Recombinant human ANGPTL3 protein is a Human Full Length protein, in the 17 to 460 aa range, expressed in CHO, with >98% purity, < 1 EU/µg endotoxin level and suitable for ELISA, HPLC, SDS-PAGE, FuncS.
S R I D Q D N S S F D S L S P E P K S R F A M L D D V K I L A N G L L Q L G H G L K D F V H K T K G Q I N D I F Q K L N I F D Q S F Y D L S L Q T S E I K E E E K E L R R T T Y K L Q V K N E E V K N M S L E L N S K L E S L L E E K I L L Q Q K V K Y L E E Q L T N L I Q N Q P E T P E H P E V T S L K T F V E K Q D N S I K D L L Q T V E D Q Y K Q L N Q Q H S Q I K E I E N Q L R R T S I Q E P T E I S L S S K P R A P R T T P F L Q L N E I R N V K H D G I P A E C T T I Y N R G E H T S G M Y A I R P S N S Q V F H V Y C D V I S G S P W T L I Q H R I D G S Q N F N E T W E N Y K Y G F G R L D G E F W L G L E K I Y S I V K Q S N Y V L R I E L E D W K D N K H Y I E Y S F Y L G N H E T N Y T L H L V A I T G N V P N A I P E N K D L V F S T W D H K A K G H F N C P E G Y S G G W W W H D E C G E N N L N G K Y N K P R A K S K P E R R R G L S W K S Q N G R L Y S I K S T K M L I H P T D S E S F E H H H H H H H H
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application HPLC | Reactivity Reacts | Dilution info - | Notes - |
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes Migrates by SDS-PAGE analysis at an apparent molecular weight of 62 kDa. |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
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Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism (PubMed:11788823, PubMed:12909640, PubMed:23661675, PubMed:25495645). Proposed to play a role in the trafficking of energy substrates to either storage or oxidative tissues in response to food intake (By similarity). Has a stimulatory effect on plasma triglycerides (TG), which is achieved by suppressing plasma TG clearance via inhibition of LPL activity. The inhibition of LPL activity appears to be an indirect mechanism involving recruitment of proprotein convertases PCSK6 and FURIN to LPL leading to cleavage and dissociation of LPL from the cell surface; the function does not require ANGPTL3 proteolytic cleavage but seems to be mediated by the N-terminal domain, and is not inhibited by GPIHBP1 (PubMed:12097324, PubMed:19318355, PubMed:20581395). Can inhibit endothelial lipase, causing increased plasma levels of high density lipoprotein (HDL) cholesterol and phospholipids (PubMed:17110602, PubMed:19028676). Can bind to adipocytes to activate lipolysis, releasing free fatty acids and glycerol (PubMed:12565906). Suppresses LPL specifically in oxidative tissues which is required to route very low density lipoprotein (VLDL)-TG to white adipose tissue (WAT) for storage in response to food; the function may involve cooperation with circulating, liver-derived ANGPTL8 and ANGPTL4 expression in WAT (By similarity). Contributes to lower plasma levels of low density lipoprotein (LDL)-cholesterol by a mechanism that is independent of the canonical pathway implicating APOE and LDLR. May stimulate hypothalamic LPL activity (By similarity). ANGPTL3(17-221). In vitro inhibits LPL activity; not effective on GPIHBP1-stabilized LPL. Involved in angiogenesis. Binds to endothelial cells via integrin alpha-V/beta-3 (ITGAV:ITGB3), activates FAK, MAPK and Akt signaling pathways and induces cell adhesion and cell migration (PubMed:11877390). Secreted from podocytes, may modulate properties of glomerular endothelial cells involving integrin alpha-V/beta-3 and Akt signaling (PubMed:18535744). May increase the motility of podocytes. May induce actin filament rearrangements in podocytes implicating integrin alpha-V/beta-3 and Rac1 activation. Binds to hematopoietic stem cells (HSC) and is involved in the regulation of HSC activity probably implicating down-regulation of IKZF1/IKAROS (By similarity).
