Analytical Data
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Gene name
SVIP
- Application
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Alternative Names
SVIP；Small VCP/p97-interacting Protein
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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
Q8NHG7
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Expression Region
1-77aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMGLCFPC PGESAPPTPD LEEKRAKLAE AAERRQKEAA SRGILDVQSV QEKRKKKEKI EKQIATSGPP PEGGLRWTVS
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Molecular Weight
11 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
SVIP (Small VCP/p97-Interacting Protein) is a crucial component in various cellular processes, particularly those related to the regulation of protein homeostasis and degradation pathways. Research on SVIP gained momentum due to its role in the endoplasmic reticulum-associated degradation (ERAD) system, where it interacts with the VCP/p97 ATPase, a key player in protein dislocation and degradation. Understanding SVIP's structure and function is essential, as dysregulation of this protein can lead to several diseases, including neurodegenerative disorders and certain cancers. Recent studies have highlighted SVIP's involvement in the cellular stress response, particularly in coping with misfolded proteins, thereby making it a potential target for therapeutic interventions. The recombinant expression and purification of SVIP allow researchers to explore its binding interactions and functional mechanisms in greater detail. By employing advanced techniques like X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy, scientists aim to elucidate its structural characteristics and how mutations may affect its role in cellular homeostasis. Overall, the study of SVIP and its recombinant proteins holds significant promise for advancing our understanding of cellular stress responses and developing novel strategies for treating related diseases.
