Analytical Data
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Gene name
laaA
- Application
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Alternative Names
laaAL-amino acid amidase; EC 3.5.1.101
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Species
Pseudomonas azotoformans
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Source
E. coli
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Tag
N- His-SUMO & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q76KX0
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Expression Region
1-310aa
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Molecular Weight
54.5 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
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Protein Description
The laaA gene, which encodes a specific protein, has garnered significant interest in the field of molecular biology and biotechnology due to its potential applications in various domains, including medicine and agriculture. This gene is often associated with important biological functions, such as influencing plant growth, stress responses, and pathogen resistance. Studies have indicated that laaA may play a critical role in the synthesis of unique metabolites or secondary compounds that enhance an organism’s adaptability to environmental challenges. Researchers are particularly focused on the mechanisms through which laaA functions, the pathways it influences, and its interplay with other genetic factors. Protein recombination techniques have allowed scientists to produce laaA recombinant proteins to study their functional properties in detail, which can lead to advances in genetic engineering and crop improvement strategies. Furthermore, understanding the laaA protein's structure and function is essential for the development of biotechnological applications, such as creating genetically modified organisms with improved resistance to diseases or environmental stresses. As a result, ongoing research on laaA not only contributes to fundamental biological knowledge but also holds promise for innovative solutions to global challenges in food security and sustainable agriculture.
