Analytical Data
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Gene name
VMI2
- Application
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Alternative Names
VMI2；Viral macrophage inflammatory Protein 2
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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
Q98157
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Expression Region
1-94aa
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AA Sequence
MDTKGILLVAVLTALLCLQSGDTLGASWHRPDKCCLGYQKRPLPQVLLSSWYPTSQLCSKPGVIFLTKRGRQVCADKSKDWVKKLMQQLPVTAR
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Molecular Weight
10.4 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
VMI2, a vital protein in the context of cellular processes, has garnered significant attention in the realm of biochemical research due to its role in the regulation of mitotic progression and cellular responses to environmental stress. Initially identified in yeast, VMI2 is evolutionarily conserved and functions as part of a larger network that coordinates cell division with external stimuli. The study of VMI2 and its recombinant forms has become particularly crucial in understanding its mechanisms of action and potential implications in disease states such as cancer, where dysregulation of cell division is a hallmark. Recent advances in recombinant protein technology allow for the production of VMI2 in a more controlled environment, enabling researchers to investigate its structural and functional properties extensively. By elucidating the molecular dynamics of VMI2, scientists can better understand its interactions with other cellular components, paving the way for the development of therapeutic interventions. Additionally, characterizing VMI2 through recombinant protein techniques provides insights into its post-translational modifications and functional domains, which are essential for its activity. Overall, the research surrounding VMI2 not only enhances our comprehension of fundamental biological processes but also holds promise for medical applications, particularly in the delineation of novel strategies for cancer treatment and the management of other disorders linked to cellular regulation.
