Analytical Data
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Gene name
leucyl aminopeptidase
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简介
Leucyl aminopeptidase proteins play a role in the putative processing and normal turnover of proteins within cells. It catalyzes the removal of unsubstituted N-terminal amino acids from peptides, suggesting involvement in complex mechanisms controlling intracellular protein dynamics. leucyl aminopeptidase Protein, Geobacillus kaustophilus (His) is the recombinant leucyl aminopeptidase protein, expressed by E. coli , with N-6*His labeled tag.
- Application
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Alternative Names
pepA; Probable cytosol aminopeptidase; Leucine aminopeptidase; LAP; Leucyl aminopeptidase
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Species
Others
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Source
E. coli
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q5KVQ4
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Expression Region
M1-D500
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Protein Length
Partial
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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
Leucyl aminopeptidase (LAP) is an enzyme that plays a critical role in protein metabolism by catalyzing the removal of leucine residues from the N-terminus of peptides and proteins. This activity is essential for modulating various biological processes, including protein turnover, cellular signaling, and the regulation of bioactive peptides. LAP has gained attention due to its potential applications in biotechnology and medicine, such as in the development of enzyme-based therapies and diagnostic tools. The study of recombinant LAP has become increasingly important because it allows for the production of the enzyme in sufficient quantities and with desired modifications for specific applications. Advances in genetic engineering techniques, such as cloning and expression in heterologous systems, have facilitated the efficient production of recombinant LAP. Research on this enzyme has also revealed its structural characteristics and catalytic mechanisms, enhancing our understanding of its function. Additionally, recombinant LAP can be utilized in various industrial applications, including food processing and pharmaceuticals, making it a valuable subject of study in enzyme technology. The ongoing investigation of recombinant leucyl aminopeptidase aims to unlock its full potential, paving the way for innovative solutions in health, industry, and research fields.
