>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA. When Recombinant Mouse LDLR (Catalog # 2255-LD) is coated at 2 µg/mL, Recombinant Mouse Proprotein Convertase 9/PCSK9 (Catalog # 9258-SE) binds with an ED50 = 25-150 ng/mL.
Mouse myeloma cell line, NS0-derived Ser156-Gln694 with a C-terminal 10-His tag; Gln35-Gln155
Recombinant Mouse Proprotein Convertase 9/ PCSK9 Binds toRecombinant Mouse LDL R in an ELISA Binding Assay. When Recombinant Mouse LDL R Recombinant Mouse LDL R (Catalog # 2255-LD) is coated at 2 µg/mL, Recombinant Mouse Proprotein Convertase 9/PCSK9 (Catalog # 9258-SE) binds with an ED50 = 25-150 ng/mL.
Background: Proprotein Convertase 9/PCSK9
PCSK9 (proprotein convertase subtilisin kexin 9), also known as NARC-1, is a member of the proteinase K subfamily of subtilisin-related serine endoproteases. It is highly expressed in the liver, intestine, and kidney and plays an important role in regulating LDL R expression and circulating cholesterol levels (1). PCSK9 is synthesized as precursor protein that is autocatalytically cleaved in the endoplasmic reticulum to generate a 14 kDa prodomain and a 60 kDa catalytic domain (2). Within the secretion pathway, the prodomain remains associated with and functions as a chaperone for the catalytic domain. Mouse PCSK9 shares 78% and 93% amino acid identity with human and rat PCSK9, respectively. PCSK9 plays a key role in the regulation of cholesterol metabolism by binding to hepatic LDL R, LRP-1, VLDL R, and Apolipoprotein E R2 and promoting their lysosomal degradation instead of recycling to the plasma membrane (3-8). It can also regulate cholesterol and triglyceride handling in the intestine and adipose tissue (9-11). The ability of PCSK9 to regulate LDL R expression is inhibited by its binding to LDL particles or Annexin A2 or by additional proteolytic cleavage (12-17).
Schulz, R. et al. (2015) Basic Res. Cardiol. 110:4.
Benjannet, S. et al. (2004) J. Biol. Chem. 279:48865.
Lagace, T.A. et al. (2006) J. Clin. Invest. 116:2995.
Grefhorst, A. et al. (2008) J. Lipid Res. 49:1303.
Zhang, D.W. (2007) J. Biol. Chem. 282:18602.
DeVay, R.M. et al. (2013) J. Biol. Chem. 288:10805.
Canuel, M. et al. (2013) PLoS One 8:e64145.
Poirier, S. et al. (2008) J. Biol. Chem. 283:2363.
Levy, E. et al. (2013) Atherosclerosis 227:297.
Le May, C. et al. (2013) Arterioscler. Thromb. Vasc. Biol. 33:1484.
Roubtsova, A. et al. (2011) Arterioscler. Thromb. Vasc. Biol. 31:785.
Kosenko, T. et al. (2013) J. Biol. Chem. 288:8279.
Mayer, G. et al. (2008) J. Biol. Chem. 283:31791.
Benjannet, S. et al. (2006) J. Biol. Chem. 281:30561.
Benjannet, S. et al. (2010) J. Biol. Chem. 285:40965.
Essalmani, R. et al. (2011) J. Biol. Chem. 286:4257.
The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.