Analytical Data
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Gene name
DRIM
- Application
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Alternative Names
UTP20; DRIM; Small subunit processome component 20 homolog; Down-regulated in metastasis protein; Novel nucleolar protein 73; NNP73; Protein Key-1A6
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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
O75691
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Expression Region
946-1053aa
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AA Sequence
LHQDQMVQKITLDCIMTYKHPHVLPYRENLQRLLEDRSFKEEIVHFSISEDNAVVKTAHRADLFPILMRILYGRMKNKTGSKTQGKSASGTRMAIVLRFLAGTQPEEI
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Molecular Weight
37.62 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
DRIM (dynamin-related interactor of mitophagy) proteins have emerged as a focal point in cellular research due to their pivotal roles in mitochondrial dynamics and the regulation of mitophagy, a selective degradation process that eliminates damaged mitochondria. As mitochondrial dysfunction is implicated in various diseases, including neurodegenerative disorders and cancer, understanding the mechanisms underlying DRIM function is crucial for developing therapeutic strategies. Research into DRIM proteins has revealed their involvement in various cellular processes, such as membrane fusion and fission, which are essential for maintaining mitochondrial integrity and cellular homeostasis. Moreover, the dysregulation of DRIM proteins can lead to impaired mitophagy, contributing to the accumulation of dysfunctional mitochondria and subsequent cellular stress. Advances in genetic and biochemical techniques have facilitated the exploration of DRIM protein interactions and their signaling pathways, providing insights into their functional roles. Ongoing studies aim to elucidate the structural and functional characteristics of DRIM proteins, which could pave the way for novel interventions in diseases characterized by mitochondrial dysfunction. By unraveling the complexities of DRIM protein interactions and their implications in health and disease, researchers hope to not only enhance our understanding of mitochondrial biology but also contribute to the development of innovative therapeutic approaches to combat mitochondrial-related pathologies.
