Recombinant Human Follistatin-like 1 Protein, CF


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Product Details

Reactivity HuSpecies Glossary
Applications Bioactivity

Order Details

Recombinant Human Follistatin-like 1 Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human Follistatin‑like 1/FSTL1 is coated at 2 μg/mL (100 μL/well), the concentration of recombinant human BMP-4 that produces 50% of the optimal binding response is found to be approximately 10-60 ng/mL.
Mouse myeloma cell line, NS0-derived human Follistatin-like 1/FSTL1 protein
Met1-Ile308, with a C-terminal Asp and 10-His tag
Accession #
N-terminal Sequence
Protein/Peptide Type
Recombinant Proteins
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.


Theoretical MW
36.4 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.
45-50 kDa, reducing conditions
Read Publications using
1694-FN 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.
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 200 μg/mL in PBS.


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

Alternate Names for Recombinant Human Follistatin-like 1 Protein, CF

  • Flik
  • FLJ50214
  • Follistatin-like 1
  • Follistatin-like protein 1
  • follistatin-related protein 1
  • Follistatin-related Protein
  • FRP
  • FRPFLJ52277
  • FSL1
  • FSTL1
  • TSC-36


Follistatin‑like 1 (FSL1 or FSTL1), also known as FRP (follistatin‑related protein), Flik (follistatin‑like), and TSC‑36 (TGF‑ beta 1‑stimulated clone 36), is a secreted 45‑55 kDa extracellular glycoprotein belonging to the BM‑40/SPARC/Osteonectin family (1‑3). The human FSL‑1 cDNA encodes 308 amino acids (aa), including a 20 aa signal sequence, a cysteine‑rich Follistatin (EGF- and kazal‑like) domain, two apparently non‑functional EF‑hand calcium‑binding motifs, and a von Willebrand Factor C homology domain (1, 3). Mature human FSL1 shares 94%, 95%, 98% and 99% aa identity with mouse, rat, bovine and equine FSL1, respectively. FSL1 was first identified as a TGF‑ beta ‑induced protein from a mouse osteoblast cell line (4). It is ubiquitously expressed in early mouse development, but is mainly mesenchymal later in development (5). In vitro, FSTL1 interacts directly with BMP‑4, while in vivo, it regulates BMP‑4 signaling during normal lung development, as demonstrated by lethal respiratory failure in mice deleted for FSTL1 (6). In humans, FSL1 is a common rheumatoid arthritis auto‑antigen (2). It is reported to be either pro‑inflammatory due to promoting inflammatory cytokine secretion, or to prevent autoimmune arthritis by inhibiting matrix metalloproteinase (MMP) and prostaglandin expression (7‑10). In muscle and heart, it appears to be protective and promotes endothelial cell functions such as revascularization after ischemia, probably due to promoting expression and activation of the protein kinase AKT1 (11, 12). Cardiac and circulating FSL1 is generally increased in conditions such as heart failure and acute coronary syndrome (12‑14). FSL1 also appears to be a tumor suppressor, showing down‑regulated expression in many human cancers (4, 15, 16). In vitro, it slows proliferation and MMP‑dependent migration, and increases FAS‑dependent apoptosis of tumor cell lines (15).

  1. Zwijsen, A. et al. (1994) Eur. J. Biochem. 225:937.
  2. Tanaka, M. et al. (1998) Int. Immunol. 10:1305.
  3. Hambrook, H.O. et al. (2004) J. Biol. Chem. 279:11727.
  4. Shibanuma, M. et al. (1993) Eur. J. Biochem. 217:13.
  5. Adams, D. et al. (2007) Gene Expr. Patterns 7:491.
  6. Geng, Y et al. (2011) Proc. Natl. Acad. Sci. USA 108:7058.
  7. Clutter, S.D. et al. (2009) J. Immunol. 182:234.
  8. Miyamae, T. et al. (2006) J. Immunol. 177:4758.
  9. Kawabata, D. et al. (2004) Arthritis Rheum. 50:660.
  10. Tanaka, M. et al. (2003) Int. Immunol. 15:71.
  11. Ouchi, N. et al. (2008) J. Biol. Chem. 283:32802.
  12. Oshima, Y. et al. (2008) Circulation 117:3099.
  13. Lara-Pezzi, E. et al. (2008) Endocrinology 149:5822.
  14. Widera, C. et al. (2009) Clin. Chem. 55:1794.
  15. Chan, Q.K. et al. (2009) Carcinogenesis 30:114.
  16. Mashimo, J. et al. (1997) Cancer Lett. 113:213.

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Gene Symbol FSTL1