Analytical Data
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Gene name
Fibronectin/FN1
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简介
Fibronectin binds collagen, fibrin, heparin, DNA, and actin. It is involved in cell adhesion, motility, opsonization, wound healing and maintenance of cell shape. Fibronectin/FN1 Protein, Human is the recombinant human-derived Fibronectin/FN1 protein, expressed by E. coli, with tag free.
- Application
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Alternative Names
CIG; ED-B; FINC; FN; FNZ; GFND; GFND2; LETS; MSF; SMDCF
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Species
Human
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P02751-15
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Expression Region
P02751-15 (P1361-S1637&A1812-T2107)
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Protein Length
Partial
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Molecular Weight
57-63 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
Fibronectin (FN1) is a high-molecular-weight glycoprotein that plays a crucial role in various biological processes, including cell adhesion, migration, and wound healing. It exists in multiple isoforms and is primarily found in extracellular matrices, where it modulates cell behavior and influences tissue repair and development. In recent years, the relevance of FN1 has gained attention in cancer research, as its aberrant expression is often associated with tumor progression and metastasis. Researchers have utilized recombinant FN1 proteins to investigate its structural properties and functional roles in vitro and in vivo. These studies aim to unravel the mechanistic pathways through which FN1 contributes to cell signaling and the tumor microenvironment. Additionally, the development of FN1-based biomaterials and therapeutic strategies is being explored, focusing on its potential applications in tissue engineering and regenerative medicine. Understanding the multifaceted roles of FN1 through recombinant protein studies could provide pivotal insights into its contributions to both normal physiology and pathological conditions, paving the way for innovative therapeutic approaches targeting FN1 pathways in various diseases.
