
人 PLAAT3 抗体对
01AB00341
Phospholipase A and acyltransferase 3 (PLAAT3) is a member of the PLAAT family of enzymes, which are involved in the formation of N-acylphosphatidylethanolamines (NAPEs) and N-acyl ethanolamines (NAEs), important bioactive lipids with roles in anti-inflammation, fat catabolism, and endocannabinoid signaling. PLAAT3 exhibits N-acyltransferase, lipid binding, and phospholipase activities, specifically catalyzing the transfer of fatty acyl groups from glycerophospholipids to lysophospholipids. Structurally, PLAAT3 has a compact, globular structure stabilized by a network of 17 salt bridges, which contrasts with the more elongated structure of PLAAT4. Suppression of PLAAT3 expression has been shown to reduce adipocyte-related gene expression and lipid accumulation, highlighting its role in lipid metabolism.
| 规格 | 起售价 |
|---|---|
| 登录后可查看 | |
技术参数
- 靶点基因名
- PLAAT3
- 基因别名
- HRASLS3; HREV107; PLA2G16
- 蛋白别名
- phospholipase A and acyltransferase 3; PLAAT3
- UniProt
- P53816
- 物种
- Human
产品详情
- 靶点名称
- PLAAT3
- 蛋白名称
- phospholipase A and acyltransferase 3
- 蛋白别名
- Phospholipase A and acyltransferase 3; Adipose-specific phospholipase A2; AdPLA; Group XVI phospholipase A1/A2; H-rev 107 protein homolog; H-REV107; HREV107-1; HRAS-like suppressor 1; HRAS-like suppressor 3; HRSL3; HREV107-3; Renal carcinoma antigen NY-REN-65
- 靶点基因名
- PLAAT3
- 基因别名
- HRASLS3; HREV107; PLA2G16
- UniProt
- P53816
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Phospholipase A and acyltransferase 3 (PLAAT3) is a member of the PLAAT family of enzymes, which are involved in the formation of N-acylphosphatidylethanolamines (NAPEs) and N-acyl ethanolamines (NAEs), important bioactive lipids with roles in anti-inflammation, fat catabolism, and endocannabinoid signaling. PLAAT3 exhibits N-acyltransferase, lipid binding, and phospholipase activities, specifically catalyzing the transfer of fatty acyl groups from glycerophospholipids to lysophospholipids. Structurally, PLAAT3 has a compact, globular structure stabilized by a network of 17 salt bridges, which contrasts with the more elongated structure of PLAAT4. Suppression of PLAAT3 expression has been shown to reduce adipocyte-related gene expression and lipid accumulation, highlighting its role in lipid metabolism.