Analytical Data
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Gene name
SPSB4
- Application
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Alternative Names
SSB4
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Species
Human
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Source
E. coli
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Tag
His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96A44
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Expression Region
R33-E233
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Protein Length
Partial
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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
SPSB4, or SplA/2-related protein 4, is a member of the SPSB family of proteins, which play critical roles in various cellular processes, including signal transduction and protein degradation. Research on SPSB4 has garnered attention due to its involvement in the regulation of key signaling pathways, particularly those related to immune responses and inflammation. Studies suggest that SPSB4 can modulate the activity of certain E3 ubiquitin ligases, impacting the stability and turnover of target proteins, including those involved in immune signaling. Understanding the function and mechanisms of SPSB4 is essential, as dysregulation of its activity has been implicated in various diseases, including autoimmune disorders and certain cancers. The reconstitution of SPSB4 as a recombinant protein allows researchers to study its structure-function relationships, interact with potential substrates, and explore its role in protein ubiquitination and degradation processes. This research not only enhances our knowledge of SPSB4's biological significance but also opens up potential therapeutic avenues for conditions associated with its dysregulation. By employing advanced techniques such as crystallography and in vitro assays, scientists aim to elucidate the precise mechanisms by which SPSB4 operates within cellular contexts, contributing to the broader field of ubiquitin biology and therapeutic development.
