Analytical Data
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Gene name
FNDC1
- Application
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Alternative Names
FNDC1; FNDC2; KIAA1866; MEL4B3Fibronectin type III domain-containing protein 1; Activation-associated cDNA protein; Expressed in synovial lining protein
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q4ZHG4
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Expression Region
86-184aa
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AA Sequence
VPSRLPPRSAATVSPVAGTHPWPQYTTRAPPGHFSTTPMLSLRQRMMHARFRNPLSRQPARPSYRQGYNGRPNVEGKVLPGSNGKPNGQRIINGPQGTK
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Molecular Weight
36.63 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
FNDC1, or Fibronectin Type III Domain-Containing 1, has garnered significant interest in biomedical research due to its potential roles in various physiological and pathological processes. Initially identified as a protein involved in muscle differentiation and development, FNDC1 has since been implicated in several critical functions, including cellular adhesion, migration, and the modulation of inflammation. Its relevance has been highlighted in metabolic studies, particularly concerning energy expenditure and glucose metabolism, as it appears to interact with pathways related to exercise-induced irisin production—a peptide that plays a crucial role in the browning of white adipose tissue. Furthermore, FNDC1 has been researched in the context of cancer biology, where its expression levels may influence tumor progression and metastasis, suggesting a dual role in both metabolic regulation and oncogenesis. The recombinant expression and purification of FNDC1 are therefore pivotal for elucidating its structure-function relationships and exploring its therapeutic potentials. Understanding FNDC1's mechanisms of action could provide insights into novel treatment strategies for metabolic disorders and cancer, underscoring the importance of this protein in both basic and applied biological research.
