Analytical Data
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Gene name
SPOPL
- Application
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Alternative Names
SPOPL; Speckle-type POZ protein-like; HIB homolog 2; Roadkill homolog 2
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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
Q6IQ16
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Expression Region
1-392aa
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AA Sequence
MSREPTPPLP GDMSTGPIAE SWCYTQVKVV KFSYMWTINN FSFCREEMGE VLKSSTFSSG PSDKMKWCLR VNPKGLDDES KDYLSLYLLL VSCPKSEVRA KFKFSLLNAK REETKAMESQ RAYRFVQGKD WGFKKFIRRD FLLDEANGLL PDDKLTLFCE VSVVQDSVNI SGHTNTNTLK VPECRLAEDL GNLWENTRFT DCSFFVRGQE FKAHKSVLAA RSPVFNAMFE HEMEESKKNR VEINDLDPEV FKEMMRFIYT GRAPNLDKMA DNLLAAADKY ALERLKVMCE EALCSNLSVE NVADTLVLAD LHSAEQLKAQ AIDFINRCSV LRQLGCKDGK NWNSNQATDI METSGWKSMI QSHPHLVAEA FRALASAQCP QFGIPRKRLK QS
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Molecular Weight
44.6 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
SPOPL (Suppressor of Tumorigenicity 7) is a protein that has gained attention in the field of molecular biology and cancer research due to its role as an E3 ubiquitin ligase, which is crucial for regulating protein degradation within the cell. Its significance is underscored by its involvement in critical cellular processes such as cell cycle regulation, apoptosis, and signal transduction. Mutations and dysregulation of SPOPL have been implicated in various cancers, making it a potential biomarker for tumor progression and a target for therapeutic interventions. The understanding of SPOPL's structure-function relationship is crucial for designing inhibitors or modulators that could disrupt its oncogenic pathways. Recent studies have focused on the recombinant expression and purification of SPOPL, using techniques such as baculovirus expression systems or bacterial expression systems to obtain sufficient quantities of the protein for functional assays and structural analysis. Investigating the detailed mechanisms by which SPOPL influences tumor biology, including its substrate specificity and interaction with other cellular components, is vital for unraveling its role in cancer and developing prospective treatment strategies. Consequently, ongoing research aims to elucidate the molecular basis of SPOPL function, offering insights that could pave the way for innovative therapeutic approaches in oncology.
