Analytical Data
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Gene name
SPA
- Application
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Alternative Names
SPA；SPA1；Signal-induced proliferation-associated Protein 1
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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
Q8IWL2
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Expression Region
21-248aa
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AA Sequence
EVKDVCVGSPGIPGTPGSHGLPGRDGRDGLKGDPGPPGPMGPPGEMPCPPGNDGLPGAPGIPGECGEKGEPGERGPPGLPAHLDEELQATLHDFRHQILQTRGALSLQGSIMTVGEKVFSSNGQSITFDAIQEACARAGGRIAVPRNPEENEAIASFVKKYNTYAYVGLTEGPSPGDFRYSDGTPVNYTNWYRGEPAGRGKEQCVEMYTDGQWNDRNCLYSRLTICEF
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Molecular Weight
26.2 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 SPA (Staphylococcal Protein A) recombinant proteins has garnered significant interest due to their diverse applications in biotechnology and medicine. SPA, originally derived from Staphylococcus aureus, is a cell wall-associated protein known for its ability to bind to the Fc region of immunoglobulins, particularly IgG. This characteristic has made SPA a valuable tool in various fields, including immunology, diagnostics, and therapeutic development. Researchers have explored the potential of recombinant SPA proteins to enhance antibody purification processes and improve the performance of immunoassays, due to their specificity and affinity for antibodies. Additionally, SPA-based fusion proteins have been investigated for their role in vaccine development, as they can elicit robust immune responses when combined with antigens. The advent of recombinant DNA technology has enabled the production of SPA proteins in various expression systems, allowing for large-scale generation and the potential for modification to enhance functionality. Understanding the structure-function relationships of SPA and its variants, along with the optimization of production methods, has propelled forward the innovation of SPA-derived applications in research and therapeutics. As a result, the investigation of SPA recombinant proteins merges microbiology, immunology, and protein engineering, fostering advancements that could lead to improved diagnostic tools and therapies against infectious diseases and beyond.
