Analytical Data
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Gene name
VIM
- Application
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Alternative Names
VIM；Vimentin
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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
P08670
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Expression Region
2-466aa
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AA Sequence
STRSVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYASSPGGVYATRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNLDSLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE
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Molecular Weight
60.4 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
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Protein Description
VIM, or vimentin, is a type of intermediate filament protein that plays a crucial role in maintaining the structural integrity and mechanical stability of cells, especially mesenchymal cells. It is involved in various cellular processes, including cell proliferation, migration, and apoptosis. The study of VIM recombinant proteins has gained significant attention in recent years due to their potential applications in tissue engineering, cancer research, and regenerative medicine. Researchers have focused on generating VIM recombinant proteins to better understand its functionality in the cytoskeleton and to explore its role in diseases such as cancer, where vimentin is often upregulated and associated with tumor progression and metastasis. Additionally, studying VIM in recombinant forms allows scientists to investigate its interactions with other cytoskeletal components and signaling pathways, which is crucial for elucidating the mechanisms underlying cell behavior. The advancements in recombinant protein technology, combined with the increasing understanding of VIM's role in cellular dynamics, provide a foundation for ongoing research aimed at developing targeted therapies and biomaterial designs that leverage the unique properties of vimentin in therapeutic applications. Overall, VIM recombinant protein research represents a promising avenue for uncovering new insights into cell biology and disease pathology, ultimately contributing to novel therapeutic strategies.
