Analytical Data
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Gene name
pstS1
- Application
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Alternative Names
Antigen Ag78 Protein antigen B Short name: PAB
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Species
Mycobacterium tuberculosis
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P9WGU0
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Expression Region
24-373aa
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Molecular Weight
39.8 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
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Protein Description
The pstS1 recombinant protein is derived from the pstS gene, which is part of the phosphate-specific transport (Pst) system in bacteria, particularly in Gram-negative organisms. This protein plays a crucial role in phosphate uptake, a vital nutrient for various cellular functions, including energy metabolism and nucleic acid synthesis. In many environments, phosphate availability is limited, making efficient uptake mechanisms essential for microbial survival and growth. Research on pstS1 recombinant protein has gained significance due to its potential applications in biotechnology and medicine. By understanding the structure and function of pstS1, scientists aim to manipulate its properties for various purposes, such as developing novel strategies for bioremediation, enhancing agricultural productivity through bio-fertilizers, and even designing new antibiotics targeting bacterial phosphate transport systems. Furthermore, the study of pstS1 can provide insights into bacterial adaptation mechanisms to nutrient limitations, thereby contributing to our understanding of microbial ecology. Given the increasing concern over phosphorus scarcity in agriculture and its environmental impacts, the exploration of pstS1 holds promise not only for basic research but also for addressing practical challenges in resource management and sustainability. Understanding the dynamics of this protein could lead to innovative solutions for enhancing phosphate bioavailability and utilization in diverse ecosystems.
