抗人 MID1IP1 抗体对
01AB01993
MID1 interacting protein 1 (MID1IP1), also known as S14R, is a key regulator of hepatic lipogenesis and fatty acid biosynthesis. It functions primarily by up-regulating the activity of acetyl-CoA carboxylase (ACACA), the rate-limiting enzyme in the production of malonyl-CoA, thereby supporting the efficient synthesis of triacylglycerols, diacylglycerols, and phospholipids. Beyond its metabolic role, MID1IP1 localizes to the microtubule cytoskeleton and cytosol, where it is involved in the stabilization of microtubules and the negative regulation of microtubule depolymerization. It acts as an enzyme activator and is capable of identical protein binding to form functional complexes. While it shares homology with the thyroid hormone-responsive protein (THRSP), MID1IP1 specifically coordinates the metabolic flux required for lipid accumulation in the liver. Its role in maintaining microtubule integrity further suggests a dual function in both cellular architecture and metabolic signaling.
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技术参数
- 靶点基因名
- MID1IP1
- 基因别名
- MIG12
- 蛋白别名
- MID1 interacting protein 1; MID1IP1
- UniProt
- Q9NPA3
- 物种
- Human
产品详情
- 靶点名称
- MID1IP1
- 蛋白名称
- MID1 interacting protein 1
- 蛋白别名
- Mid1-interacting protein 1; Gastrulation-specific G12-like protein; Mid1-interacting G12-like protein; Protein STRAIT11499; Spot 14-related protein; S14R; Spot 14-R
- 靶点基因名
- MID1IP1
- 基因别名
- MIG12
- UniProt
- Q9NPA3
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
MID1 interacting protein 1 (MID1IP1), also known as S14R, is a key regulator of hepatic lipogenesis and fatty acid biosynthesis. It functions primarily by up-regulating the activity of acetyl-CoA carboxylase (ACACA), the rate-limiting enzyme in the production of malonyl-CoA, thereby supporting the efficient synthesis of triacylglycerols, diacylglycerols, and phospholipids. Beyond its metabolic role, MID1IP1 localizes to the microtubule cytoskeleton and cytosol, where it is involved in the stabilization of microtubules and the negative regulation of microtubule depolymerization. It acts as an enzyme activator and is capable of identical protein binding to form functional complexes. While it shares homology with the thyroid hormone-responsive protein (THRSP), MID1IP1 specifically coordinates the metabolic flux required for lipid accumulation in the liver. Its role in maintaining microtubule integrity further suggests a dual function in both cellular architecture and metabolic signaling.