Recombinant Human Monoglyceride Lipase (MGLL) Protein (GST)

Name: Recombinant Human Monoglyceride Lipase (MGLL) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08916P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Monoglyceride Lipase (MGLL) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q99685
Target Symbol	MGLL
Synonyms	EC 3.1.1.23; HU K5 ; HU-K5; HUK5 ; Lysophospholipase homolog; Lysophospholipase like; Lysophospholipase-like; MAGL; MGL; MGLL; MGLL_HUMAN; Monoacylglycerol lipase; Monoglyceride lipase
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MPEESSPRRTPQSIPYQDLPHLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSLGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRTATAGTASPP
Expression Range	1-303aa
Protein Length	Full Length
Mol. Weight	60.3kDa
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	HGNC: 17038 OMIM: 609699 KEGG: hsa:11343 STRING: 9606.ENSP00000265052 UniGene: PMID: 29379013 RNA interference, specific pharmacological inhibitor JZL-184 and gene knock-in of MAGL were utilized to investigate the effects of MAGL on hepatocellular carcinoma (HCC) cell proliferation, apoptosis, and invasion. MAGL played important roles in both proliferation and invasion of HCC cells. PMID: 27767105 This review summarizes the basics of monoglyceride metabolism and provides an overview on the therapeutic potential of MGL. [Review] PMID: 28213089 MGLL may have a role in progression of gastrointestinal stromal tumors PMID: 27366945 the upregulation of MAGL in hepatocellular carcinoma cells promoted cell growth and invasiveness abilities, and mediated epithelial-mesenchymal transition PMID: 27884159 we clarify the key role of Phe159 and Ile179, two conserved residues within the lid domain, in regulating substrate specificity in MAGL. We conclude by proposing that other structurally related lipases may share this lid-domain-mediated mechanism for substrate specificity. PMID: 28088576 the presence and differential distribution of fatty acid amide hydrolase (FAAH) and monoglyceride lipase (MGLL) in relation to CB1 during the maturation of human oocytes, was investigated. PMID: 26948343 there was evidence that MGLL rs604300 genotype interacts with early life adversity to predict threat-related basolateral amygdala habituation, a neural phenotype linked to the endocannabinoid system and addiction PMID: 26595473 This study unravels a novel mechanism of SND1 function and identifies MGLL as a unique tumor suppressor for HCC. MGLL might function as a homeostatic regulator of Akt restraining its activation. PMID: 26997225 The data highlight specific inter-residue interactions within hMGL PMID: 26555264 Monoacylglycerol lipase sulfenylation might act as an intrinsic neuroprotective mechanism by potentiating 2-AG signaling at CB1 receptors. PMID: 26000748 Molecular dynamics and nudged elastic band simulations were used to explore the conformational transition pathway of the helix alpha4 of human monoacylglycerol lipase. PMID: 25078047 role of monoacylglycerol lipase (MAGL) in the cancer progress PMID: 24633487 Our findings establish that MAGL promotes metastases in nasopharyngeal carcinoma PMID: 25120746 In subcutaneous adipose tissue, DAGL-a mRNA was upregulated and fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase (MAGL) mRNAs were down-regulated in obese subjects, but the diets had no influence. PMID: 24616451 In obese humans, FAAH or MGL activity in adipocytes is not affected by diabetes, dyslipidaemia or other markers of metabolic dysfunction. PMID: 24593280 Mutation of Cys242 was also found to impair inhibition of monoacylglycerol lipase. PMID: 24368842 MGL interaction with a phospholipid membrane bilayer induces regional changes in the enzyme's conformation that favor its recruiting lipophilic substrate from membrane stores to the active site resulting in enhanced MGL catalytic activity. PMID: 23553709 Data indicate that N,N-dimethyl-5-(4-phenoxyphenyl)-2H-tetrazole-2-carboxamide inhibited monoacylglycerol lipase (MAGL) with IC50 0.028 muM. PMID: 23455058 MGL expression declines after peaking in infancy. PMID: 22827915 results suggest that MGL plays a negative regulatory role in phosphatidylinositol-3 kinase/Akt signaling and tumor cell growth PMID: 22349814 No association was found between our inflammatory bowel disease cohort and the candidate single nucleotide polymorphisms for MGL (CD/HC: P=0.37 and UC/HC: P=0.25). PMID: 22664939 MAGL is elevated in androgen-independent versus androgen-dependent human prostate cancer cell lines, and pharmacological or RNA-interference disruption of this enzyme impairs prostate cancer aggressiveness. PMID: 21802006 High MAGL is associated with colorectal cancer. PMID: 21543155 Data present a high-resolution structure of a ligand-bound, soluble form of human monoglyceride lipase. PMID: 21308848 One interval in the FAAH promoter and three intervals in the MGLL gene were associated with high BMI. PMID: 21118518 Arachidonoylglycerol (2-AG) is the most abundant endocannabinoid in the brain and is believed to be hydrolyzed primarily by serine hydrolase monoacylglycerol lipase (MAGL) in a transgenic mouse model with targeted disruption of MAGL. PMID: 20855465 Identification of an active site hydrogen bond network in human monoacylglycerol lipase. PMID: 20464001 An apolar helix covering the active site also gives structural insight into the amphitropic character of MAGL, and likely explains how MAGL interacts with membranes to recruit its substrate. PMID: 19957260 MGL shares the classic fold of the alpha/beta hydrolase family but depicts an unusually large hydrophobic occluded tunnel with a highly flexible lid at its entry and the catalytic triad buried at its end. PMID: 19962385 Study shows that monoacylglycerol lipase (MAGL) is highly expressed in aggressive cancer cells and primary tumors; it regulates a fatty acid network enriched in oncogenic signaling lipids that promotes migration, invasion, survival, and tumor growth. PMID: 20079333 not associated with susceptibility to alcoholism in a Japanese population. PMID: 17621164 full proteomic characterization of hMGL was carried out, which showed (1) an absence of intramolecular disulfide bridges in the functional, recombinant enzyme and (2) the post-translational removal of the enzyme's N-terminal methionine PMID: 18452279 Identification of amino acids critical to the catalytic activity PMID: 18721756 Gene Ontology analysis indicated a significant alteration of oxygen transport (increased hemoglobin gene expression) and lipid metabolism [including monoglyceride lipase and low density lipoprotein receptor-related protein 5 (LRP5) gene]. PMID: 19233690

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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.