Analytical Data
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Gene name
MRPL12
- Application
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Alternative Names
5c5-2
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P52815
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Expression Region
1-198aa
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Molecular Weight
43.4 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
MRPL12, a mitochondrial ribosomal protein, plays a crucial role in protein synthesis within the mitochondria, which are essential for cellular energy production and metabolic regulation. Recent studies have highlighted its importance in various cellular processes, including apoptosis, oxidative stress response, and mitochondrial biogenesis. Given the role of mitochondrial dysfunction in numerous diseases, including neurodegenerative disorders and cancer, understanding the function and regulation of MRPL12 can provide insights into therapeutic targets for these conditions. Researchers have been investigating the structural and functional properties of MRPL12 through techniques such as recombinant protein expression, which enables the study of its interactions with other mitochondrial components and ribosomal subunits. Characterizing MRPL12's function may reveal significant details about mitochondrial dynamics and its implications in health and disease, ultimately contributing to the development of novel treatment strategies aimed at enhancing mitochondrial function or correcting defects associated with MRPL12 deficiency. This research emphasizes the critical necessity of investigating mitochondrial proteins like MRPL12 to unravel the complex web of cellular mechanisms that underpin normal physiology and pathological states.
