Recombinant Mouse Monoglyceride Lipase (MGLL) Protein (His-SUMO)

Name: Recombinant Mouse Monoglyceride Lipase (MGLL) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-08088P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Mgll.

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Product Overview

Description	Recombinant Mouse Monoglyceride Lipase (MGLL) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O35678
Target Symbol	MGLL
Synonyms	MgllMonoglyceride lipase; MGL; EC 3.1.1.23; Monoacylglycerol lipase; MAGL
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MPEASSPRRTPQNVPYQDLPHLVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLAAKLLNFVLPNMTLGRIDSSVLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRIAAAGAGCPP
Expression Range	1-303aa
Protein Length	Full Length
Mol. Weight	49.4kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes the endocannabinoid 2-arachidonoylglycerol, and thereby contributes to the regulation of endocannabinoid signaling, nociperception and perception of pain. Regulates the levels of fatty acids that serve as signaling molecules and promote cancer cell migration, invasion and tumor growth.
Subcellular Location	Cytoplasm, cytosol. Membrane; Peripheral membrane protein.
Protein Families	AB hydrolase superfamily, Monoacylglycerol lipase family
Database References	KEGG: mmu:23945 STRING: 10090.ENSMUSP00000127374 UniGene: PMID: 27775008 Results provide evidence that MGL deficiency causes complex changes in cholesterol metabolism and in the regulation of gut transit. PMID: 28380440 N-arachidonoyl ethanolamine and 2-arachidonoyl glycerol hydrolyzing enzymes, FAAH and MAGL, and the CB1 receptor link the endocannabinoid system to broader lipid signaling networks in contrasting ways, potentially altering neurotransmission and behavior independently of cannabinoid receptor signaling. PMID: 27109320 Results suggest that neuronal and astrocytic MAGL collaborate to terminate endocannabinoid-mediated synaptic suppression and prompt synapse-specificity of endocannabinoid signaling in the cerebellum. PMID: 27182552 Activities of adipose triglyceride lipase (ATGL), hormone sensitive lipolitic enzyme (HSL) and monoacylglycerol lipase (MGL) were significantly higher (51 %, 38 %, 49 %) in the DE group than the HF group (p < 0.05). MGL, there were no differences between the CO group, HF group, and DC group, with the DE group (70 %) being significantly higher (p < 0.05). PMID: 27596982 MGL in astrocytes is an important regulator of 2-arachidonoylglyerol levels, arachidonic acid availability, and neuroinflammation. PMID: 26565024 Genetic and pharmacological ablation of Magl attenuated centrally-mediated fever response. PMID: 26287872 the results indicate that global MGL deletion leads to systemic changes that produce a leaner phenotype and an improved serum metabolic profile. PMID: 25842377 This study showed that Genetic deletion of monoacylglycerol lipase leads to impaired cannabinoid receptor CBR signaling and anxiety-like behavior. PMID: 26223500 Suggest that organophosphate agents induce plasma hypertriglyceridemia in mouse through single or dual inhibition of FAAH or/and MAGL, apparently leading to overstimulation of cannabinoid signal regulating energy metabolism. PMID: 24361246 Inactivation of Monoacylglycerol lipase robustly suppressed production and accumulation of beta-amyloid (Abeta) associated with reduced expression of beta-site amyloid precursor protein cleaving enzyme 1 (BACE1) in a mouse model of Alzheimer's disease. PMID: 23122958 Data indicate that nerve growth factor (NGF) controls monoacylglycerol lipase (MGL) degradation in vitro and in vivo. PMID: 23319656 The results therefore suggest a role for intestinal MGL in whole body energy balance via regulation of food intake as well as metabolic rate. PMID: 22937137 MGL regulates 2-arachidonoylglycerol signaling rather broadly within a certain range of neural tissue, although MGL expression is heterogeneous and limited to a subset of nerve terminals and astrocytes. PMID: 22783023 results indicate that genetic deletion of MAGL causes profound changes in eCB signaling, long-term synaptic plasticity, and learning behavior. PMID: 21940435 pathway exists in brain where MAGL hydrolyzes 2-arachidonoylglycerol to generate arachidonate precursor pool for neuroinflammatory prostaglandins; found MAGL as metabolic node coupling endocannabinoid to prostaglandin signaling networks in nervous system PMID: 22021672 MGL deficiency impairs lipolysis and attenuates diet-induced insulin resistance PMID: 21454566 MAGL is the major regulator of 2- arachidonoylglycerol (2-AG) levels and signaling. PMID: 20855465 spatially confined MGL activity generates a 2-arachidonoyl glycerol sensing microdomain and configures 2-arachidonoyl glycerol signaling to promote axonal growth PMID: 20962221 sustained inactivation of monoacylglycerol lipase impairs specific endocannabinoid-mediated forms of synaptic plasticity; ligand diversification may be important for shaping the distinct functions and properties of endocannabinoid signaling pathways PMID: 20729846 Astrocytes express monoacylglycerol lipase, the main hydrolyzing enzyme of 2-arachidonoylglycerol. Pharmacological inhibition of MGL potentiates ATP-induced 2-AG production. PMID: 15371507 analysis of developmental and nutritional regulation of monoacylglycerol lipase and monoacylglycerol acyltransferase PMID: 17848545

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.