Mouse Recombinant FST protein, His Tag (V2LY-0526-LY8337)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Mouse
Tag
His Tag
Protein Construction
This product is Mouse Recombinant FST protein, His Tag consist of Amino Acid: 1-344 and predicts a molecular mass of 36.1 kDa.
Molecule Mass
36.1 kDa
Sequence
Amino Acid: 1-344
Species
Mouse

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
>98% as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Follistatin
Function
Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH).
Biological Process
BMP signaling pathway Source: Ensembl
Cell differentiation Source: GO_Central
Female gonad development Source: Ensembl
Gamete generation Source: Ensembl
Hair follicle morphogenesis Source: Ensembl
Hematopoietic progenitor cell differentiation Source: UniProtKB
Keratinocyte proliferation Source: Ensembl
Negative regulation of activin receptor signaling pathway Source: UniProtKB
Negative regulation of cell differentiation Source: Ensembl
Negative regulation of transcription by RNA polymerase II Source: UniProtKB
Odontogenesis of dentin-containing tooth Source: Ensembl
Pattern specification process Source: Ensembl
Positive regulation of hair follicle development Source: MGI
Regulation of BMP signaling pathway Source: GO_Central
Skeletal system development Source: Ensembl
Cellular Location
Secreted

Chen, Y. J., Deng, S. M., Chen, H. W., Tsao, C. H., Chen, W. T., Cheng, S. J., ... & Huang, G. J. (2021). Follistatin mediates learning and synaptic plasticity via regulation of Asic4 expression in the hippocampus. Proceedings of the National Academy of Sciences, 118(39), e2109040118.

Panagiotou, G., Ghaly, W., Upadhyay, J., Pazaitou-Panayiotou, K., & Mantzoros, C. S. (2021). Serum follistatin is increased in thyroid cancer and is associated with Adverse tumor characteristics in humans. The Journal of Clinical Endocrinology & Metabolism, 106(5), e2137-e2150.

Pervin, S., Reddy, S. T., & Singh, R. (2021). Novel roles of follistatin/myostatin in transforming growth factor-β signaling and adipose browning: Potential for therapeutic intervention in obesity related metabolic disorders. Frontiers in Endocrinology, 12, 653179.

Sylow, L., Vind, B. F., Kruse, R., Møller, P. M., Wojtaszewski, J. F., Richter, E. A., & Højlund, K. (2020). Circulating follistatin and activin A and their regulation by insulin in obesity and type 2 diabetes. The Journal of Clinical Endocrinology & Metabolism, 105(5), 1343-1354.

Motahari Rad, M., Bijeh, N., Attarzadeh Hosseini, S. R., & Raouf Saeb, A. (2020). The effect of two concurrent exercise modalities on serum concentrations of FGF21, irisin, follistatin, and myostatin in men with type 2 diabetes mellitus. Archives of Physiology and Biochemistry, 1-10.

Han, X., Møller, L. L. V., De Groote, E., Bojsen‐Møller, K. N., Davey, J., Henríquez‐Olguin, C., ... & Sylow, L. (2019). Mechanisms involved in follistatin‐induced hypertrophy and increased insulin action in skeletal muscle. Journal of Cachexia, Sarcopenia and Muscle, 10(6), 1241-1257.

Mehta, N., Gava, A. L., Zhang, D., Gao, B., & Krepinsky, J. C. (2019). Follistatin protects against glomerular mesangial cell apoptosis and oxidative stress to ameliorate chronic kidney disease. Antioxidants & redox signaling, 31(8), 551-571.

Singh, R., Pervin, S., Lee, S. J., Kuo, A., Grijalva, V., David, J., ... & Reddy, S. T. (2018). Metabolic profiling of follistatin overexpression: a novel therapeutic strategy for metabolic diseases. Diabetes, Metabolic Syndrome and Obesity: Targets and Therapy, 65-84.

Zhang, L., Liu, K., Han, B., Xu, Z., & Gao, X. (2018). The emerging role of follistatin under stresses and its implications in diseases. Gene, 639, 111-116.

Tao, R., Wang, C., Stöhr, O., Qiu, W., Hu, Y., Miao, J., ... & White, M. F. (2018). Inactivating hepatic follistatin alleviates hyperglycemia. Nature medicine, 24(7), 1058-1069.

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For research use only. Not intended for any clinical use.

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