Analytical Data
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Gene name
slpA
- Application
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Alternative Names
slpA；Outer membrane Protein SlpA
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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
P32053
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Expression Region
1-413aa
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AA Sequence
MARKTKPLTD TEIKAAKPKD ADYQLYDGDG LTLLIKSSGS KLWQFRYYRP LTKQRTKQSF GAYPAVSLSD ARKLRAESKV LLAKDIDPQE HQKEQVRNSQ EAKTNTFLLV AERWWNVKKT SVTEDYADDI WRSLERDIFP AIGDISITEI KAHTLVKAVQ PVQARGALET VRRLCQRINE VMIYAQNTGL IDAVPSVNIG KAFEKPQKKN MPSIRPDQLP QLMHTMRTAS ISMSTRCLFM WQLLTITRPA EAAEARWDEI DFNASEWKIP AARMKMNRDH TVPLSDGALA ILEMMKPLSG GREFIFPSRI KPNQPMNSQT VNAALKRAGL GGVLVSHGLR SIASTALNEE GFPPDVIEAA LAHVDKNEVR RAYNRSDYLE QRRPMMQWWA DLVKAADSGS IVLTHLSKIR LVG
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Molecular Weight
46.6 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
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Protein Description
The study of the slpA gene and its recombinant protein, SlpA, has garnered significant attention due to its essential role in the pathogenesis of various bacteria, particularly in relation to human infections. SlpA, a surface-layer protein, serves as a crucial factor in bacterial adhesion, immune evasion, and biofilm formation, thereby facilitating the establishment of infections. Research into SlpA recombinant protein provides valuable insights into the molecular mechanisms underpinning these processes and helps to delineate its interaction with host immune systems. The potential for SlpA to act as a vaccine candidate is also being explored, given its surface exposure and immunogenic properties. By generating recombinant forms of SlpA, researchers aim to better understand its structure-function relationships and evaluate its efficacy in eliciting protective immune responses. Furthermore, studies on SlpA contribute to the broader field of microbial pathogenesis and vaccine development, offering promising strategies for controlling bacterial infections and enhancing public health outcomes. Through characterizing SlpA and its biological functions, researchers hope to pave the way for novel therapeutic approaches, addressing the rising challenge of antibiotic resistance and the need for innovative solutions in infectious disease management.
