Analytical Data
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Gene name
MRPL33
- Application
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Alternative Names
39S ribosomal protein L33; L33mt; mitochondrial; MRP-L33; mRpL33; RM33_HUMAN
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Species
Human
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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
O75394
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Expression Region
1-65 aa
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AA Sequence
MFLSAVFFAK SKSKNILVRM VSEAGTGFCF NTKRNRLREK LTLLHYDPVV KQRVLFVEKK KIRSL
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Molecular Weight
7.6 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
MRPL33, a mitochondrial ribosomal protein, plays a crucial role in the protein synthesis machinery of mitochondria, which are vital for cellular energy production and metabolism. Research into MRPL33 has garnered attention due to its potential involvement in various cellular processes and diseases, particularly those related to mitochondrial dysfunction. Mitochondrial diseases, often characterized by energy deficiency and metabolic disturbances, have highlighted the importance of mitochondrial ribosomal proteins, as they are essential for the accurate assembly of mitochondrial ribosomes and, consequently, the synthesis of mitochondrial-encoded proteins. Furthermore, mutations in mitochondrial ribosomal proteins have been linked to conditions such as cardiomyopathies, neurodegenerative diseases, and age-related disorders. Understanding the structure and function of MRPL33 could provide insights into its mechanistic roles in mitochondrial biology and disease. Recent advances in recombinant protein technology have allowed for the production and study of MRPL33 in vitro, facilitating investigations into its interactions with other mitochondrial components and its implications in the translation process. Such studies are critical for developing targeted therapies for mitochondrial-related diseases and enhancing our overall understanding of mitochondrial functions within cells.
