Analytical Data
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Gene name
laaA
- Application
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Alternative Names
laaA；L-amino acid amidase
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Species
E.coli
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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
Q76KX0
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Expression Region
1-310aa
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AA Sequence
MEFIEKIREGYAAFGAYQTWYRVTGDLSSGRTPLVVIHGGPGCTHDYVDAFKDVAASGHAVIHYDQLGNGRSTHLPDKDPSFWTVGLFLEELNNLLDHLQISDNYAILGQSWGGMLGSEHAILQPKGLRAFIPANSPTCMRTWVSEANRLRKLLPEGVHETLLKHETAGTYQDPEYLAASRVFYDHHVCRVIPWPEEVARTFAAVDADPTVYHAMSGPTEFHVIGSLKDWKSTGRLSAINVPTLVISGRHDEATPLVVKPFLDEIADVRWALFEDSSHMPHVEERQACMGTVVKFLDEVCSAKYKVLKAS
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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
Related Products
Protein Description
The laaA gene, a member of the large and diverse family of microbial genes, encodes a protein that has garnered significant interest due to its potential applications in biotechnology and medicine. Research on laaA has primarily focused on its role in bacterial metabolism, particularly in the context of amino acid biosynthesis and regulation. Understanding the function of laaA and its encoded protein can provide valuable insights into microbial physiology and the mechanisms underlying metabolic pathways. Additionally, the recombinant laaA protein has shown promise in various applications, such as enzyme catalysis and bioremediation, due to its stability and specificity. The advent of genetic engineering techniques, including CRISPR and recombinant DNA technology, has facilitated the study and manipulation of laaA, enabling researchers to investigate its structure-function relationships and enhance its properties for industrial applications. This research not only contributes to fundamental microbiological knowledge but also holds practical implications for developing novel bioprocesses and therapeutics. As the demand for sustainable solutions continues to rise, the exploration of laaA-recombinant protein could play a crucial role in addressing challenges in health and environmental management.
