Lon protease, an ATP-dependent mitochondrial protease, is important in mitochondrial protein maintenance. Lon protease is a multifunctional enzyme, and its functions include the degradation of damaged proteins and naturally short-lived proteins, ATPase and chaperone-like activities, as well as DNA binding. Lon protease plays a major role in the protein quality control system in mammalian cell mitochondria. It is present in the mitochondrial matrix and degrades oxidized and misfolded proteins, thereby protecting the cell from various extracellular stresses, including oxidative stress. The intellectual disability-associated and thalidomide-binding protein cereblon (CRBN) contains a large, highly conserved Lon domain. The Lon ATP-dependent protease plays an important role in regulating many biological processes in bacteria.
Pack Size | Availability | Price/USD | Quantity |
---|---|---|---|
50 μg | In stock | $ 386.00 | |
100 μg | 5 days | $ 660.00 | |
200 μg | 5 days | $ 1,120.00 | |
500 μg | 5 days | $ 2,270.00 |
Biological Information | Testing in progress |
Description | Lon protease, an ATP-dependent mitochondrial protease, is important in mitochondrial protein maintenance. Lon protease is a multifunctional enzyme, and its functions include the degradation of damaged proteins and naturally short-lived proteins, ATPase and chaperone-like activities, as well as DNA binding. Lon protease plays a major role in the protein quality control system in mammalian cell mitochondria. It is present in the mitochondrial matrix and degrades oxidized and misfolded proteins, thereby protecting the cell from various extracellular stresses, including oxidative stress. The intellectual disability-associated and thalidomide-binding protein cereblon (CRBN) contains a large, highly conserved Lon domain. The Lon ATP-dependent protease plays an important role in regulating many biological processes in bacteria. |
Species | E. coli |
Expression System | E. coli |
Tag | His |
Accession Number | P0A9M0 |
Construction | ANXA5 / Annexin Ⅴ / Annexin A5 protein are conjugated with FITC under optimum conditions, the unreacted FITC was removed. |
Protein Purity |
> 90 % as determined by SDS-PAGE
|
Molecular Weight | Approxiamtely 88.3 kDa |
Endotoxin | Please contact us for more information. |
Formulation | Lyophilized from sterile PBS, 10% glycerol, pH 7.4. Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0. 01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA. |
Reconstitution | A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information. |
Stability & Storage |
Sodium azide is toxic to cells and should be disposed of properly. Flush with large volumes of water during disposal. |
Shipping |
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. |
Research Background | Lon protease, an ATP-dependent mitochondrial protease, is important in mitochondrial protein maintenance. Lon protease is a multifunctional enzyme, and its functions include the degradation of damaged proteins and naturally short-lived proteins, ATPase and chaperone-like activities, as well as DNA binding. Lon protease plays a major role in the protein quality control system in mammalian cell mitochondria. It is present in the mitochondrial matrix and degrades oxidized and misfolded proteins, thereby protecting the cell from various extracellular stresses, including oxidative stress. The intellectual disability-associated and thalidomide-binding protein cereblon (CRBN) contains a large, highly conserved Lon domain. The Lon ATP-dependent protease plays an important role in regulating many biological processes in bacteria. |
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