Analytical Data
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Gene name
spi
- Application
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Alternative Names
spi; Spiralin
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Species
Spiroplasma citri
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P19215
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Expression Region
24-241aa
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Molecular Weight
39 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
The study of SPI (Serpin Protease Inhibitor) recombinant proteins has gained significant attention in recent years due to their vital role in regulating proteolysis, which is essential for various physiological processes, including the immune response, coagulation, and inflammation. Serpins are a superfamily of proteins that function primarily as inhibitors of serine proteases, and their dysregulation has been implicated in numerous diseases, such as thrombosis, cancer, and neurodegenerative disorders. Given their importance, researchers have increasingly focused on the production of recombinant SPI proteins for therapeutic and diagnostic applications. These recombinantly produced proteins offer advantages over their natural counterparts, including increased purity, enhanced stability, and the ability for site-directed mutagenesis to improve efficacy. Advances in biotechnology have facilitated the development of various expression systems, such as bacterial, yeast, and mammalian cells, to optimize the yield and functionality of SPI proteins. Furthermore, understanding the structure-activity relationship of these inhibitors aids in the design of novel drugs targeting specific proteases involved in disease pathways. Overall, the exploration of SPI recombinant proteins could lead to innovative treatments and advancements in the field of biomedicine, making it a promising area of ongoing research.
