Analytical Data
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Gene name
SP2
- Application
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Alternative Names
Transcription factor Sp2
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q02086
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Expression Region
1-249 aa
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AA Sequence
MAATAAVSPSDYLQPAASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLSPGKNSFGILSSKGNILQIQGSQLSASYPGGQLVFAIQNPTMINKGTRSNANIQYQAVPQIQASNSQTIQVQPNLTNQIQIIPGTNQAIITPSPSSHKPVPIKPAPIQKSSTTTTPVQSGANVVKLTGGGGNVTLTLPVNNLVNASDTGAPTQLLTASCQTGMLNSTRMFLFLAFINVL
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Molecular Weight
52 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
SP2 protein, a member of the splicing factor family, plays a crucial role in the regulation of gene expression and alternative splicing processes. Its involvement in various biological functions, including cell differentiation, proliferation, and apoptosis, has garnered significant interest in the scientific community. Recent studies have highlighted the importance of SP2 in neurological development and its potential links to various diseases, including neurodegenerative disorders and cancers. Researchers are investigating the mechanisms by which SP2 influences splicing activity and contributes to the pathophysiology of these conditions. The ability to produce and study recombinant SP2 protein has become essential to elucidate its structure-function relationship and interaction with other cellular components. Advances in techniques such as recombinant DNA technology and protein purification are facilitating the exploration of SP2’s biological roles and its potential as a therapeutic target. Understanding the dynamics of SP2 in cellular contexts may open new avenues for therapeutic intervention in diseases where its activity is dysregulated.
