Analytical Data
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Gene name
FN1
- Application
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Alternative Names
FN1；FN；Fibronectin
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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
P02751
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Expression Region
732-911aa
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AA Sequence
TASSFVVSWVSASDTVSGFRVEYELSEEGDEPQYLDLPSTATSVNIPDLLPGRKYIVNVYQISEDGEQSLILSTSQTTAPDAPPDPTVDQVDDTSIVVRWSRPQAPITGYRIVYSPSVEGSSTELNLPETANSVTLSDLQPGVQYNITIYAVEENQESTPVVIQQETTGTPRSDTVPSPR
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Molecular Weight
23.6 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
FN1, or fibronectin 1, is a high-molecular-weight glycoprotein synthesized by various cell types, including fibroblasts and endothelial cells, and plays a pivotal role in cellular adhesion, migration, and wound healing. It is primarily found in the extracellular matrix and is crucial for tissue repair and maintenance. Research has shown that FN1 is involved in numerous physiological and pathological processes, including development, fibrosis, and cancer metastasis. Its diverse functions are attributed to its unique structure, featuring multiple domains that interact with cell surfaces and other extracellular matrix components. Consequently, FN1 has garnered significant attention in biomedical research, particularly in understanding its role in disease mechanisms and potential therapeutic applications. Scientists have successfully developed recombinant FN1 proteins, allowing for in-depth studies of its biochemical properties and interactions. These recombinant proteins serve as valuable tools in investigating FN1's function in cell signaling pathways, ECM remodeling, and its influence on tumor progression and metastasis. The ongoing research into FN1’s molecular mechanisms offers the potential for innovative strategies in disease treatment and regenerative medicine, reinforcing its significance in both basic research and clinical applications.
