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| Cat.No | ACP08732 | Target Name | AGPAT2 |
|---|---|---|---|
| Target Synonyms | AGPAT2; 1-acyl-sn-glycerol-3-phosphate acyltransferase beta; 1-acylglycerol-3-phosphate O-acyltransferase 2; 1-AGP acyltransferase 2; 1-AGPAT 2; Lysophosphatidic acid acyltransferase beta; LPAAT-beta | Form | Liquid or Lyophilized powder |
| Expression System | Mammalian cell | Protein Length | Partial |
| Purity | >85% (SDS-PAGE) | Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | O15120 |
|---|
Uniprot Id
O15120
Target Species
Human
Target Name
AGPAT2
Target Full Name
1-acyl-sn-glycerol-3-phosphate acyltransferase beta
Target Function
Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone.
Target Involvement
Congenital generalized lipodystrophy 1 (CGL1)
Target Subcellular Location
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Target Protein Families
1-acyl-sn-glycerol-3-phosphate acyltransferase family
Target Tissue Specificity
Expressed predominantly in adipose tissue, pancreas and liver.
Target Synonyms
AGPAT2; 1-acyl-sn-glycerol-3-phosphate acyltransferase beta; 1-acylglycerol-3-phosphate O-acyltransferase 2; 1-AGP acyltransferase 2; 1-AGPAT 2; Lysophosphatidic acid acyltransferase beta; LPAAT-beta
Target Background
This gene encodes a member of the 1-acylglycerol-3-phosphate O-acyltransferase family. The protein is located within the endoplasmic reticulum membrane and converts lysophosphatidic acid to phosphatidic acid, the second step in de novo phospholipid biosynthesis. Mutations in this gene have been associated with congenital generalized lipodystrophy (CGL), or Berardinelli-Seip syndrome, a disease characterized by a near absence of adipose tissue and severe insulin resistance. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
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