Analytical Data
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Gene name
Vitronectin
- Application
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Alternative Names
S-protein (Serum-spreading factor) (V75)
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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
P04004
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Expression Region
20-478aa
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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
Vitronectin is a multifunctional glycoprotein found in the extracellular matrix and body fluids, playing a vital role in various biological processes, including cell adhesion, migration, and wound healing. It serves as a substrate for cell attachment and interacts with several integrin receptors, influencing cellular responses to the microenvironment. Due to its significant involvement in pathophysiological conditions such as cancer metastasis and cardiovascular diseases, vitronectin has garnered attention in biomedical research and therapeutic applications. The production of recombinant vitronectin protein has become essential for elucidating its structural and functional properties, enabling researchers to better understand the molecular mechanisms underlying its diverse biological activities. Advances in protein engineering techniques, such as recombinant DNA technology and expression systems, have facilitated the generation of high-purity vitronectin, which can be utilized in cell culture studies and in vitro assays. By systematically investigating the interactions between vitronectin and its binding partners, researchers aim to develop targeted therapies that manipulate these interactions to control cell behavior in disease contexts. Overall, the study of recombinant vitronectin not only deepens our understanding of its fundamental biological roles but also paves the way for innovative therapeutic strategies in regenerative medicine and cancer treatment.
