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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human AFG3L2 Protein, N-His |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 54.14 kDa |
Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
Form | Liquid |
Delivery condition | Dry Ice |
Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
Storage condition | 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection) |
Brand | Arovia |
Host species | Escherichia coli (E.coli) |
Fragment Type | Lys297-Ser765 |
Aliases /Synonyms | AFG3-like protein 2, AFG3L2, Paraplegin-like protein |
Reference | YHK41901 |
Note | For research use only. |
Recombinant Human AFG3L2 Protein, also known as ATP-dependent zinc metalloprotease AFG3L2, is a member of the AAA (ATPases associated with diverse cellular activities) family of proteins. It is encoded by the AFG3L2 gene and is found in both the cytoplasm and mitochondria of human cells.
The AFG3L2 protein consists of 825 amino acids and has a molecular weight of approximately 93 kDa. It is composed of three domains: an N-terminal domain, a central domain, and a C-terminal domain. The N-terminal domain contains a zinc-binding motif and is responsible for the protease activity of AFG3L2. The central domain is involved in protein-protein interactions, while the C-terminal domain is responsible for the ATPase activity of the protein.
The structure of AFG3L2 is highly conserved among different species, indicating its importance in cellular processes. It is also known to form oligomeric complexes with other proteins, such as SPG7 and paraplegin, to carry out its functions.
AFG3L2 is a key component of the mitochondrial quality control system, which is responsible for maintaining the integrity and function of mitochondria. It acts as a protease, breaking down damaged or misfolded proteins in the mitochondria, thus preventing their accumulation and potential toxicity.
In addition to its role in protein quality control, AFG3L2 also plays a crucial role in mitochondrial biogenesis, the process by which new mitochondria are formed. It is involved in the assembly and maintenance of the mitochondrial respiratory chain, which is responsible for producing ATP, the main energy source of the cell.
Furthermore, AFG3L2 has been shown to play a role in regulating apoptosis, or programmed cell death, by interacting with and cleaving pro-apoptotic proteins. This highlights the diverse functions of AFG3L2 in maintaining cellular homeostasis.
The use of recombinant AFG3L2 protein has been instrumental in studying its structure and function, as well as its role in various cellular processes. It can be produced in large quantities using recombinant DNA technology, making it a valuable tool for research and potential therapeutic applications.
One potential application of recombinant AFG3L2 protein is in the treatment of neurodegenerative diseases. Mutations in the AFG3L2 gene have been linked to spinocerebellar ataxia type 28 (SCA28), a rare neurodegenerative disorder characterized by progressive loss of coordination and balance. Studies have shown that recombinant AFG3L2 protein can rescue the defective mitochondrial function in cells carrying these mutations, providing a potential therapeutic avenue for SCA28 and other related diseases.
Recombinant AFG3L2 protein has also been used in studies to understand its role in mitochondrial diseases, such as Leigh syndrome, a severe neurological disorder caused by mutations in mitochondrial DNA. These studies have provided insights into the mechanisms underlying these diseases and have potential implications for developing targeted therapies.
In summary, Recombinant Human AFG3L2 Protein is a multifunctional protein with important roles in maintaining mitochondrial function and cellular homeostasis. Its structure, activity, and applications have been extensively studied, and it holds potential for therapeutic use in various diseases. Further research on this protein will continue to provide valuable insights into its functions and potential clinical applications.
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