Analytical Data
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Gene name
Use1
- Application
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Alternative Names
(Protein D12)(USE1-like protein)
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Species
Mouse
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9CQ56
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Expression Region
1-242aa
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Molecular Weight
34.6 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
Use1 is a critical protein belonging to the class of membrane fusion proteins, which play a vital role in various cellular processes, including vesicle trafficking, organelle shaping, and the fusion of membranes during cellular events such as cytokinesis and viral entry. The study of Use1 is particularly important due to its involvement in the fusion of transport vesicles with acceptor membranes, a fundamental step in intracellular communication and protein transport. Research has indicated that misregulation or malfunction of Use1 can lead to several diseases, including neurodegenerative disorders and metabolic syndromes, highlighting its potential as a therapeutic target. In addition, understanding the structural and functional characteristics of Use1 could provide insights into membrane dynamics and the molecular mechanisms underlying membrane fusion. Recent innovations in biochemistry and structural biology have facilitated the detailed investigation of this protein, leading to the identification of its functional domains and interaction partners. This research not only enhances our fundamental understanding of cell biology but also opens avenues for developing novel interventions that target membrane fusion processes in disease contexts. Consequently, the exploration of Use1 and its functional implications is not only academically enriching but also pivotal in the quest for new therapeutic strategies.
