Analytical Data
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Gene name
Sp100
- Application
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Alternative Names
Sp100；Nuclear autoantigen Sp-100
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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
P23497
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Expression Region
1-480aa
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AA Sequence
MAGGGGDLSTRRLNECISPVANEMNHLPAHSHDLQRMFTEDQGVDDRLLY DIVFKHFKRNKVEISNAIKKTFPFLEGLRDRDLITNKMFEDSQDSCRNLV PVQRVVYNVLSELEKTFNLPVLEALFSDVNMQEYPDLIHIYKGFENVIHD KLPLQESEEEEREERSGLQLSLEQGTGENSFRSLTWPPSGSPSHAGTTPP ENGLSEHPCETEQINAKRKDTTSDKDDSLGSQQTNEQCAQKAEPTESCEQ IAVQVNNGDAGREMPCPLPCDEESPEAELHNHGIQINSCSVRLVDIKKEK PFSNSKVECQAQARTHHNQASDIIVISSEDSEGSTDVDEPLEVFISAPRS EPVINNDNPLESNDEKEGQEATCSRPQIVPEPMDFRKLSTFRESFKKRVI GQDHDFSESSEEEAPAEASSGALRSKHGEKAPMTSRSTSTWRIPSRKRRF SSSDFSDLSNGEELQETCSSSLRRGSGKED
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Molecular Weight
79 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
SP100 is a nuclear protein that plays a significant role in various cellular processes, including transcription regulation, DNA repair, and the response to viral infections. Originally discovered as a component of nuclear bodies known as SP100 domains, it has been found to have implications in the immune response and cell cycle regulation. Research has indicated that SP100 is involved in the pathogenesis of several diseases, particularly autoimmune disorders and cancers. Its expression is often altered in pathological conditions, making it a potential biomarker for disease diagnosis and prognosis. The interest in recombinant SP100 proteins has surged, as they can be utilized to elucidate the protein's function, interactions, and post-translational modifications in a controlled environment. Additionally, recombinant SP100 can be employed in the development of therapeutic strategies or vaccines, particularly in the context of viral infections, where its role in antiviral defense mechanisms is crucial. Understanding the structure-function relationship of SP100 through recombinant production can provide deeper insights into its biological roles and contribute to the advancement of targeted therapies. Overall, the study of SP100 recombinant proteins is significant for both basic research and potential clinical applications, highlighting its importance in cellular biology and medicine.
