Recombinant Human Follistatin 288 (FS-288) Protein, CF

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human Follistatin 288 (FS-288) 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 0.05‑0.25 μg/mL in the presence of 7.5 ng/mL of recombinant human Activin A.
• Source: Spodoptera frugiperda, Sf 21 (baculovirus)-derived human Follistatin protein
  Gly30-Asn317, with an N-terminal Met
• Accession #: P19883
• N-terminal Sequence: Met
• Protein/Peptide Type: Recombinant Proteins
• Gene: FST
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 31.7 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: 30-40 kDa, reducing conditions

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 Acetonitrile and TFA.
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 100 μg/mL in PBS.

Notes

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

Alternate Names for Recombinant Human Follistatin 288 (FS-288) Protein, CF

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

Background

Follistatin 288 (FST288) is one of three forms of follistatin, a secreted glycoprotein that was first identified as a follicle-stimulating hormone inhibiting substance in ovarian follicular fluid (1, 2). Human follistatin 288 cDNA encodes a 317 amino acid (aa) protein with a 29 aa signal sequence, and a 288 aa mature region. Human FST288 shares 97 - 99% aa identity with corresponding regions of mouse, rat, equine, ovine, porcine and bovine FST. All forms of follistatin, including FST288, FST303 and FST315, contain an N-terminal atypical TGF binding domain and three follistatin domains (FS1 - 3) that contain EGF-like and kazal-like motifs. A highly acidic C-terminal tail is missing in the splice variant FST288, partially present in the proteolytically produced FST303, and full-length in the most abundant form, FST315 (5, 8, 9). FSTs inhibit activins by surrounding activin dimers. FST288 shows the highest affinity for activins due to its extended configuration, while FST315 is in a folded form (2, 8). Expression of the isoforms is restricted such that FST288, which has higher affinity for heparin-sulfated proteoglycans when unbound, is present in tissues while FST315 is the sole form in plasma and ovarian follicular fluid (5, 8, 9). In addition to activin, follistatins regulate the bioavailability of other members of the TGF-beta superfamily, such as BMP6, BMP7 and myostatin (5). Follistatins also regulate hematopoietic stem cell adhesion to fibronectin via FS2, and bind angiogenin via FS2 and FS3 (6, 7). 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). Mice that express only the FST315 isoform survive, but exhibit 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.

Publications for Follistatin (5836-FS/CF)(9)

Publications using 5836-FS/CF

• J Li, Y Qi, K Yang, L Zhu, X Cui, Z Liu Follistatin Is a Novel Chemoattractant for Migration and Invasion of Placental Trophoblasts of Mice Cells, 2022-11-29;11(23):. 2022-11-29 [PMID: 36497076] (Cell Culture, Mouse)
• G Mancinelli, C Torres, N Krett, J Bauer, K Castellano, R McKinney, D Dawson, G Guzman, R Hwang, S Grimaldo, P Grippo, B Jung Role of stromal activin A in human pancreatic cancer and metastasis in mice Scientific Reports, 2021-04-12;11(1):7986. 2021-04-12 [PMID: 33846512] (Reference Standard, Human)
• J Bauer, MAB Emon, JJ Staudacher, AL Thomas, J Zessner-Sp, G Mancinelli, N Krett, MT Saif, B Jung Increased stiffness of the tumor microenvironment in colon cancer stimulates cancer associated fibroblast-mediated prometastatic activin A signaling Sci Rep, 2020-01-09;10(1):50. 2020-01-09 [PMID: 31919369] (Cell Culture, Human)
• Jonas J Staudacher, Cemal Yazici, Timothy Carroll, Jessica Bauer, Jingbo Pang, Nancy Krett, Yinglin Xia, Annette Wilson, Georgios Papachris, Andrea Dirmeier, Claudia Kunst, David C Whitcomb, Giamila Fantuzzi, Barbara Jung Activin in acute pancreatitis: Potential risk-stratifying marker and novel therapeutic target. Scientific Reports, 2017-10-06;0(0):2045-2322. 2017-10-06 [PMID: 28986573] (In Vivo, Mouse)
• JJ Staudacher, J Bauer, A Jana, J Tian, T Carroll, G Mancinelli, Ö Özden, N Krett, G Guzman, D Kerr, P Grippo, B Jung Activin signaling is an essential component of the TGF-? induced pro-metastatic phenotype in colorectal cancer Sci Rep, 2017-07-17;7(1):5569. 2017-07-17 [PMID: 28717230] (Bioassay, Human)
• RG Walker, M Czepnik, EJ Goebel, JC McCoy, A Vujic, M Cho, J Oh, S Aykul, KL Walton, G Schang, DJ Bernard, AP Hinck, CA Harrison, E Martinez-H, AJ Wagers, RT Lee, TB Thompson Structural basis for potency differences between GDF8 and GDF11 BMC Biol, 2017-03-03;15(1):19. 2017-03-03 [PMID: 28257634] (Bioassay, Human)
• Y Choudhury, YC Toh, J Xing, Y Qu, J Poh, L Huan, HS Tan, R Kanesvaran, H Yu, MH Tan Patient-specific hepatocyte-like cells derived from induced pluripotent stem cells model pazopanib-mediated hepatotoxicity Sci Rep, 2017-01-25;7(0):41238. 2017-01-25 [PMID: 28120901] (Bioassay, Human)
• Leddy H, McNulty A, Lee S, Rothfusz N, Gloss B, Kirby M, Hutson M, Cohn D, Guilak F, Liedtke W Follistatin in chondrocytes: the link between TRPV4 channelopathies and skeletal malformations. FASEB J, 2014-02-27;28(6):2525-37. 2014-02-27 [PMID: 24577120] (Bioassay, Chicken)
• Mukhopadhyay A, Chan SY, Lim IJ, Phillips DJ, Phan TT The role of the activin system in keloid pathogenesis. Am. J. Physiol., Cell Physiol., 2006-09-13;292(4):C1331-8. 2006-09-13 [PMID: 16971493] (Bioassay, Human)

Bioinformatics

• Gene Symbol: FST
• Uniprot:
  • P19883()