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
Related Products
Protein Description
FN1, or Fibronectin 1, is a glycoprotein that plays a crucial role in various biological processes, including cell adhesion, migration, and wound healing. It exists in two primary forms: soluble plasma fibronectin and insoluble extracellular matrix fibronectin. Research into FN1 has gained momentum due to its significant involvement in tumor progression and metastasis, where it facilitates cancer cell interactions with the extracellular matrix and immune system evasion. The reorganization of FN1 in the tumor microenvironment can influence cancer cell behavior and therapeutic responses. Additionally, FN1 is emerging as a potential biomarker for various diseases, with alterations in its expression patterns linked to conditions such as fibrosis, cardiovascular diseases, and certain cancers. Recent advances in recombinant protein technology have enabled the production of FN1 and its fragments, facilitating detailed studies of its structure-function relationships, interaction with other biomolecules, and role in cellular processes. Investigating FN1 as a therapeutic target or diagnostic tool continues to be a promising area of research, with potential implications for improving cancer treatment and understanding tissue repair mechanisms.
