Analytical Data
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Gene name
MRO
- Application
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Alternative Names
B29; beside the Ma29 deletion; C18orf3; Male-specific transcription in the developing reproductive organs; Mro; MSTRO_HUMAN; Protein B29; Protein maestro
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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
Q9BYG7
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Expression Region
1-248 aa
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AA Sequence
MDQRQRRILG QPLSIPTSQP KQKRTSMISF FSKVSWKLRF QKREPLKNVF FILAERARDP SAKKRHMAMR NLGTMAYEAP DKVRKYKKIV LDLLVYGLYD PVNLEVIHES MKTLTVVLGK IQGKGLGSFF IDITLQTRTL LDDENDSLRY SAFVLFGQLA AFAGRKWKKF FTSQVKQTRD SLLIHLQDRN PQVAKACKTT FQACSPYLKL KEEYSFQSEE DQRNTKLYQQ LSHYHPEILQ FFYANKIL
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Molecular Weight
29.0 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
MRO (Mitochondrial Ribosomal Protein) reorganization has emerged as a significant area of research due to its crucial role in mitochondrial function and cellular metabolism. Mitochondria, known as the powerhouse of the cell, are responsible for energy production through oxidative phosphorylation, which requires a finely tuned balance of mitochondrial and nuclear gene expression. The MRO proteins are essential components of the mitochondrial ribosome, facilitating translation during protein synthesis. Recent studies have revealed that alterations in the expression and function of MRO proteins are linked to various metabolic disorders and mitochondrial diseases, including diabetes, neurodegenerative conditions, and certain myopathies. Additionally, MRO proteins are now recognized for their involvement in stress responses and apoptosis, further highlighting their importance in maintaining cellular homeostasis. The investigation of MRO protein dynamics and their interactions with other mitochondrial components can provide insights into the molecular mechanisms underlying mitochondrial dysfunction. This research may pave the way for novel therapeutic strategies aimed at rectifying mitochondrial impairments, emphasizing the relevance of MRO proteins in health and disease. Understanding how MRO reorganization influences mitochondrial activity and overall cellular physiology remains a key challenge in contemporary biomedical research, making it a vital topic of interest in the fields of genetics, molecular biology, and medicine.
