Monoglyceride lipase Protein, Rat (P.pastoris, His)

Monoglyceride lipase is a key enzyme in lipid metabolism and plays a key role in converting monoacylglycerols into free fatty acids and glycerol, contributing to important cellular processes. In addition to being involved in lipid metabolism, this enzyme also hydrolyzes the endocannabinoid 2-arachidonoylglycerol, thereby affecting the complex regulation of endocannabinoid signaling, nociception, and pain perception. Monoglyceride lipase Protein, Rat (P.pastoris, His) is the recombinant rat-derived Monoglyceride lipase protein, expressed by P. pastoris , with N-His labeled tag. The total length of Monoglyceride lipase Protein, Rat (P.pastoris, His) is 303 a.a., with molecular weight of ~35.5 kDa.

Monoglyceride lipase (MGLL) is a pivotal enzyme with diverse functions in lipid metabolism and signaling pathways. It plays a central role in converting monoacylglycerides into free fatty acids and glycerol. Additionally, MGLL is involved in the hydrolysis of the endocannabinoid 2-arachidonoylglycerol, contributing to the regulation of endocannabinoid signaling and influencing nociperception and pain perception. Beyond its role in lipid metabolism, MGLL is implicated in the modulation of fatty acid levels, acting as signaling molecules that facilitate cancer cell migration, invasion, and tumor growth (By similarity). The multifunctional nature of Monoglyceride lipase underscores its importance in various physiological processes, including lipid homeostasis, pain regulation, and potential implications in cancer progression.

Rat

P. pastoris

N-His

Q8R431 (1M-303P)

29254  [NCBI]

MPEASSPRRTPQNVPYQDLPHLVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDLLQHVNTVQKDYPEVPVFLLGHSMGGAISILAAAERPTHFSGMILISPLILANPESASTLKVLAAKLLNFVLPNISLGRIDSSVLSRNKSEVDLYNSDPLICHAGVKVCFGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSQDKTLKMYEGAYHVLHKELPEVTNSVLHEINTWVSHRIAVAGARCLP

Approximately 35.5 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.