ANGPT5, UNQ153/PRO179, ANGPTL3, Angiopoietin-related protein 3, Angiopoietin-5, Angiopoietin-like protein 3, ANG-5
Recombinant human ANGPTL3 protein is a Human Full Length protein, in the 17 to 460 aa range, expressed in CHO, with >98% purity, < 1 EU/µg endotoxin level and suitable for ELISA, HPLC, SDS-PAGE, FuncS.
Constituents: 0.14% Sodium phosphate
Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism (PubMed:11788823, PubMed:12909640, PubMed:23661675, PubMed:25495645). Proposed to play a role in the trafficking of energy substrates to either storage or oxidative tissues in response to food intake (By similarity). Has a stimulatory effect on plasma triglycerides (TG), which is achieved by suppressing plasma TG clearance via inhibition of LPL activity. The inhibition of LPL activity appears to be an indirect mechanism involving recruitment of proprotein convertases PCSK6 and FURIN to LPL leading to cleavage and dissociation of LPL from the cell surface; the function does not require ANGPTL3 proteolytic cleavage but seems to be mediated by the N-terminal domain, and is not inhibited by GPIHBP1 (PubMed:12097324, PubMed:19318355, PubMed:20581395). Can inhibit endothelial lipase, causing increased plasma levels of high density lipoprotein (HDL) cholesterol and phospholipids (PubMed:17110602, PubMed:19028676). Can bind to adipocytes to activate lipolysis, releasing free fatty acids and glycerol (PubMed:12565906). Suppresses LPL specifically in oxidative tissues which is required to route very low density lipoprotein (VLDL)-TG to white adipose tissue (WAT) for storage in response to food; the function may involve cooperation with circulating, liver-derived ANGPTL8 and ANGPTL4 expression in WAT (By similarity). Contributes to lower plasma levels of low density lipoprotein (LDL)-cholesterol by a mechanism that is independent of the canonical pathway implicating APOE and LDLR. May stimulate hypothalamic LPL activity (By similarity).
O-glycosylated at Thr-226 by GALNT2; blocks processing and activation by proprotein convertases.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
ANGPTL3 also known as angiopoietin-like protein 3 or betatrophin is a protein that functions mechanistically in lipid metabolism. It consists of approximately 70 kDa mass and is expressed mainly in the liver. ANGPTL3 is synthesized and secreted as a glycoprotein and it undergoes post-translational modifications important for its function. The protein exists predominantly in a monomeric form in circulation.
ANGPTL3 inhibits lipoprotein lipase (LPL) activity to regulate plasma lipid levels. It independently interacts with lipids and facilitates the storage of triglycerides making it an important modulator of lipid metabolism. ANGPTL3 does not form a stable complex with other proteins but modulates the presence and stability of LPL on the endothelial surface reducing lipid clearance. ANGPT1 ELISA can measure ANGPTL3 levels as part of routine assays including ANGPTL3 ELISA and beta-trophin ELISA.
ANGPTL3 plays a central role in the lipid metabolism and energy homeostasis pathways. In the lipid metabolism pathway ANGPTL3's ability to inhibit LPL links it to other proteins involved in lipid transport and storage such as LDL and HDL particles. Another related protein ANGPTL4 shares similar functions with ANGPTL3 indicating a level of redundancy and regulation within these pathways. ANGPTL3 like ANGPTL4 is a significant player in balancing lipid processing and storage.
ANGPTL3 strongly associates with hyperlipidemia and atherosclerosis. Abnormalities in ANGPTL3 levels can lead to altered lipid profiles raising the risk for cardiovascular diseases. Familial combined hypolipidemia involves mutations in the ANGPTL3 gene leading to drastically lower lipid levels. Disorders such as hypercholesterolemia also demonstrate connections with ANGPTL3 highlighting its role in lipid imbalance. These associations make the anti-ANGPTL3 antibodies important for the study and treatment of such lipid disorders.
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