Analytical Data
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Gene name
Trap1a
- Application
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Alternative Names
Trap1a；P1a；Tumor rejection antigen P815A
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Species
Mouse
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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
P19473
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Expression Region
1-134aa
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AA Sequence
MSDNKKPDKAHSGSGGDGDGNRCNLLHRYSLEEILPYLGWLVFAVVTTSFLALQMFIDALYEEQYERDVAWIARQSKRMSSVDEDEDDEDDEDDYYDDEDDDDDAFYDDEDDEEEELENLMDDESEDEAEEEMS
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Molecular Weight
23.1 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
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Protein Description
Trap1a, a mitochondrial chaperone protein, plays a crucial role in maintaining mitochondrial function and cellular homeostasis. It is part of the heat shock protein (HSP) family and is implicated in various cellular processes, including mitochondrial protein folding, prevention of oxidative stress, and regulation of apoptosis. Research has shown that Trap1a interacts with numerous mitochondrial proteins and is involved in the management of protein misfolding, which is essential for mitochondrial integrity under stress conditions. Dysregulation of Trap1a has been linked to several diseases, including neurodegenerative disorders and cancer, where altered mitochondrial dynamics and stress responses are observed. The study of recombinant Trap1a proteins has gained attention as scientists seek to elucidate its precise functions and mechanisms, which are vital for the development of therapeutic strategies aimed at mitigating mitochondrial dysfunction. Understanding the structural and functional properties of Trap1a through recombinant protein studies can provide insights into its role in cellular protection and might offer potential avenues for intervention in mitochondrial-related diseases. This research is particularly significant in the context of aging and diseases marked by mitochondrial pathologies, as enhancing Trap1a activity could prove beneficial in promoting cellular resilience and health.
