• Purity

  >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

• Endotoxin Level

  <0.10 EU per 1 μg of the protein by the LAL method.  

• Activity

  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 ED    ₅₀ = 25-150 ng/mL.

• Source

  Mouse myeloma cell line, NS0-derived Ser156-Gln694 with a C-terminal 10-His tag; Gln35-Gln155

• Accession #

• N-terminal Sequence    
  Analysis

  Ser156 (mature form); No results obtained for pro domain, Gln35 inferred from enzymatic pyroglutamate treatment revealing Asp36

• Structure / Form

  Pro domain & mature form

• Predicted Molecular Mass

  14 kDa (pro domain) and 59 kDa (mature form)

• SDS-PAGE

  18 kDa (pro domain) and 57-67 kDa (mature form), reducing conditions 

Data Images

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).

• References:

1. Schulz, R. et al. (2015) Basic Res. Cardiol. 110:4.

2. Benjannet, S. et al. (2004) J. Biol. Chem. 279:48865.

3. Lagace, T.A. et al. (2006) J. Clin. Invest. 116:2995.

4. Grefhorst, A. et al. (2008) J. Lipid Res. 49:1303.

5. Zhang, D.W. (2007) J. Biol. Chem. 282:18602.

6. DeVay, R.M. et al. (2013) J. Biol. Chem. 288:10805.

7. Canuel, M. et al. (2013) PLoS One 8:e64145.

8. Poirier, S. et al. (2008) J. Biol. Chem. 283:2363.

9. Levy, E. et al. (2013) Atherosclerosis 227:297.

10. Le May, C. et al. (2013) Arterioscler. Thromb. Vasc. Biol. 33:1484.

11. Roubtsova, A. et al. (2011) Arterioscler. Thromb. Vasc. Biol. 31:785.

12. Kosenko, T. et al. (2013) J. Biol. Chem. 288:8279.

13. Mayer, G. et al. (2008) J. Biol. Chem. 283:31791.

14. Benjannet, S. et al. (2006) J. Biol. Chem. 281:30561.

15. Benjannet, S. et al. (2010) J. Biol. Chem. 285:40965.

16. Essalmani, R. et al. (2011) J. Biol. Chem. 286:4257.

17. Han, B. et al. (2014) J. Lipid Res. 55:1505.

• Entrez Gene IDs:

  255738 (Human); 100102 (Mouse); 298296 (Rat)

• Alternate Names:

  EC 3.4.21; EC 3.4.21.111; FH3; FH3neural apoptosis regulated convertase 1; HCHOLA3; hypercholesterolemia, autosomal dominant 3; LDLCQ1; NARC-1; NARC-1convertase subtilisin/kexin type 9 preproprotein; NARC1EC 3.4.21.-; Neural apoptosis-regulated convertase 1; PC9; PCSK9; Proprotein Convertase 9; proprotein convertase subtilisin/kexin type 9; Subtilisin/kexin-like protease PC9