Analytical Data
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Gene name
FS
- Application
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Alternative Names
FS；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
35-283aa
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AA Sequence
RQAKNGRCQVLYKTELSKEECCSTGRLSTSWTEEDVNDNTLFKWMIFNGG APNCIPCKETCENVDCGPGKKCRMNKKNKPRCVCAPDCSNITWKGPVCGL DGKTYRNECALLKARCKEQPELEVQYQGRCKKTCRDVFCPGSSTCVVDQT NNAYCVTCNRICPEPASSEQYLCGNDGVTYSSACHLRKATCLLGRSIGLA YEGKCIKAKSCEDIQCTGGKKCLWDFKVGRGRCSLCDELCPDSKSDEPV
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Molecular Weight
33 kDa
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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
FS (Fused Silica) recombinant proteins have garnered significant attention in the field of biotechnology and biomedical research due to their unique properties and potential applications. The primary motivation behind researching FS recombinant proteins lies in their ability to mimic naturally occurring proteins while providing enhanced stability and functionality. These proteins are engineered using recombinant DNA technology, allowing for the production of specific protein variants that can be optimized for various applications, such as drug development, vaccine formulation, and diagnostic tools. The versatility of FS recombinant proteins also extends to their use in therapeutic interventions, where they can serve as targeted agents in the treatment of diseases. Furthermore, the use of FS recombinant proteins in research facilitates the understanding of protein-protein interactions, enzymatic activities, and cellular processes, thereby contributing to the advancement of molecular biology. As researchers continue to explore the structure-function relationships of these proteins, the potential for innovative solutions in combating diseases and enhancing biotechnological processes is expanding, making FS recombinant proteins a crucial area of study in the quest for progress in life sciences.
