The encoded 22 kDa protein contains an N-terminal secretion signal and two coiled-coil domains and is a member of the angiopoietin-like (ANGPTL) protein family. However, in contrast to other ANGPTL proteins, ANGPTL8 lacks the C-terminal fibrinogen-like domain, and therefore it is an atypical member of the ANGPTL family. It shares with ANGPTL4 and ANGPTL8 the ability to inhibit the enzyme Lipoprotein lipase (LPL), and its hepatic overexpression causes elevation of circulating Triglyceride levels in mice. In mice ANGPTL8 is secreted by the liver and by adipose tissue. Despite having elevated post-heparin plasma LPL activity, mice lacking ANGPTL8 exhibit markedly decreased uptake of Very low-density lipoprotein-derived fatty acids into white adipose tissue (WAT). The defect in fatty acids uptake by WAT in ANGPTL8-null mice is likely due to the enhanced fatty acid uptake by the heart and skeletal muscle, because of the elevated LPL activity in these two tissues,[13] as suggested by the ANGPTL3-4-8 model.

C19orf80; ANGL8_HUMAN; Angiopoietin-like protein 8; Betatrophin; Lipasin; Refeeding-induced fat and liver protein; PRO1185; PVPA599; RIFL; TD26; Chromosome 19 open reading frame 80; hepatocellular carcinoma-associated gene TD26; Hepatocellular carcinoma-associated protein TD26.

q6uxh0

WB,IHC

WB 1:500-2000
IHC 1:100-500

Human,Mouse

Predicted size: 22 kDa

Mouse

Secreted.

Protein G affinity purified.

Mouse monoclonal

IgG

Liquid

0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Store at +4°C short term. Store at -20°C long term. Avoid freeze / thaw cycle.