Analytical Data
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Gene name
nblA
- Application
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Alternative Names
/
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Species
Synechococcus elongatus
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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
P35087
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Expression Region
1-59aa
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Molecular Weight
14.5 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
NblA is a regulatory protein associated with the nitrogen starvation response in cyanobacteria, particularly in species such as *Synechocystis sp.* PCC 6803. As a part of the nitrogen metabolism network, NblA plays a crucial role in the degradation of the nitrogen storage protein, phycobilisome, during periods of nitrogen deprivation. Understanding NblA's function is essential for elucidating the mechanisms of nitrogen assimilation and the adaptation strategies of cyanobacteria to nutrient-limited environments. Furthermore, the study of NblA and its interactions with other cellular components can provide insights into the broader implications for carbon and nitrogen cycling in aquatic ecosystems. Recent advances in genetic engineering and recombinant protein technology have facilitated the expression and purification of NblA, enabling researchers to investigate its structure-function relationships and regulatory pathways in detail. By exploring its potential applications, such as bioengineering for improved photosynthetic efficiency and growth in cyanobacteria-based biofuel production, NblA has garnered significant interest in the fields of microbiology, biochemistry, and environmental science. This research not only enhances our understanding of nitrogen metabolism in cyanobacteria but also holds promise for biotechnological innovations aimed at sustainable agriculture and renewable energy sources.
