Analytical Data
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Gene name
lon
- Application
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Alternative Names
lon；LONP；Lon protease homolog 2. peroxisomal
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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
P78025
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Expression Region
1-206aa
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AA Sequence
MPAVKKPQILVVRNQVIFPYNGFELDVGRERSKKLIKALKNLKTKRLVLVTQKNSDQLNPEFDDIYHCGTLCDIDEIIEVPSEDGKTADYKIKGKGLQRVAITSFSDADLTKYDHHFLNSTLTENKALDKLLERIFPDKEDFAEILDSLNSFLELQELKKLSKVPKDIKRYDIITFKLASLIFKDITLQQAILEENDIEKRLQKII
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Molecular Weight
39.8 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
Lon protease, a member of the AAA+ (ATPases Associated with diverse cellular Activities) protein family, plays a crucial role in the maintenance of cellular homeostasis by regulating protein quality control, degradation of misfolded or damaged proteins, and the modulation of various metabolic processes. Initially identified in bacteria, Lon protease has since been characterized in several organisms, including archaea and eukaryotes, highlighting its evolutionary conservation and fundamental biological significance. Its distinct substrate specificity and ATP-dependent mechanisms make it a key player in cellular responses to stress and in regulating protein levels. In addition to its proteolytic activity, recent research has suggested that Lon may interact with various signaling pathways, influencing processes such as cell division, apoptosis, and stress responses. Dysfunction or aberrant activity of Lon has been linked to several diseases, including neurodegenerative disorders and cancer, making it a target of interest for therapeutic interventions. Understanding the structure, function, and regulation of Lon protease is thus essential for elucidating its roles in health and disease, and ongoing research aims to explore its potential as a biomarker and therapeutic target.
