Analytical Data
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Gene name
FST
- Application
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Alternative Names
FST;Follistatin
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P19883
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Expression Region
30-344aa
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AA Sequence
G NCWLRQAKNG RCQVLYKTEL SKEECCSTGR LSTSWTEEDV NDNTLFKWMI FNGGAPNCIP CKETCENVDC GPGKKCRMNK KNKPRCVCAP DCSNITWKGP VCGLDGKTYR NECALLKARC KEQPELEVQY QGRCKKTCRD VFCPGSSTCV VDQTNNAYCV TCNRICPEPA SSEQYLCGND GVTYSSACHL RKATCLLGRS IGLAYEGKCI KAKSCEDIQC TGGKKCLWDF KVGRGRCSLC DELCPDSKSD EPVCASDNAT YASECAMKEA ACSSGVLLEV KHSGSCNSIS EDTEEEEEDE DQDYSFPISS ILEW
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
FST (Follistatin) recombinant protein research has gained significant attention in the fields of molecular biology and biomedicine due to its critical role in regulating muscle growth, tissue repair, and cellular functions. Originally identified as a specific binding protein for Activin, a member of the TGF-β superfamily, FST inhibits the biological activity of Activin and other related factors, thus playing a pivotal role in modulating various physiological processes, including muscle hypertrophy, follicular development, and inflammation. The therapeutic potential of FST is being explored in various contexts, including muscle-wasting diseases, infertility treatments, and age-related muscle decline. Recent advances in biotechnology have enabled the production of recombinant FST proteins, allowing researchers to study their structure-function relationships and therapeutic applications more effectively. Additionally, FST's ability to counteract the inhibitory effects of myostatin—another crucial regulator of muscle growth—has made it a focal point for developing interventions aimed at enhancing muscle mass and function in both clinical and athletic settings. Through ongoing research, FST recombinant proteins are expected to contribute to the development of novel therapeutic strategies for overcoming muscle-related disorders and optimizing performance in diverse populations. This growing body of work highlights the importance of FST in various biological contexts, emphasizing its potential as a valuable tool in regenerative medicine and performance enhancement.
