Analytical Data
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Gene name
splB
- Application
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Alternative Names
splB；Serine protease SplB
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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
A7X3Q8
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Expression Region
37-240aa
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AA Sequence
ENNVTKIQDTNIFPYTGVVAFKSATGFVVGKNTILTNKHVSKNYKVGDRITAHPNSDKGNGGIYSIKKIINYPGKEDVSVIQVEERAIERGPKGFNFNDNVTPFKYAAGAKAGERIKVIGYPHPYKNKYVLYESTGPVMSVEGSSIVYSAHTESGNSGSPVLNSNNELVGIHFASDVKNDDNRNAYGVYFTPEIKKFIAENIDK
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Molecular Weight
29.8 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 research on the recombinant protein SplB, a secreted protease derived from the bacterium *Streptococcus pneumoniae*, has gained significant attention due to its crucial role in bacterial pathogenesis and potential implications for therapeutic development. SplB is part of the pneumococcal virulence factor arsenal, contributing to the bacterium's ability to evade host immune responses and promote infection. The interest in studying recombinant SplB stems from its unique enzymatic properties and specificity, which can provide insights into the molecular mechanisms underlying pneumococcal infections. Understanding the structure-function relationship of SplB can aid in designing inhibitors that target this protease, thus offering a novel strategy for combating pneumococcal diseases. Furthermore, the use of recombinant technologies allows for the production of this protein in a controlled environment, facilitating detailed functional assays and studies on its interactions with host cells. As the prevalence of antibiotic-resistant strains of *Streptococcus pneumoniae* increases, exploring the role of virulence factors like SplB represents a promising avenue for developing alternative therapeutic approaches and enhancing our overall understanding of bacterial pathogenesis.
