LON PROTEASE Protein, E. coli, Recombinant (His)
Cat# TMPY-00541-50ug
Size : 50ug
Brand : TargetMol
LON PROTEASE Protein, E. coli, Recombinant (His)
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LON PROTEASE Protein, E. coli, Recombinant (His)
Catalog No. TMPY-00541
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.
All TargetMol products are for research purposes only and cannot be used for human consumption. We do not provide products or services to individuals. Please comply with the intended use and do not use TargetMol products for any other purpose. | Pack Size | ||
|---|---|---|
| 50 μg | In Stock | |
| 100 μg | 7-10 days | |
| 200 μg | 7-10 days | |
| 500 μg | 7-10 days |
Biological Description
| Biological Information | Activity testing is in progress. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first. |
| 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 | C-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 | 88.3 kDa (predicted) |
| Endotoxin | Please contact us for more information. |
| Formulation | Lyophilized from a solution filtered through a 0.22 μm filter, containing PBS, 10% glycerol, pH 7.4. Typically, a mixture containing 5% to 8% trehalose, mannitol, and 0.01% Tween 80 is incorporated as a protective agent before lyophilization. |
| Reconstitution | A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA 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, Lyophilized powders are shipping with blue ice. |
| 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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