protein, it could play roles in lipid metabolism, membrane remodeling, or cellular signaling. Recombinant versions allow researchers to study these mechanisms under controlled conditions, bypassing challenges like low natural abundance or complex purification processes.

In therapeutics, PLPL recombinant proteins are explored for drug development, particularly in targeting metabolic disorders, inflammatory diseases, or cancers. Their engineered features—such as improved stability, reduced immunogenicity, or enhanced binding affinity—make them advantageous over natural proteins. Additionally, they serve as critical tools in diagnostics, vaccine production, and structural biology.

Challenges in PLPL recombinant protein production include ensuring proper folding, post-translational modifications (e.g., glycosylation), and scalability. Advances in expression systems (e.g., CHO cells for complex proteins) and purification techniques (affinity chromatography, tag-based systems) continue to address these hurdles.

Overall, PLPL recombinant proteins exemplify the intersection of genetic engineering and functional biology, driving innovations in both research and clinical applications. Their tailored design and versatility underscore their growing importance in addressing unmet medical and industrial needs.

*(Note: "PLPL" is used as a placeholder; actual proteins may have context-specific nomenclature or functions.)*

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