Analytical Data
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Gene name
VTN
- Application
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Alternative Names
VTN；Vitronectin
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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
P04004
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Expression Region
20-478aa
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AA Sequence
DQESCKGRCTEGFNVDKKCQCDELCSYYQSCCTDYTAECKPQVTRGDVFTMPEDEYTVYDDGEEKNNATVHEQVGGPSLTSDLQAQSKGNPEQTPVLKPEEEAPAPEVGASKPEGIDSRPETLHPGRPQPPAEEELCSGKPFDAFTDLKNGSLFAFRGQYCYELDEKAVRPGYPKLIRDVWGIEGPIDAAFTRINCQGKTYLFKGSQYWRFEDGVLDPDYPRNISDGFDGIPDNVDAALALPAHSYSGRERVYFFKGKQYWEYQFQHQPSQEECEGSSLSAVFEHFAMMQRDSWEDIFELLFWGRTSAGTRQPQFISRDWHGVPGQVDAAMAGRIYISGMAPRPSLAKKQRFRHRNRKGYRSQRGHSRGRNQNSRRPSRATWLSLFSSEESNLGANNYDDYRMDWLVPATCEPIQSVFFFSGDKYYRVNLRTRRVDTVDPPYPRSIAQYWLGCPAPGHL
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Molecular Weight
52.4 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
VTN (vitronectin) is a multifunctional glycoprotein that plays a crucial role in various biological processes, including cell adhesion, migration, and wound healing. Research on VTN has gained significance due to its involvement in several pathological conditions, including cancer progression, cardiovascular diseases, and tissue repair mechanisms. VTN interacts with various cell types through its binding to integrins and other extracellular matrix proteins, influencing cell behavior and extracellular matrix dynamics. This has led to increased interest in the potential of VTN as a therapeutic target and biomarker for disease states. Studies have shown that altered levels of VTN can be associated with tumor growth and metastasis, making it a candidate for cancer diagnostics and treatment strategies. Furthermore, advances in recombinant protein technology have enabled the production and purification of VTN for detailed functional studies, paving the way for innovative applications in regenerative medicine and targeted therapies. Understanding the complex roles of VTN in cellular processes and its interactions with other biomolecules continues to be a focus of research, potentially leading to novel insights and approaches for managing various diseases.
