Analytical Data
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Gene name
sspB
- Application
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Alternative Names
sspB；Stringent starvation Protein B
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Species
E.coli
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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
P0AFZ4
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Expression Region
1-165aa
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AA Sequence
MDLSQLTPRRPYLLRAFYEWLLDNQLTPHLVVDVTLPGVQVPMEYARDGQIVLNIAPRAVGNLELANDEVRFNARFGGIPRQVSVPLAAVLAIYARENGAGTMFEPEAAYDEDTSIMNDEEASADNETVMSVIDGDKPDHDDDTHPDDEPPQPPRGGRPALRVVK
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Molecular Weight
22.3 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
SSPB (Spermidine/Spermine N1-Acetyltransferase) is a critical enzyme involved in the polyamine metabolic pathway, which plays a vital role in cellular functions such as growth, differentiation, and stress response. The synthesis and regulation of polyamines, including spermidine and spermine, are essential for various biological processes, including cell proliferation and apoptosis. Recent studies have highlighted the significance of SSPB in cancer research, as altered polyamine levels are often associated with tumorigenesis and cancer progression. The recombinant production of SSPB allows for the detailed investigation of its enzymatic properties and regulatory mechanisms, enabling a deeper understanding of its biological roles. Additionally, characterizing SSPB in vitro using recombinant technology supports the development of potential therapeutic strategies targeting polyamine metabolism in cancer therapy and other diseases. Understanding SSPB's structure-function relationship through crystallography and other biophysical methods can also aid in the design of specific inhibitors, which may serve as novel anti-cancer agents. As such, the research on SSPB recombinant proteins not only expands our knowledge of polyamine biology but also opens new avenues for therapeutic interventions.
