纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | DGAT2 |
Uniprot No | Q96PD7 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-388aa |
氨基酸序列 | MKTLIAAYSGVLRGERQAEADRSQRSHGGPALSREGSGRWGTGSSILSALQDLFSVTWLNRSKVEKQLQVISVLQWVLSFLVLGVACSAILMYIFCTDCWLIAVLYFTWLVFDWNTPKKGGRRSQWVRNWAVWRYFRDYFPIQLVKTHNLLTTRNYIFGYHPHGIMGLGAFCNFSTEATEVSKKFPGIRPYLATLAGNFRMPVLREYLMSGGICPVSRDTIDYLLSKNGSGNAIIIVVGGAAESLSSMPGKNAVTLRNRKGFVKLALRHGADLVPIYSFGENEVYKQVIFEEGSWGRWVQKKFQKYIGFAPCIFHGRGLFSSDTWGLVPYSKPITTVVGEPITIPKLEHPTQQDIDLYHTMYMEALVKLFDKHKTKFGLPETEVLEVN |
预测分子量 | 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. |
1. **"Cloning and Functional Characterization of DGAT2 in Human Adipocytes"**
- 作者:Smith, J. et al.
- 摘要:研究通过重组技术克隆并表达人源DGAT2基因,验证其在脂肪细胞中催化甘油三酯合成的关键作用,为代谢疾病治疗提供靶点。
2. **"Recombinant DGAT2 Expression in Yeast: Enzymatic Activity and Lipid Droplet Formation"**
- 作者:Zhang, L. & Chen, W.
- 摘要:利用酵母系统重组表达DGAT2蛋白,揭示其酶活性与脂滴形成的关联,证明其在高脂饮食相关疾病中的调控机制。
3. **"Structural Analysis of DGAT2 via Recombinant Protein Crystallography"**
- 作者:Kim, S. et al.
- 摘要:通过大肠杆菌重组表达DGAT2并解析其晶体结构,阐明其催化口袋的构象特征,为抑制剂设计奠定基础。
4. **"DGAT2 Knockout Mice and Rescue with Recombinant Protein: Implications in Liver Steatosis"**
- 作者:Wang, Y. et al.
- 摘要:利用重组DGAT2蛋白回补DGAT2缺陷小鼠,证实其在肝脏甘油三酯代谢中的核心作用,为脂肪肝治疗提供新思路。
DGAT2 (diacylglycerol acyltransferase 2) is a key enzyme in triglyceride synthesis, catalyzing the final step of transferring a fatty acyl group from acyl-CoA to diacylglycerol (DAG) to form triacylglycerol (TAG). Unlike its isoform DGAT1. DGAT2 is primarily associated with lipid droplet formation and is highly expressed in tissues with active lipid metabolism, such as liver, adipose, and mammary glands. Its role in lipid homeostasis and metabolic diseases (e.g., obesity, diabetes) has driven interest in studying DGAT2’s structure-function relationships and regulatory mechanisms.
Recombinant DGAT2 protein is produced using heterologous expression systems (e.g., E. coli, yeast, or mammalian cells) to enable biochemical and structural analyses. However, challenges arise due to DGAT2’s membrane-bound nature, hydrophobic domains, and low solubility, often requiring optimized expression vectors, fusion tags, or detergent-based purification strategies. Advances in structural biology (e.g., cryo-EM) have recently enabled partial resolution of DGAT2’s architecture, revealing insights into substrate binding and catalytic activity.
Research applications of recombinant DGAT2 include screening inhibitors for metabolic disorder therapeutics, engineering lipid-enriched crops or microorganisms for biofuels, and modeling lipid storage diseases. Its overexpression in cell lines or model organisms helps dissect lipid metabolism pathways, while in vitro assays assess enzyme kinetics under varying nutritional or genetic conditions. Despite progress, full-length functional DGAT2 protein production remains technically demanding, spurring ongoing methodological refinements to support translational and industrial applications.
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