Recombinant Human Follistatin (aa 30-344) Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human Follistatin (aa 30-344) Protein, CF Summary

Details of Functionality
Measured by its ability to neutralize Activin-mediated erythroid differentiation of K562 human chronic myelogenous leukemia cells. The ED50 for this effect is 0.01‑0.05 µg/mL in the presence of 7.5 ng/mL of rhActivin A.
Source
Chinese Hamster Ovary cell line, CHO-derived human Follistatin protein
Gly30-Trp344
Accession #
N-terminal Sequence
Gly30
Protein/Peptide Type
Recombinant Proteins
Gene
FST
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
34.7 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.
SDS-PAGE
40-50 kDa, reducing conditions
Publications
Read Publications using
4889-FN/CF in the following applications:

Packaging, Storage & Formulations

Storage
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.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

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

Alternate Names for Recombinant Human Follistatin (aa 30-344) Protein, CF

  • follistatin isoform FST317
  • Follistatin
  • FS
  • FSActivin-binding protein
  • FST

Background

Follistatin (FST) is a secreted glycoprotein that was first identified as a follicle-stimulating hormone inhibiting substance in ovarian follicular fluid. (1, 2). Human Follistatin cDNA encodes a 344 amino acid (aa) protein with a 29 aa signal sequence, an N-terminal atypical TGF binding domain, three Follistatin domains that contain EGF-like and kazal-like motifs, and a highly acidic C-terminal tail. The first Follistatin domain (FS1) contains a heparin binding site, while FS1 and FS2 are most critical for activin binding and neutralization (3, 4). In addition to activin, Follistatin regulates bioavailability of many non-TGF-beta members of the TGF-beta superfamily, such as BMP6, BMP7 and myostatin (5). It also regulates hematopoietic stem cell adhesion to fibronectin via FS2, and binds angiogenin via FS2 and FS3 (6, 7). Some Follistatin binding partners will also bind Follistatin-like proteins such as FSL-3 (3, 5, 6). Of three Follistatin isoforms, the full-length mature Follistatin (FST315) is the most abundant and the sole form in plasma, but has lower binding affinity for both activins and heparins than alternative isoforms (5, 8, 9). The acidic tail is missing in the splice variant FST288 which shows the highest affinity for activins, while a partial tail exists in the proteolytically produced FST303, which shows intermediate activin affinity (5, 8, 9). FST315 shares 98% aa identity with mouse, rat, equine and ovine FST, 99% with porcine and 97% with bovine FST. Genetic deletion of Follistatin in mice, or expression of only the FST288 form, is perinatally lethal due to defects of lung, skin and musculoskeletal system (10). Expression of only the FST315 isoform allows survival, with defects in vascularization and female fertility (10).

  1. Shimasaki, S. et al. (1988) Proc. Natl. Acad. Sci. USA 85:4218. 
  2. Thompson, T.B. et al. (2005) Dev. Cell 9:535. 
  3. Sidis, Y. et al. (2005) Endocrinology 146:130. 
  4. Keutmann, H.T. et al. (2004) Mol. Endocrinol. 18:228. 
  5. Sidis, Y. et al. (2006) Endocrinology 147:3586. 
  6. Maguer-Satta, V. et al. (2006) Exp. Cell Res. 312:434.
  7. Gao, X. et al. (2007) FEBS Lett. 581:5505.
  8. Lerch, T.F. et al. (2007) J. Biol. Chem. 282:15930.
  9. Schneyer, A.L. et al. (2004) J. Clin. Endocrinol. Metab. 89:5067.
  10. Lin, S-Y. et al. (2008) Mol. Endocrinol. 22:415.

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Publications for Follistatin (4889-FN/CF)(3)

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Bioinformatics

Gene Symbol FST
Uniprot