Analytical Data
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Gene name
VPS4A
- Application
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Alternative Names
(Protein SKD2)(VPS4-1)(hVPS4)
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Species
Human
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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
Q9UN37
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Expression Region
1-437aa
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Molecular Weight
53.9 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
VPS4A (Vacuolar Protein Sorting 4A) is a vital protein involved in the endosomal sorting complex required for transport (ESCRT) pathway, which plays a crucial role in various cellular processes, including the degradation of membrane proteins, cellular response to stress, and the regulation of various signaling pathways. Understanding the function and mechanisms of VPS4A is essential due to its implications in diseases such as cancer, where its role in maintaining cellular homeostasis and regulating apoptosis is highlighted. Research indicates that VPS4A is involved in the membrane remodeling necessary for the budding of viruses and the biogenesis of multivesicular bodies, which are key components of exosome formation. Additionally, VPS4A has been linked to cellular responses to oxidative stress and is thought to contribute to the maintenance of proteostasis within the cell. As ongoing studies explore the structural dynamics and functional properties of VPS4A, there is a growing interest in its potential as a therapeutic target, particularly in oncological contexts where the manipulation of cellular degradation pathways could enhance treatment efficacy. Therefore, characterizing VPS4A and understanding its regulatory mechanisms at the molecular level is crucial for unraveling its contribution to cellular biology and its potential implications for innovative therapeutic strategies.
