Analytical Data
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Gene name
slpA
- Application
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Alternative Names
(Surface layer protein)(SA-protein)
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Species
Lactobacillus acidophilus
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P35829
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Expression Region
25-444aa
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Molecular Weight
51.7 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 the slpA recombinant protein is grounded in its significant role in various biological processes, particularly in the context of bacterial pathogenesis. slpA, which encodes the secreted and surface-associated lipoprotein A, has garnered attention due to its involvement in virulence factors and its potential as a target for vaccine development. Research indicates that slpA is crucial for the survival and colonization of pathogenic bacteria in host organisms, making it a key player in infectious diseases. Additionally, the protein is believed to facilitate immune evasion by modulating the host's immune response. The recombinant expression of slpA allows for the investigation of its structure-function relationship, which is essential for understanding its mechanisms of action. This research can lead to the identification of novel therapeutic strategies against bacterial infections by exploiting slpA's immunogenic properties. Moreover, insights gained from slpA studies can contribute to the development of improved diagnostic tools and vaccines aimed at enhancing host resistance to pathogenic bacteria. As a result, the exploration of slpA recombinant protein has broad implications not only for microbiology and immunology but also for clinical applications in managing bacterial diseases.
