ANGPTL3 (fibrinogen-like domain) (human) (rec.)
|Synonyms||Angiopoietin-like Protein 3; Angiopoietin-5; ANG-5|
|Source/Host||HEK 293 cells|
Fibrinogen-like domain of human ANGPTL3 (aa 224-460) is fused at the N-terminus to a FLAG®-tag.
|Endotoxin Content||<0.01EU/μg purified protein (LAL test).|
for 10µg size: 0.1mg/ml
for 50µg size: 1 mg/ml
10µg size: Reconstitute with 100µl sterile water.
50µg size: Reconstitute with 50µl sterile water.
|Formulation||Lyophilized. Contains PBS.|
|Other Product Data||
UniProt link Q9Y5C1: ANGPTL3 (human) [Precursor]
FLAG is a registered trademark of Sigma-Aldrich Co.
|Shipping and Handling|
|Short Term Storage||+4°C|
|Long Term Storage||-20°C|
After opening, prepare aliquots and store at -20°C.
Avoid freeze/thaw cycles.
Centrifuge lyophilized vial before opening and reconstitution.
For maximum product recovery after thawing, centrifuge the vial before opening the cap.
Stable for at least 6 months after receipt when stored at -20°C.
Working aliquots are stable for up to 3 months when stored at -20°C.
|Product Specification Sheet|
ANGPTL3 (Angiopoietin-like protein 3) regulates angiogenesis and also directly regulates lipid, glucose and energy metabolism. Angiopoietin-like 3 (ANGPTL3) is a regulator of plasma triglyceride (TRG) levels due to its inhibitory action on the activity of lipoprotein lipase (LPL). ANGPTL3 induces angiogenesis by binding to integrin αvβ3. ANGPTL3 is predominantly produced in the liver and can therefore be classified as a hepatokine. In the human plasma, ANGPTL3 is cleaved to release two fragments: a N-terminal coiled-coil domain-containing fragment (aa17-207) important for inhibiting the lipolysis of triglyceride and the C-terminal fibrinogen-like domain-containing fragment (aa208-460).
- Angiopoietin-like-2 and -3 act through their coiled-coil domains to enhance survival and replating capacity of human cord blood hematopoietic progenitors: H.E. Broxmeyer, et al.; Blood Cells Mol. Dis. 48, 25 (2012)
- The Fibrinogen-like Domain of ANGPTL3 Facilitates Lipolysis in 3T3-L1 Cells by Activating the Intracellular Erk Pathway: S. Bini, et al.; Biomolecules 12, 585 (2022)