ANGPTL4 Human
Description
The Angiopoietin-like Protein 4 His -Tagged Fusion Protein is 25 kDa protein containing 204 amino acid residues of the Angiopoietin-like Protein 4 and 16 additional amino acid residues - His Tag (underlined).
Product Specs
Also known as ANGPTL4, PGAR, or HFARP, FIAF (fasting-induced adipose factor) is an adipocytokine whose expression is increased by fasting, peroxisome proliferator-activated receptor agonists, and hypoxia. ANGPTL4 can be found in both human and mouse blood plasma in its full-length form as well as in a truncated form. Studies have shown that only the full-length form of ANGPTL4 is detectable in human white adipose tissue and SGBS adipocytes. In contrast, truncated ANGPTL4 is the predominant form observed during the differentiation of mouse 3T3-L1 adipocytes. It's worth noting that the truncated form of ANGPTL4 is generated by the human liver. Within human blood plasma, FIAF primarily exists as a truncated form (FIAF-S2), and experimental data indicates that treatment leads to an elevation in its levels. Interestingly, there is interindividual variability observed in the levels of both the truncated and full-length forms of ANGPTL4. However, these levels appear to be unaffected by prolonged periods of semistarvation and do not exhibit any correlation with body mass index.
To reconstitute the lyophilized pellet, dissolve it completely in 0.1M Acetate buffer with a pH of 4. For adjusting the pH to a higher value, it is recommended to dilute the solution extensively with an appropriate buffer to a final concentration of 10 µg/ml. It's important to note that the solubility of this antigen is limited at higher concentrations.
Product Science Overview
Angiopoietin-like Protein 4 (ANGPTL4) is a multifaceted secreted protein that plays a significant role in lipid metabolism, inflammation, and various diseases, including cancer. It belongs to the angiopoietin-like protein family and is encoded by the ANGPTL4 gene. This protein is highly expressed in adipose tissues and the liver, with lower expression levels in the heart, muscle, kidney, and skin .
ANGPTL4 was discovered simultaneously by three different institutions in 2000 and later unified by the HUGO Gene Nomenclature Committee as ANGPTL4 . The protein contains an N-terminal coiled-coil domain and a C-terminal fibrinogen-like domain, which can be proteolytically separated in vivo . The recombinant form of ANGPTL4 is often produced in mouse myeloma cell lines and is available in both carrier-free and carrier-containing formulations .
ANGPTL4 is involved in the regulation of lipid metabolism by inhibiting lipoprotein lipase (LPL) activity, which affects triglyceride (TG) metabolism . It is induced under hypoxic conditions and is a target of peroxisome proliferator-activated receptors . The protein has pleiotropic functions with both anti- and pro-inflammatory properties, making it a key player in various inflammatory diseases .
ANGPTL4 has been implicated in numerous cancers, where it modulates vascular permeability, cancer cell motility, and invasiveness . It is also a diagnostic and prognostic biomarker for hepatocellular carcinoma (HCC) and has potential therapeutic applications in suppressing HCC growth, angiogenesis, and metastasis . Genetic inactivation of ANGPTL4 can significantly reduce the risk of developing coronary artery disease and diabetes .
The therapeutic potential of ANGPTL4 is being explored in various contexts. For instance, human monoclonal antibodies against ANGPTL4 have been shown to reduce circulating TG levels in mice and monkeys . However, there are challenges, such as undesirable effects like lymphadenopathy and ascites observed in animal models .
