ANGPTL4/Angiopoietin-related 4 Protein, Human (GST)

ANGPTL4 protein mediates lipoprotein lipase (LPL) inactivation, regulating triglyceride clearance and lipid metabolism. It also affects glucose homeostasis, insulin sensitivity, endothelial cell function, and angiogenesis. Cleaved ANGPTL4 is more active in LPL inactivation, highlighting its multifaceted role in metabolic and vascular regulation. ANGPTL4/Angiopoietin-related 4 Protein, Human (GST) is the recombinant human-derived ANGPTL4/Angiopoietin-related 4 protein, expressed by E. coli , with N-GST labeled tag.

The ANGPTL4/Angiopoietin-related 4 protein functions as a mediator in the inactivation of lipoprotein lipase (LPL), playing a crucial role in the regulation of triglyceride clearance from the blood serum and lipid metabolism. Additionally, it is implicated in the potential regulation of glucose homeostasis and insulin sensitivity. ANGPTL4 inhibits endothelial cell proliferation, migration, and tubule formation, thereby reducing vascular leakage. It also interferes with the adhesion of endothelial cells to the extracellular matrix, inhibiting the reorganization of the actin cytoskeleton, formation of actin stress fibers, and focal adhesions. In certain contexts, ANGPTL4 may modulate angiogenesis related to tumor development. The cleaved form of ANGPTL4 exhibits higher activity in LPL inactivation compared to the uncleaved protein, highlighting its multifaceted role in metabolic and vascular regulation.

Human

E. coli

N-GST

Q9BY76-1 (V28-E403)

51129  [NCBI]

VQSKSPRFASWDEMNVLAHGLLQLGQGLREHAERTRSQLSALERRLSACGSACQGTEGSTDLPLAPESRVDPEVLHSLQTQLKAQNSRIQQLFHKVAQQQRHLEKQHLRIQHLQSQFGLLDHKHLDHEVAKPARRKRLPEMAQPVDPAHNVSRLHRLPRDCQELFQVGERQSGLFEIQPQGSPPFLVNCKMTSDGGWTVIQRRHDGSVDFNRPWEAYKAGFGDPHGEFWLGLEKVHSITGDRNSRLAVQLRDWDGNAELLQFSVHLGGEDTAYSLQLTAPVAGQLGATTVPPSGLSVPFSTWDQDHDLRRDKNCAKSLSGGWWFGTCSHSNLNGQYFRSIPQQRQKLKKGIFWKTWRGRYYPLQATTMLIQPMAAE

69.6 kDa

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

<1 EU/μg, determined by LAL method.