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Recombinant Mouse Serpin F1/PEDF Protein, CF


Recombinant Mouse Serpin F1/PEDF enhances the adhesion of Saos‑2 human osteosarcoma cells to a bovine Collagen I coated plate. The ED50 for this effect is 0.1-0.6 μg/mL.
1 μg/lane of Recombinant Mouse Serpin F1/PEDF was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silver staining, showing R bands at 48.8, 42.5 kDa and NR bands at 140.8, more

Product Details

Reactivity MuSpecies Glossary
Applications Bioactivity

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Recombinant Mouse Serpin F1/PEDF Protein, CF Summary

Details of Functionality
Measured by its ability to enhance the adhesion of Saos‑2 human osteosarcoma cells to bovine Collagen I coated plate. Eth, E.K. et al. (2007) Cancer Gene Therapy. 14:616. The ED50 for this effect is 0.1-0.6 μg/mL.
Mouse myeloma cell line, NS0-derived mouse Serpin F1/PEDF protein
Gln20-Thr417, with a C-­terminal 6-His tag
Accession #
N-terminal Sequence
No results obtained: Gln20 inferred from enzymatic pyroglutamate treatment revealing Asn21.
Protein/Peptide Type
Recombinant Proteins
>95%, by SDS-PAGE with silver staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.


  • Bioactivity
Theoretical MW
45 kDa.
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.
50-56 kDa, reducing conditions
Read Publications using
8295-SF in the following applications:

Packaging, Storage & Formulations

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in PBS and NaCl.
>95%, by SDS-PAGE with silver staining.
Reconstitution Instructions
Reconstitute at 250 μg/mL in steril PBS.


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

Alternate Names for Recombinant Mouse Serpin F1/PEDF Protein, CF

  • Cell proliferation-inducing gene 35 protein
  • EPC-1
  • EPC-1PIG35
  • PEDF
  • PEDFpigment epithelium-derived factor
  • pigment epithelium derived factor), member 1
  • proliferation-inducing protein 35
  • serine (or cysteine) proteinase inhibitor, clade F (alpha-2 antiplasmin
  • Serpin F1
  • serpin peptidase inhibitor, clade F (alpha-2 antiplasmin, pigment epitheliumderived factor), member 1


Serpin Peptidase Inhibitor, clade F (Serpin F1), also called Pigment Epithelium-Derived Factor (PEDF), EPC-1, and PIG35, is a member of the Serpin superfamily of serine protease inhibitors (1-5). This superfamily is comprised of two protein groups with dissimilar functions. One group demonstrates protease inhibition while proteins in the other group display no protease inhibition, but rather, perform diverse functions, such as molecular chaperones, circulating transporters, and tumor suppressors (2). Serpin F1 is part of this latter group. It is a 50 kDa, monomeric phosphoglycoprotein that is comprised of three beta -sheets, 8-10 alpha -helices, and a C-terminal reactive center loop (RCL), a structure common to all Serpins (2-5). However, unlike Serpins that exhibit protease inhibiting activity, the RCL of Serpin F1 does not undergo a conformational change, a prerequisite for anti-protease activity (3, 5). Such cleavage does, however, generate a 46 kDa fragment that possesses nonprotease-associated bioactivity (6). Mouse Serpin F1 displays 88% and 93% amino acid sequence identity with the human and rat orthologs, respectively.

Serpin F1 is a multifunctional protein that is synthesized by multiple cell types and is expressed in many tissues including the retinal pigment epithelium, liver, bone, connective, heart, and adipose tissues (1, 3, 5, 7, 8). It has been shown to bind to several different cell surface molecules including the PEDF Receptor, Laminin Receptor, LRP-6, and the F1 ATP Synthase (5, 9-13). It also has binding affinity for several extracellular matrix components, such as Heparin, Heparin Sulphate, Hyaluronan, and Collagens (5, 3). It is believed that the multiple and varied biological activities attributed to Serpin F1 are due to its interactions with these different cell surface molecules. Serpin F1 has been shown to be involved in neurogenesis, neuronal cell survival, angiogenesis, tumorgenesis, stem cell survival and multipotency, and inflammation (2-5, 10, 12-15). In humans, Serpin F1 has been suggested to play a role in choroidal neovascularization, obesity and insulin resistance, cardiovascular disease, osteogenesis imperfecta, and cancer (3-5, 15-19).

  1. Kozaki, K. et al. (1998) J. Biol. Chem. 273:15125.
  2. Filleur, S. et al. (2009) J. Cell. Biochem. 106:769.
  3. Kawaguchi, T. et al. (2010) Curr. Mol. Med. 10:302.
  4. Chandolu, V. and C.R. Dass (2012) J. Biomed. Biotechnol. 2012:740295.
  5. Becerra, S.P. and V. Notario (2013) Nat. Rev. Cancer 13:258.
  6. Wu, Y.Q. and S.P. Becerra (1996) Invest. Ophthalmol. Vis. Sci. 37:1984.
  7. Singh, V.K. et al. (1998) Mol. Vis. 4:7.
  8. Tombran-Tink, J. and C.J. Barnstable (2004) Biochem. Biophys. Res. Commun. 316:573.
  9. Notari, L. et al. (2006) J. Biol. Chem. 281:38022.
  10. Notari, L. et al. (2010) FEBS J. 277:2192.
  11. Park, K. et al. (2011) Mol. Cell. Biol. 31:3038.
  12. Bernard, A. et al. (2009) J. Biol. Chem. 284:10480.
  13. Matsui, T. et al. (2014) Biochem. Biophys. Res. Commun. 443:847.
  14. Elahy, M. et al. (2012) J. Biomed. Biotechol. 2012:239091.
  15. Chavan, S.S. et al. (2012) Mol. Med. 18:1161.
  16. Wang, P. et al. (2008) Eur. J. Endocrinol. 159:713.
  17. Homan, E.P. et al. (2011) J. Bone Miner. Res. 26:2798.
  18. Taube, A. et al. (2012) Am. J. Physiol. Heart Circ. Physiol. 302:H2148.
  19. Venturi, G. et al. (2012) J. Bone Miner. Res. 27:723.

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Gene Symbol Serpinf1