Analytical Data
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Gene name
VCP
- Application
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Alternative Names
IBMPFD; p97; TERA; Transitional Endoplasmic Reticulum ATPase; 15S Mg(2+)-ATPase p97 subunit
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P55072
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Expression Region
Gly125~Ile371
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Molecular Weight
36kDa
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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
The study of VCP (valosin-containing protein) recombinant proteins has emerged as a critical focus in the fields of molecular biology and cell physiology due to their pivotal roles in various cellular processes. VCP is a highly conserved ATPase associated with various cellular activities, including protein quality control, endoplasmic reticulum-associated degradation (ERAD), and autophagy. Disruption of VCP function has been linked to several human diseases, including neurodegenerative disorders like ALS and frontotemporal dementia, as well as muscle degenerations such as inclusion body myopathy. Researchers have increasingly turned to recombinant VCP proteins to elucidate their mechanisms of action and to explore therapeutic avenues. By cloning and expressing VCP in heterologous systems, scientists can investigate its functional domains, interaction partners, and regulatory mechanisms in greater detail. This approach not only allows the study of VCP's role in disease pathogenesis but also facilitates the development of potential interventions, as understanding the molecular basis of VCP-related dysfunction could lead to innovative treatment strategies. Furthermore, the production of VCP recombinant proteins serves as a platform for structure-function analyses and the identification of small-molecule inhibitors or modulators that may restore VCP function in pathological contexts, thereby holding promise for drug discovery efforts aimed at treating diseases associated with VCP dysregulation. Overall, research on VCP recombinant proteins is at the forefront of efforts to decode their biological significance and therapeutic potential.
