Analytical Data
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Gene name
Fibronectin
- Application
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Alternative Names
FN; CIG; FN1; ED-B; FINC; FNZ; GFND; GFND2; LETS; MSF; SMDCF
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Species
Human
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Source
HEK293
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Tag
C-8*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P02751-13
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Expression Region
E1266-T1356
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Protein Length
Partial
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Molecular Weight
Predicted band size: 10.81 kDa; Observed band size: 15-25 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
Fibronectin is a high-molecular-weight glycoprotein that plays a crucial role in cell adhesion, migration, and differentiation, making it an essential component of the extracellular matrix. Its importance extends to wound healing, embryogenesis, and tissue repair, as well as its involvement in various pathological conditions, including cancer metastasis and fibrosis. Due to its significant biological functions, fibronectin has become a target for therapeutic and diagnostic applications. The advent of recombinant DNA technology has enabled the production of fibronectin recombinant proteins, which offer advantages over native forms, including greater purity, consistency, and the ability to engineer specific domains for enhanced functionality. Research in this area focuses on optimizing expression systems, such as bacterial, yeast, or mammalian cells, to produce bioactive fibronectin fragments or full-length proteins that maintain their structural integrity and biological activity. These recombinant proteins are being explored for their potential in regenerative medicine, drug delivery systems, and as biomaterials for tissue engineering. Moreover, studies on the interaction of fibronectin with other proteins and cell types are providing valuable insights into its role in cellular signaling pathways. Overall, the investigation of fibronectin recombinant proteins holds great promise for advancing our understanding of cellular processes and developing novel therapeutic strategies for various diseases.
