Analytical Data
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Gene name
TOMM22
- Application
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Alternative Names
TOMM22; TOM22; Mitochondrial import receptor subunit TOM22 homolog; hTom22; 1C9-2; Translocase of outer membrane 22 kDa subunit homolog
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NS69
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Expression Region
1-142 aa
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AA Sequence
MAAAVAAAGAGEPQSPDELLPKGDAEKPEEELEEDDDEELDETLSERLWGLTEMFPERVRSAAGATFDLSLFVAQKMYRFSRAALWIGTTSFMILVLPVVFETEKLQMEQQQQLQQRQILLGPNTGLSGGMPGALPSLPGKI
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Molecular Weight
41.36 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
TOMM22, part of the translocase of the outer mitochondrial membrane (TOM) complex, plays a critical role in the import of proteins into mitochondria, facilitating the translocation of precursor proteins across the outer mitochondrial membrane. Given the essential functions of mitochondria in energy production, metabolism, and apoptosis, dysregulation of TOMM22 has been implicated in various diseases, including neurodegenerative disorders and cancer. Research has increasingly focused on the molecular mechanisms underlying TOMM22's function and its interactions with other mitochondrial proteins, as understanding these pathways can offer insights into mitochondrial dysfunction. Additionally, the study of TOMM22 recombinant proteins aims to elucidate its structure-function relationships, potentially leading to novel therapeutic strategies targeting mitochondrial diseases. Consequently, producing and characterizing TOMM22 recombinant proteins is crucial for advancing our knowledge of mitochondrial biology and developing interventions for related pathologies.
