Analytical Data
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Gene name
AFG3L2
- Application
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Alternative Names
AFG3L2；Mitochondrial inner membrane m-AAA protease component AFG3L2
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Species
Human
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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
Q9Y4W6
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Expression Region
588-797aa
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AA Sequence
ADPLLKVSIIPRGKGLGYAQYLPKEQYLYTKEQLLDRMCMTLGGRVSEEIFFGRITTGAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDLPRQGDMVLEKPYSEATARLIDDEVRILINDAYKRTVALLTEKKADVEKVALLLLEKEVLDKNDMVELLGPRPFAEKSTYEEFVEGTGSLDEDTSLPEGLKDWNKEREKEKEEPPGEKVAN
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Molecular Weight
50.8 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
AFG3L2, a member of the AAA+ ATPase family, is primarily involved in mitochondrial function and is crucial for maintaining mitochondrial proteostasis. Mutations in the AFG3L2 gene have been linked to hereditary spastic paraplegia, a neurological disorder characterized by progressive weakness and stiffness of the legs. Research on the AFG3L2 recombinant protein has gained momentum due to its role in mitochondrial dynamics, including protein unfolding and degradation. Understanding the structure and function of the AFG3L2 protein can shed light on its involvement in mitochondrial-related diseases and may unveil therapeutic targets for conditions linked to mitochondrial dysfunction. Furthermore, recombinant AFG3L2 protein studies can facilitate the exploration of its activity in cellular models, enabling researchers to decipher the molecular mechanisms underlying its cytoprotective properties and interaction with other mitochondrial proteins. Investigating AFG3L2 holds promise for advancing our knowledge of mitochondrial biology and developing strategies to combat mitochondrial disorders.
