Analytical Data
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基因名
slpA
- Application
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别名
(Surface layer protein)(SA-protein)
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种属
Lactobacillus acidophilus
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表达系统
E. coli
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标签
N- His & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P35829
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表达区间
25-444aa
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分子量
51.7 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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 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.
