Analytical Data
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Gene name
MRPL30
- Application
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Alternative Names
MRPL30; MRPL28; RPML28; HSPC249; 39S ribosomal protein L30; mitochondrial; L30mt; MRP-L30; 39S ribosomal protein L28; mitochondrial; L28mt; MRP-L28; Mitochondrial large ribosomal subunit protein uL30m
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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
Q8TCC3
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Expression Region
35-161 aa
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AA Sequence
KFTRSR IPEKVFQASP EDHEKYGGDP QNPHKLHIVT RIKSTRRRPY WEKDIIKMLG LEKAHTPQVH KNIPSVNAKL KVVKHLIRIK PLKLPQGLPA EENMSNTCLK STGELVVQWH LKPVEQKAHE S
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Molecular Weight
18.5 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
MRPL30, or mitochondrial ribosomal protein L30, is a crucial component of the mitochondrial ribosome, playing a significant role in protein synthesis within mitochondria. Its involvement in decoding mitochondrial mRNA and facilitating the assembly of mitochondrial ribosomes underscores its importance in maintaining mitochondrial function and cellular energy metabolism. Research into MRPL30 has emerged due to growing concerns about mitochondrial dysfunction, which is linked to a variety of diseases, including neurodegenerative disorders, metabolic syndromes, and certain cancers. The study of MRPL30 offers insights into mitochondrial biology and the potential for targeted therapeutic strategies. Understanding its structure, function, and the mechanisms by which it contributes to mitochondrial ribosome assembly can shed light on the pathophysiology of diseases associated with mitochondrial malfunction. Advances in techniques such as X-ray crystallography and cryo-electron microscopy have provided valuable structural information, allowing researchers to explore the functional implications of MRPL30 mutations and their impact on mitochondrial translation. Moreover, investigating MRPL30 in the context of mitochondrial dynamics and interaction with other mitochondrial proteins is essential for painting a comprehensive picture of mitochondrial health. As research continues to unravel the complexities of MRPL30, its significance as a potential biomarker or therapeutic target in mitochondrial-related diseases is increasingly recognized, highlighting the necessity for further investigation in this promising area of study.
