Analytical Data
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Gene name
LARS
- Application
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Alternative Names
LARS；KIAA1352；LARS；Leucine--tRNA ligase. cytoplasmic
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Species
Human
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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
P10586
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Expression Region
全长
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AA Sequence
full
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Molecular Weight
212.8 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
Related Products
Protein Description
LARS (Leucyl-tRNA Synthetase) is a key enzyme implicated in the protein synthesis machinery of cells, responsible for attaching leucine, an essential amino acid, to its corresponding tRNA. The study of LARS and its recombinant protein has gained significant attention due to its critical role in various cellular processes, including translation fidelity, regulation of gene expression, and involvement in specific diseases. Abnormal activity or mutations in LARS are linked to severe pathologies such as neurodegenerative disorders and certain types of cancers, highlighting its potential as a therapeutic target. Additionally, understanding the structure and function of LARS can provide insights into the mechanisms of aminoacylation and the overall functioning of the ribosome. Technological advancements in recombinant protein expression and purification techniques have facilitated the study of LARS, making it possible to analyze its biochemical properties, substrate specificity, and interactions with other cellular components. This research not only aims to elucidate the fundamental biological functions of LARS but also explores its potentials in biotechnology and medicine, offering a pathway for developing novel diagnostic and therapeutic strategies aimed at diseases associated with its dysfunction. As such, the ongoing investigation of LARS recombinant proteins represents a vital intersection of molecular biology, biochemistry, and translational research.
