Analytical Data
-
Gene name
AGPAT1
- Application
-
Alternative Names
AGPAT1; G15; 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha; 1-acylglycerol-3-phosphate O-acyltransferase 1
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q99943
-
Expression Region
1-283aa
-
AA Sequence
MDLWPGAWMLLLLLFLLLLFLLPTLWFCSPSAKYFFKMAFYNGWILFLAVLAIPVCAVRGRNVENMKILRLMLLHIKYLYGIRVEVRGAHHFPPSQPYVVVSNHQSSLDLLGMMEVLPGRCVPIAKRELLWAGSAGLACWLAGVIFIDRKRTGDAISVMSEVAQTLLTQDVRVWVFPEGTRNHNGSMLPFKRGAFHLAVQAQVPIVPIVMSSYQDFYCKKERRFTSGQCQVRVLPPVPTEGLTPDDVPALADRVRHSMLTVFREISTDGRGGGDYLKKPGGGG
-
Molecular Weight
58.1 KDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
AGPAT1 (1-acylglycerol-3-phosphate O-acyltransferase 1) is an essential enzyme involved in glycerolipid metabolism, playing a crucial role in the synthesis of triglycerides and phospholipids. Mutations in the AGPAT1 gene are linked to various metabolic disorders, particularly serious conditions such as congenital lipodystrophy, which is characterized by an abnormal distribution of body fat and severe insulin resistance. The study of AGPAT1 recombinant protein has gained significant attention in recent years as researchers strive to understand its function and regulation in lipid metabolism and energy homeostasis. By producing AGPAT1 as a recombinant protein, scientists can investigate its enzymatic activity, interaction with other proteins, and potential regulatory mechanisms at the molecular level. This understanding can lead to insights into the pathophysiology of lipid-related diseases and may pave the way for developing therapeutic strategies aimed at treating metabolic disorders associated with AGPAT1 dysfunction. Thus, research on AGPAT1 recombinant protein not only contributes to our fundamental knowledge of lipid biochemistry but also holds promise for advancing medical interventions for metabolic syndromes.
