Analytical Data
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Gene name
MRPL20
- Application
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Alternative Names
MRPL20; 39S ribosomal protein L20; mitochondrial; L20mt; MRP-L20; Mitochondrial large ribosomal subunit protein bL20m
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9BYC9
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Expression Region
46-149aa
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Molecular Weight
27.8 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
MRPL20, or Mitochondrial Ribosomal Protein L20, is a crucial component of the mitochondrial ribosome, playing an essential role in protein synthesis within mitochondria. Research into MRPL20 has gained traction due to its involvement in various cellular processes, including mitochondrial biogenesis and oxidative phosphorylation, which are vital for energy production and cellular metabolism. Mutations or dysregulation of MRPL20 have been linked to a variety of mitochondrial disorders, emphasizing its importance in maintaining mitochondrial function and overall cellular health. Given the rising incidence of diseases related to mitochondrial dysfunction, understanding the structure, function, and regulation of MRPL20 is pivotal for developing therapeutic strategies. Recent studies have employed advanced techniques, such as cryo-electron microscopy and functional assays, to elucidate its role in mitochondrial dynamics and stress response. By investigating MRPL20's interactions with other mitochondrial proteins and its contributions to the ribosomal assembly process, researchers aim to uncover novel insights into mitochondrial pathophysiology and potential interventions for mitochondrial diseases. This research not only deepens our understanding of mitochondrial biology but also holds promise for translating findings into clinical applications, addressing the challenges posed by mitochondrial dysfunction in human health. As the field progresses, continued exploration of MRPL20's molecular mechanisms will be crucial for developing targeted therapies to combat mitochondrial disorders and enhance our understanding of cellular energy metabolism.
