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Human Angiopoietin-like 3 / ANGPTL3 Protein  pdf  pdf  pdf


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Synonym

ANGPTL3, ANGPT5, ANG-5, Angiopoietin-5, FHBL2

Source

Recombinant Human ANGPTL3 / ANGPT5 Protein (rh ANGPTL3 /ANGPT5) Ser 17 - Pro 220 (Accession # NP_055310) was produced in human 293 cells (HEK293) at ACROBiosystems.

Molecular Characterization

rh ANGPTL3 /ANGPT5 is fused with a polyhistidine tag at the C-terminus, and has a calculated MW of 24.6 kDa. The predicted N-terminus is Ser 17. DTT-reduced Protein migrates as 26-38 kDa in SDS-PAGE due to glycosylation.

Endotoxin

Less than 1.0 EU per μg of the rh ANGPTL3 /ANGPT5 by the LAL method.

Purity

>95% as determined by reduced SDS-PAGE.

Formulation

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally Mannitol or Trehalose are added as protectants before lyophilization.

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Reconstitution

See Certificate of Analysis for reconstitution instructions and specific concentrations.

Storage

Avoid repeated freeze-thaw cycles.

No activity loss was observed after storage at:
In lyophilized state for 1 year (4oC); After reconstitution under sterile conditions for 3 months (-70oC).

 

SDS-PAGE


Recombinant Human ANGPTL3 / ANGPT5 Protein
The purity of rh ANGPTL3 /ANGPT5 was determined by DTT-reduced (+) SDS-PAGE and staining overnight with Coomassie Blue.
 
 

Background

Angiopoietin-like protein 3 (ANGPTL3) is also known as Angiopoietin-related protein 3, Angiopoietin-5 (ANGPT5 / ANG-5), is a member of the angiopoietin-like family of secreted factors. ANGPTL3 / ANGPT5 is predominantly expressed in the liver, and has the characteristic structure of angiopoietins, consisting of a signal peptide, N-terminal coiled-coil domain and the C-terminal fibrinogen (FBN)-like domain. The FBN-like domain in angiopoietin-like 3 protein was shown to bind alpha-5/beta-3 integrins, and this binding induced endothelial cell adhesion and migration. This protein may also play a role in the regulation of angiogenesis. Angptl3 also acts as dual inhibitor of lipoprotein lipase (LPL) and endothelial lipase (EL), and increases plasma triglyceride and HDL cholesterol in rodents. ANGPTL3 inhibit endothelial lipase to catalyze HDL-phospholipid and increase HDL-PL levels. Circulating PL-riched HDL particles have high cholesterol efflux abilities.

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References

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