Analytical Data
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Gene name
VTI1B
- Application
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Alternative Names
Vesicle transport v-SNARE protein Vti1-like 1Vti1-rp1
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UEU0
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Expression Region
7-208aa
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Molecular Weight
39.4 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
VTI1B, a member of the VTI (Vesicle Transport Protein) family, plays a crucial role in intracellular vesicle trafficking, particularly in the transport of proteins and lipids between the endoplasmic reticulum (ER) and the Golgi apparatus. Research into VTI1B has gained significance due to its involvement in various physiological processes and its implications in several diseases. Studies have shown that VTI1B is essential for the maintenance of cellular homeostasis and plays a pivotal role in membrane fusion events, essential for exocytosis and endocytosis. Additionally, its dysfunction has been linked to pathologies such as neurodegenerative diseases, where impaired vesicle transport can lead to the accumulation of toxic proteins. Understanding the structural and functional characteristics of VTI1B is vital for elucidating the molecular mechanisms underlying these conditions. Recent advancements in protein engineering and structural biology have facilitated the development of recombinant VTI1B protein, enabling researchers to investigate its biological activities and interactions in detail. This knowledge could pave the way for novel therapeutic strategies aimed at modulating VTI1B function in disease contexts. Through a combination of biochemical assays and cellular models, ongoing research is focusing on how VTI1B can be targeted to enhance vesicle transport processes, providing hope for interventions in related disorders. As such, VTI1B represents a promising candidate for further investigation in the realms of cell biology and pharmacology, offering insights that could potentially translate into clinical applications.
