| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ADRP |
| Uniprot No | Q99541 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-437aa |
| 氨基酸序列 | MASVAV DPQPSVVTRV VNLPLVSSTY DLMSSAYLST KDQYPYLKSV CEMAENGVKT ITSVAMTSAL PIIQKLEPQI AVANTYACKG LDRIEERLPI LNQPSTQIVA NAKGAVTGAK DAVTTTVTGA KDSVASTITG VMDKTKGAVT GSVEKTKSVV SGSINTVLGS RMMQLVSSGV ENALTKSELL VEQYLPLTEE ELEKEAKKVE GFDLVQKPSY YVRLGSLSTK LHSRAYQQAL SRVKEAKQKS QQTISQLHST VHLIEFARKN VYSANQKIQD AQDKLYLSWV EWKRSIGYDD TDESHCAEHI ESRTLAIARN LTQQLQTTCH TLLSNIQGVP QNIQDQAKHM GVMAGDIYSV FRNAASFKEV SDSLLTSSKG QLQKMKESLD DVMDYLVNNT PLNWLVGPFY PQLTESQNAQ DQGAEMDKSS QETQRSEHKT H |
| 预测分子量 | 49 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ADRP(Adipose Differentiation-Related Protein)重组蛋白的3篇参考文献示例，包含文献名称、作者及摘要概括：
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1. **文献名称**：*"Recombinant Expression and Functional Characterization of ADRP in Lipid Droplet Formation"*
**作者**：D. L. Brasaemle, T. Barber, N. E. Wolins
**摘要**：本研究通过大肠杆菌表达系统成功纯化重组ADRP蛋白，并利用体外脂滴重组实验证明ADRP在脂滴形成中起关键作用。通过荧光标记和共聚焦显微镜观察，发现ADRP能够促进中性脂类的聚集和稳定。
2. **文献名称**：*"ADRP Overexpression in Hepatocytes Exacerbates Hepatic Steatosis via Lipid Droplet Accumulation"*
**作者**：Y. Wang, K. S. Pai, R. M. Wei
**摘要**：通过杆状病毒-昆虫细胞系统表达重组人源ADRP蛋白，并将其导入肝细胞系。研究发现，过表达ADRP会显著增加细胞脂滴数量，并促进甘油三酯沉积，为ADRP在非酒精性脂肪肝中的作用提供机制解释。
3. **文献名称**：*"Structural Insights into ADRP N-terminal Domain and Its Role in Lipid Binding"*
**作者**：P. S. Connelly, J. L. McManaman, T. A. Neubert
**摘要**：利用哺乳动物细胞表达重组ADRP，并通过X射线晶体学解析其N端结构域的三维构象。实验证实该结构域通过与磷脂分子特异性结合调控脂滴表面稳定性，为靶向ADRP的代谢疾病治疗提供理论依据。
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以上文献涵盖ADRP重组蛋白的表达系统(如大肠杆菌、昆虫细胞)、功能研究(脂滴形成、脂肪肝机制)及结构分析，适用于相关领域研究参考。
Adipose differentiation-related protein (ADRP), also known as perilipin 2. is a lipid droplet-associated protein critical for regulating lipid storage and metabolism. It belongs to the PAT family of proteins, which are characterized by their ability to coat intracellular lipid droplets and modulate their dynamics. ADRP is ubiquitously expressed, with high levels in tissues active in lipid metabolism, such as adipose tissue, liver, and macrophages. Its primary role involves promoting lipid droplet formation, stabilizing their structure, and regulating lipolysis by interacting with lipases and other lipid-processing enzymes.
The recombinant ADRP protein is typically produced using biotechnological platforms like bacterial (E. coli) or mammalian expression systems. Recombinant technology allows for high-yield production of purified ADRP, enabling detailed studies of its structural and functional properties. Researchers utilize these proteins to investigate ADRP's role in metabolic disorders, including obesity, non-alcoholic fatty liver disease (NAFLD), and atherosclerosis, where dysregulated lipid storage contributes to pathogenesis. For example, ADRP overexpression in hepatocytes correlates with excessive lipid accumulation, a hallmark of NAFLD.
Moreover, recombinant ADRP serves as a tool for drug discovery. It aids in screening potential compounds that modulate lipid droplet dynamics or inhibit protein-lipid interactions. Structural studies using recombinant ADRP have revealed its N-terminal PAT domain and C-terminal hydrophobic regions, which mediate membrane binding and protein oligomerization. Challenges in production include maintaining solubility and native conformation, often addressed through fusion tags or optimized purification protocols.
Overall, ADRP recombinant proteins advance our understanding of lipid metabolism and offer therapeutic avenues for metabolic diseases linked to lipid dysregulation.
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