Analytical Data
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Gene name
FNDC5
- Application
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Alternative Names
FNDC5；FRCP2；Fibronectin type III domain-containing Protein 5
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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
Q8NAU1
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Expression Region
16-136aa
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AA Sequence
MSYYHHHHHH DYDIPTTENL YFQGAMGSDS PSAPVNVTVR HLKANSAVVS WDVLEDEVVI GFAISQQKKD VRMLRFIQEV NTTTRSCALW DLEEDTEYIV HVQAISIQGQ SPASEPVLFK TPREAEKMAS KNKDEVTMKE MGRNQQLRT
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Molecular Weight
17 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
FNDC5, or Fibronectin Type III Domain-Containing Protein 5, has emerged as a significant target of research due to its roles in various physiological processes, including metabolism, fibrosis, and inflammation. Discovered originally as a myokine secreted by skeletal muscle during physical exercise, FNDC5 has been implicated in the regulation of brown adipose tissue and energy expenditure, effectively linking physical activity to metabolic health. The protein is primarily known for its cleavage product, irisin, which has gained attention for its potential in combating obesity and related metabolic disorders. As interest in FNDC5 increases, researchers are investigating its restructured forms to understand their functional properties, interactions with cellular pathways, and potential therapeutic applications. This focus on FNDC5 recombinant proteins not only aids in elucidating its biological mechanisms but also enhances the development of innovative treatments for metabolic diseases. Overall, the study of FNDC5 recombinant proteins provides crucial insights into the molecular underpinnings of exercise physiology and metabolic regulation.
