Analytical Data
-
Gene name
MGLL
- Application
-
Alternative Names
HU-K5, MGLL; MAGL; Monoglyceride Lipase; Lysophospholipase homolog; Lysophospholipase-like; Monoacylglycerol lipase
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q99685
-
Expression Region
Met1~Pro303
-
Molecular Weight
37kDa
-
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
The study of the MGLL (Monoacylglycerol Lipase) recombinant protein has garnered significant attention due to its crucial role in lipid metabolism and potential implications in various pathologies, including obesity, diabetes, and neurodegenerative diseases. MGLL is a serine hydrolase responsible for the hydrolysis of monoacylglycerols into glycerol and free fatty acids, thus regulating endocannabinoid signaling pathways and energy homeostasis. This enzyme's activity influences numerous physiological processes, including pain perception and appetite regulation. Given the increasing prevalence of metabolic disorders and the complexity of endocannabinoid system interactions, researchers are focusing on the structural and functional characterization of MGLL to better understand its mechanisms and therapeutic potential. The generation of recombinant MGLL allows for detailed biochemical analyses, substrate specificity assessments, and the exploration of potential inhibitors, which could pave the way for novel therapeutics targeting MGLL-related pathways. Improvements in recombinant protein expression systems have enabled the production of MGLL in adequate quantities for high-resolution crystallography and functional assays, facilitating insights into its catalytic mechanism and regulatory interactions. Consequently, a comprehensive understanding of MGLL's role in health and disease could lead to innovative treatment strategies to manage conditions associated with dysregulated lipid metabolism and cannabinoid signaling.
