Human ANGPTL4 / angiopoietin-like protein 4 (Fc Tag)

Human ANGPTL4 / angiopoietin-like protein 4 (Fc Tag)

• DataSheet
• Material Safety Data Sheets (MSDS)

Protein with hypoxia-induced expression in endothelial cells. May act as a regulator of angiogenesis and modulate tumorigenesis. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. May exert a protective function on endothelial cells through an endocrine action. It is directly involved in regulating glucose homeostasis, lipid metabolism, and insulin sensitivity. In response to hypoxia, the unprocessed form of the protein accumulates in the subendothelial extracellular matrix (ECM). The matrix-associated and immobilized unprocessed form limits the formation of actin stress fibers and focal contacts in the adhering endothelial cells and inhibits their adhesion. It also decreases motility of endothelial cells and inhibits the sprouting and tube formation (By similarity).

Angiopoietin-related protein 4

PPARG ANGIOPOIETIN RELATED PROTEIN; NG27; SECRETED PROTEIN BK89; UNQ171; PP1158; PGARG; HEPATIC ANGIOPOIETIN-RELATED PROTEIN; PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR (PPAR) GAMMA INDUCED ANGIOPOIETIN-RELATED PROTEIN; TGQTL; 425O18-1; FIAF; ANGPTL2; HARP; FASTING-INDUCED ADIPOSE FACTOR; PGAR; ARP4; FIBRINOGEN/ANGIOPOIETIN-RELATED PROTEIN; NL2; HEPATIC FIBRINOGEN/ANGIOPOIETIN-RELATED PROTEIN; MAJOR HISTOCOMPATIBILITY COMPLEX REGION NG27; BK89; ANGIOPOIETIN-RELATED PROTEIN 4; ANGIOPOIETIN-LIKE PROTEIN 4; HFARP

Q9BY76

ANGPTL4; ARP4; HFARP; PGAR; PP1158; PSEC0166; UNQ171/PRO197

Human Cells

A DNA sequence encoding the human ANGPTL4 (Q9BY76) (Pro166-Ser406) was expressed,with the fused Fc region of human IgG1 at the N-terminus.

Human

The recombinant human ANGPTL4/Fc is a disulfide-linked homodimer. The reduced monomer comprises 501 amino acids and has a predicted molecular mass of 55.5 kDa. The apparent molecular mass of the protein is approximately 65 kDa in SDS-PAGE under reducing conditions due to glycosylation.

> 92 % as determined by SDS-PAGE