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The antibody against ANGPTL3 was raised in rabbit using the Human ANGPTL3 as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, WB, IHC.
The antibody against ANGPTL3 was raised in rabbit using the Human ANGPTL3 as the immunogen. This antibody exists as a non-conjugated isotype IgG, Antigen affinity purified. This antibody has been validated on ELISA, WB, IHC.
$600.00
| Cat.No | ADC-54128A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | ANGPTL3 |
| Form | Liquid | Species Reactivity | Human, Mouse, Rat |
| Isotype | IgG | Storage Buffer | 50% Glycerol, Avoid freeze / thaw cycles., PBS with 0.1% Sodium Azide |
| Purification Method | Antigen affinity purified | Conjugate | Non-conjugated |
| Application | ELISA, IHC, WB | Storage | Upon receipt |
| Immunogen Description | Human ANGPTL3 | Target Species | Human |
|---|---|---|---|
| Immunogen Sequence | Complete sequences for the immunogen, target protein, and peptides are available upon request. | Uniprot ID | Q9Y5C1 |
Uniprot Id
Q9Y5C1
Target Species
Human
Target Name
ANGPTL3
Target Full Name
Angiopoietin-related protein 3
Target Function
Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism. Proposed to play a role in the trafficking of energy substrates to either storage or oxidative tissues in response to food intake. 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. Can inhibit endothelial lipase, causing increased plasma levels of high density lipoprotein (HDL) cholesterol and phospholipids. Can bind to adipocytes to activate lipolysis, releasing free fatty acids and glycerol. 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. 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.; 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. Secreted from podocytes, may modulate properties of glomerular endothelial cells involving integrin alpha-V/beta-3 and Akt signaling. 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.
Target Involvement
Hypobetalipoproteinemia, familial, 2 (FHBL2)
Target Subcellular Location
Secreted. Cell projection, lamellipodium.
Target Tissue Specificity
Expressed principally in liver. Weakly expressed in kidney. Binds to adipocytes. Increased expression and colocalization with activated ITGB3 in glomeruli of patients with nephrotic syndrome showing effaced podocyte foot processes (at protein level).
Target Synonyms
ANG 5; ANG-5; ANG5; Angiopoietin 5; Angiopoietin like 3; Angiopoietin related protein 3; Angiopoietin-5; Angiopoietin-like protein 3; Angiopoietin-related protein 3; ANGL3_HUMAN; ANGPT5; ANGPTL3; ANL3; FHBL2; OTTHUMP00000010719; UNQ153/PRO179
Target Background
This gene encodes a member of a family of secreted proteins that function in angiogenesis. The encoded protein, which is expressed predominantly in the liver, is further processed into an N-terminal coiled-coil domain-containing chain and a C-terminal fibrinogen chain. The N-terminal chain is important for lipid metabolism, while the C-terminal chain may be involved in angiogenesis. Mutations in this gene cause familial hypobetalipoproteinemia type 2.
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