Analytical Data
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Gene name
Vimentin
- Application
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Alternative Names
CTRCT30; Epididymis luminal protein 113; FLJ36605; HEL113; VIM; VIME_HUMAN; Vimentin
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P08670
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Expression Region
2-466aa
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Molecular Weight
57.5 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
Vimentin is a type III intermediate filament protein that plays a crucial role in maintaining cellular integrity, providing structural support, and facilitating intracellular signaling. It is predominantly expressed in mesenchymal cells and is essential for various cellular functions, including migration, adhesion, and proliferation. Over the years, research has shown that vimentin is involved in the processes of epithelial-to-mesenchymal transition (EMT) and tumor metastasis, making it an important biomarker for cancer progression. The production of recombinant vimentin protein has garnered significant interest as it allows for the comprehensive study of its biochemical properties and functions in a controlled environment. By using recombinant DNA technology, researchers can produce larger quantities of vimentin, enabling detailed structural and functional analyses, such as studies on its role in cytoskeletal organization and interactions with other cellular proteins. Moreover, recombinant vimentin is valuable in drug discovery and therapeutic applications, particularly in identifying small molecules or antibodies that could inhibit its functions, thereby offering potential strategies for cancer treatment. The exploration of vimentin as a target for therapeutic intervention highlights its significance not just in cancer biology, but also in regenerative medicine and tissue engineering, where understanding its role in cellular mechanics and migration can lead to innovations in wound healing and tissue regeneration strategies. Overall, the study of recombinant vimentin protein opens a new avenue for understanding its multifaceted roles in health and disease, paving the way for advancements in both basic and applied biomedical research.
