Leukotriene A4 Hydrolase/LTA4H Protein, Human (sf9, His)

The jADRB1 protein, a member of the beta-adrenergic receptor family, plays a critical role in mediating the activation of adenylate cyclase by catecholamines through G protein signaling. It exhibits similar affinity for binding to epinephrine and norepinephrine. Moreover, ADRB1 protein facilitates Ras activation via G(s)-alpha- and cAMP-mediated signaling pathways. Interestingly, it is also involved in regulating sleep/wake behaviors. ADRB1 protein directly interacts with RAPGEF2 through its C-terminus PDZ motif and further interacts with GOPC, MAGI3, and DLG4. Moving on to the Leukotriene A4 Hydrolase/LTA4H Protein, it is a bifunctional zinc metalloenzyme that possesses both epoxide hydrolase (EH) and aminopeptidase activities. LTA4H acts as an epoxide hydrolase, catalyzing the conversion of LTA4 to the pro-inflammatory mediator leukotriene B4 (LTB4). Additionally, it demonstrates aminopeptidase activity, specifically targeting N-terminal arginines of various synthetic tripeptides. Apart from its pro-inflammatory EH activity, LTA4H may counteract inflammation through its aminopeptidase activity by inactivating the neutrophil attractant Pro-Gly-Pro (PGP), a bioactive collagen fragment generated by matrix metalloproteinase-9 (MMP9) and prolylendopeptidase (PREPL). Furthermore, LTA4H is involved in the biosynthesis of resolvin E1 and 18S-resolvin E1 from eicosapentaenoic acid, which are lipid mediators with potent anti-inflammatory and pro-resolving actions.