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Recombinant Human LIPC protein

  • 中文名: 肝脂酶(LIPC)重组蛋白
  • 别    名: LIPC;HTGL;Hepatic triacylglycerol lipase
货号: PA1000-8429
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点LIPC
Uniprot NoP11150
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-499aa
氨基酸序列MDTSPLCFSILLVLCIFIQSSALGQSLKPEPFGRRAQAVETNKTLHEMKTRFLLFGETNQGCQIRINHPDTLQECGFNSSLPLVMIIHGWSVDGVLENWIWQMVAALKSQPAQPVNVGLVDWITLAHDHYTIAVRNTRLVGKEVAALLRWLEESVQLSRSHVHLIGYSLGAHVSGFAGSSIGGTHKIGRITGLDAAGPLFEGSAPSNRLSPDDANFVDAIHTFTREHMGLSVGIKQPIGHYDFYPNGGSFQPGCHFLELYRHIAQHGFNAITQTIKCSHERSVHLFIDSLLHAGTQSMAYPCGDMNSFSQGLCLSCKKGRCNTLGYHVRQEPRSKSKRLFLVTRAQSPFKVYHYQFKIQFINQTETPIQTTFTMSLLGTKEKMQKIPITLGKGIASNKTYSFLITLDVDIGELIMIKFKWENSAVWANVWDTVQTIIPWSTGPRHSGLVLKTIRVKAGETQQRMTFCSENTDDLLLRPTQEKIFVKCEIKSKTSKRKIR
预测分子量55,9 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

以下为示例性质的参考文献格式,供参考(具体文献需通过学术数据库验证):

1. **标题**: "Expression and characterization of recombinant human hepatic lipase (LIPC) in mammalian cells"

**作者**: Smith J, et al.

**摘要**: 报道在HEK293细胞中重组表达人LIPC蛋白,通过亲和层析纯化并验证其磷脂酶活性,证实重组蛋白在体外具有水解甘油三酯的功能。

2. **标题**: "Structural analysis of LIPC variants using recombinant protein expression systems"

**作者**: Lee H, et al.

**摘要**: 利用昆虫细胞-杆状病毒系统表达LIPC突变体,结合X射线晶体学解析其三维结构,揭示关键氨基酸对酶催化活性的影响。

3. **标题**: "Functional characterization of LIPC recombinant protein in lipid metabolism regulation"

**作者**: Wang Y, et al.

**摘要**: 在大肠杆菌中高效表达可溶性LIPC重组蛋白,通过体外实验证明其参与HDL代谢调控,并评估了其在动脉粥样硬化模型中的作用。

4. **标题**: "Optimization of LIPC recombinant protein production in Pichia pastoris"

**作者**: Gonzalez R, et al.

**摘要**: 采用毕赤酵母表达系统优化LIPC的分泌表达,获得高产量活性蛋白,并应用于血清脂质水平的体外检测试剂开发。

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**提示**:实际文献可通过以下方式查找:

1. 在 **PubMed** 或 **Google Scholar** 中搜索关键词:

`"LIPC recombinant protein"`, `"hepatic lipase expression"`

2. 关注涉及脂代谢、蛋白纯化或酶动力学的期刊(如*Protein Expression and Purification*, *Biochimica et Biophysica Acta*)。

3. 注意筛选近5-10年文献以获取最新方法。

背景信息

**Background of LIPC Recombinant Protein**

Lipase C, hepatic type (LIPC), also known as hepatic lipase, is a key enzyme encoded by the *LIPC* gene, primarily synthesized in the liver. It plays a critical role in lipid metabolism by hydrolyzing triglycerides and phospholipids in circulating lipoproteins, particularly high-density lipoproteins (HDL) and intermediate-density lipoproteins (IDL). This enzyme facilitates the remodeling of lipoproteins, influencing their uptake and clearance, thereby regulating plasma lipid levels. LIPC’s activity is closely associated with cardiovascular health, as dysregulation contributes to atherosclerosis and metabolic disorders.

Recombinant LIPC protein is produced using biotechnological methods, such as expression in mammalian cell lines (e.g., HEK293 or CHO cells) or microbial systems, followed by purification to ensure high specificity and activity. Its recombinant form retains the native enzyme’s functional domains, including the catalytic triad (Ser-149. Asp-173. His-257) and heparin-binding regions critical for interaction with lipoprotein substrates. Researchers utilize recombinant LIPC to study its enzymatic mechanisms, structure-function relationships, and role in diseases like dyslipidemia.

Additionally, this protein serves as a tool for drug discovery, enabling the screening of inhibitors or activators targeting lipid metabolism pathways. Its application extends to diagnostic assays for evaluating hepatic lipase deficiencies linked to genetic mutations. By providing a standardized and scalable source of functional LIPC, recombinant technology advances both basic research and therapeutic development in cardiometabolic diseases. Studies continue to explore its interplay with other lipases and potential as a biomarker or therapeutic target.

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