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Recombinant Mouse Proprotein Convertase 9/PCSK9 Protein, CF

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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, ...read more

Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Mouse Proprotein Convertase 9/PCSK9 Protein, CF Summary

Details of Functionality
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.
Source
Mouse myeloma cell line, NS0-derived mouse Proprotein Convertase 9/PCSK9 protein
Ser156-Gln694 with a C-terminal 10-His tag; Gln35-Gln155
Accession #
N-terminal Sequence
Ser156 (mature form); No results obtained for pro domain, Gln35 inferred from enzymatic pyroglutamate treatment revealing Asp36
Structure / Form
Pro domain & mature form
Protein/Peptide Type
Recombinant Enzymes
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
14 kDa (pro domain) and 59 kDa (mature form).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
18 kDa (pro domain) and 57-67 kDa (mature form), reducing conditions 
Publications
Read Publications using
9258-SE in the following applications:

Packaging, Storage & Formulations

Storage


Buffer
Supplied as a 0.2 μm filtered solution in Tris, NaCl and Glycerol.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse Proprotein Convertase 9/PCSK9 Protein, CF

  • EC 3.4.21
  • EC 3.4.21.111
  • FH3
  • FH3neural apoptosis regulated convertase 1
  • FHCL3
  • HCHOLA3
  • hypercholesterolemia, autosomal dominant 3
  • LDLCQ1
  • NARC1
  • 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

Background

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).
  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.

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