| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PLCL2 |
| Uniprot No | Q9UPR0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1127aa |
| 氨基酸序列 | MAECGRGGAAGGALPTSPGPALGAKGALKAGVGEGGGGGGRLGHGRARYDSGGVSNGDCSLGVSGDEARASPTRGPRGVALAPTPSAVVCTLPRESKPGGLPRRSSIIKDGTKQKRERKKTVSFSSMPTEKKISSASDCINSMVEGSELKKVRSNSRIYHRYFLLDADMQSLRWEPSKKDSEKAKIDIKSIKEVRTGKNTDIFRSNGISDQISEDCAFSVIYGENYESLDLVANSADVANIWVTGLRYLISYGKHTLDMLESSQDNMRTSWVSQMFSEIDVDNLGHITLCNAVQCIRNLNPGLKTSKIELKFKELHKSKDKAGTEVTKEEFIEVFHELCTRPEIYFLLVQFSSNKEFLDTKDLMMFLEAEQGVAHINEEISLEIIHKYEPSKEGQEKGWLSIDGFTNYLMSPDCYIFDPEHKKVCQDMKQPLSHYFINSSHNTYLIEDQFRGPSDITGYIRALKMGCRSVELDVWDGPDNEPVIYTGHTMTSQIVFRSVIDIINKYAFFASEYPLILCLENHCSIKQQKVMVQHMKKLLGDKLYTTSPNVEESYLPSPDVLKGKILIKAKKLSSNCSGVEGDVTDEDEGAEMSQRMGKENMEQPNNVPVKRFQLCKELSELVSICKSVQFKEFQVSFQVQKYWEVCSFNEVLASKYANENPGDFVNYNKRFLARVFPSPMRIDSSNMNPQDFWKCGCQIVAMNFQTPGLMMDLNIGWFRQNGNCGYVLRPAIMREEVSFFSANTKDSVPGVSPQLLHIKIISGQNFPKPKGSGAKGDVVDPYVYVEIHGIPADCAEQRTKTVHQNGDAPIFDESFEFQINLPELAMVRFVVLDDDYIGDEFIGQYTIPFECLQTGYRHVPLQSLTGEVLAHASLFVHVAITNRRGGGKPHKRGLSVRKGKKSREYASLRTLWIKTVDEVFKNAQPPIRDATDLRENMQNAVVSFKELCGLSSVANLMQCMLAVSPRFLGPDNTPLVVLNLSEQYPTMELQGIVPEVLKKIVTTYDMMIQSLKALIENADAVYEKIVHCQKAAMEFHEHLHSIGTKEGLKERKLQKAVESFTWNITILKGQADLLKYAKNETLENLKQIHFAAVSCGLNKPGTENADVQKPRRSLEVIPEKANDETGE |
| 预测分子量 | 125,8 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PLCL2重组蛋白的3篇示例文献(注：内容为虚构示例，实际文献需通过学术数据库检索确认)：
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1. **文献名称**：*"Recombinant PLCL2 Protein Modulates Inflammatory Signaling in Macrophages"*
**作者**：Chen, L. et al.
**摘要**：研究通过大肠杆菌表达系统成功纯化重组PLCL2蛋白，并证明其通过调控NF-κB通路抑制巨噬细胞炎症反应，为治疗炎症性疾病提供潜在靶点。
2. **文献名称**：*"Structural and Functional Analysis of PLCL2 in Calcium Signaling"*
**作者**：Yamamoto, K. et al.
**摘要**：利用重组PLCL2蛋白解析其晶体结构，揭示其PH结构域在钙离子信号转导中的关键作用，为理解PLCL家族蛋白功能提供新依据。
3. **文献名称**：*"PLCL2 Recombinant Protein Enhances Cardiac Fibroblast Proliferation via TGF-β Pathway"*
**作者**：Wang, Q. et al.
**摘要**：通过哺乳动物细胞表达系统制备功能性PLCL2重组蛋白，证实其通过激活TGF-β/Smad通路促进心脏成纤维细胞增殖，可能与心肌纤维化相关。
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建议通过PubMed、Web of Science或Google Scholar以关键词“PLCL2 recombinant protein”“PLCL2 expression”检索真实文献。
PLCL2 (Phospholipase C-like 2) is a protein belonging to the phospholipase C (PLC) family, which plays diverse roles in cellular signaling. Unlike canonical PLC enzymes that hydrolyze phosphatidylinositol 4.5-bisphosphate (PIP2) into secondary messengers (IP3 and diacylglycerol), PLCL2 is classified as a "pseudoenzyme" due to mutations in its catalytic domain that likely render it enzymatically inactive. Despite this, PLCL2 retains structural homology to active PLC isoforms, including conserved pleckstrin homology (PH) and EF-hand domains, suggesting potential regulatory functions in phosphoinositide signaling pathways. Its exact biological role remains under investigation, but studies propose involvement in intracellular calcium regulation, cytoskeletal organization, and receptor-mediated signaling crosstalk.
Recombinant PLCL2 protein is engineered for research applications, typically produced using expression systems like bacterial, insect, or mammalian cells. The recombinant form often includes affinity tags (e.g., His-tag, GST) to facilitate purification and detection. Researchers utilize PLCL2 recombinant protein to study its interactions with signaling molecules, membrane components, or cytoskeletal proteins, aiming to clarify its non-catalytic mechanisms. It has also been implicated in pathological contexts; PLCL2 overexpression correlates with certain cancers, neurological disorders, and immune dysregulation, hinting at its potential as a diagnostic marker or therapeutic target. Structural studies of recombinant PLCL2 help map critical domains responsible for its scaffolding or competitive binding roles, providing insights into its modulation of PLC-driven pathways. Current research focuses on deciphering how PLCL2 fine-tunes cellular responses despite lacking enzymatic activity, possibly through allosteric regulation or sequestration of signaling intermediates.
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