Analytical Data
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Gene name
GDF15
- Application
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Alternative Names
GDF15；MIC1；PDF;Growth/differentiation factor 15
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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
Q99988
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Expression Region
197-308aa
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AA Sequence
ARNGDHCPLGPGRCCRLHTVRASLEDLGWADWVLSPREVQVTMCIGACPS QFRAANMHAQIKTSLHRLKPDTVPAPCCVPASYNPMVLIQKTDTGVSLQT YDDLLAKDCHCI
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Molecular Weight
12 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
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Protein Description
GDF15, or Growth Differentiation Factor 15, is a member of the transforming growth factor-beta (TGF-β) superfamily and plays a critical role in various physiological and pathological processes, including inflammation, metabolism, and cellular stress response. Elevated levels of GDF15 have been associated with several diseases, including cardiovascular conditions, cancer, and metabolic disorders, making it a biomarker of interest for disease diagnosis and prognosis. Research has revealed that GDF15 is produced in response to stressors such as injury or inflammation, influencing cellular communication and adaptation. The recombinant protein form of GDF15 facilitates detailed studies into its biological functions, signaling pathways, and potential therapeutic applications. By using the recombinant protein, researchers can analyze the specific interactions of GDF15 with its receptors and downstream signaling molecules, providing insights into its role in various disease states. Additionally, recombinant GDF15 is being explored for its potential as a therapeutic agent, offering possibilities for developing treatments that modulate its expression or activity to mitigate disease progression. Understanding the mechanisms by which GDF15 exerts its effects may lead to novel therapeutic strategies in managing conditions where its dysregulation is involved. This line of research holds promise for enhancing our knowledge of GDF15 and its implications in health and disease, establishing it as a key player in the intersection of metabolic and inflammatory pathways.
