Analytical Data
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Gene name
lon
- Application
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Alternative Names
ATP-dependent protease La
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Species
Mycoplasma pneumoniae
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Source
E. coli
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Tag
N- His-SUMO
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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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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
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Protein Description
LON protease, a key member of the ATP-dependent protease family, is an essential mitochondrial enzyme in eukaryotic cells that plays a critical role in maintaining mitochondrial protein homeostasis. It participates in the degradation of misfolded or damaged proteins, thus preventing the accumulation of toxic substrates that could compromise mitochondrial function and cellular health. The dysfunction of LON protease has been implicated in various pathologies, including neurodegenerative diseases, cancer, and aging-related disorders. Research into LON protease has gained momentum due to its dual role in protein quality control and regulatory functions in mitochondrial dynamics. Recent studies have focused on understanding the structural features of LON, its substrate specificity, and the mechanistic aspects of how it recognizes and unfolds substrates for degradation. The modulation of LON activity presents a promising therapeutic avenue for enhancing mitochondrial function and combating diseases associated with mitochondrial stress. Furthermore, insights into LON's interactions with other mitochondrial chaperones and proteases are crucial for delineating its role within the cellular proteolytic landscape, thereby offering potential targets for drug development aimed at restoring mitochondrial health and improving therapeutic outcomes in related diseases.
