Analytical Data
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Gene name
MRPL38
- Application
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Alternative Names
MRPL38; HSPC262; 39S ribosomal protein L38; mitochondrial; L38mt; MRP-L38; Mitochondrial large ribosomal subunit protein mL38
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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
Q96DV4
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Expression Region
27-380 aa
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AA Sequence
RRTP PLGPMPNSDI DLSNLERLEK YRSFDRYRRR AEQEAQAPHW WRTYREYFGE KTDPKEKIDI GLPPPKVSRT QQLLERKQAI QELRANVEEE RAARLRTASV PLDAVRAEWE RTCGPYHKQR LAEYYGLYRD LFHGATFVPR VPLHVAYAVG EDDLMPVYCG NEVTPTEAAQ APEVTYEAEE GSLWTLLLTS LDGHLLEPDA EYLHWLLTNI PGNRVAEGQV TCPYLPPFPA RGSGIHRLAF LLFKQDQPID FSEDARPSPC YQLAQRTFRT FDFYKKHQET MTPAGLSFFQ CRWDDSVTYI FHQLLDMREP VFEFVRPPPY HPKQKRFPHR QPLRYLDRYR DSHEPTYGIY
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Molecular Weight
44.5 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
MRPL38, a mitochondrial ribosomal protein, plays a crucial role in protein synthesis within mitochondria, which are essential for cellular energy production and metabolism. Recent studies have highlighted its significance in various biological processes, including mitochondrial biogenesis, stress responses, and regulation of apoptosis. Aberrations in MRPL38 expression and function have been linked to several diseases, including certain types of cancer and mitochondrial disorders. Understanding the structure and function of MRPL38 is imperative for elucidating its role in these pathological conditions. The study of recombinantly expressed MRPL38 not only enhances our knowledge of mitochondrial ribosome assembly and function but also provides potential insights into therapeutic targets for mitochondrial-related diseases. Through the generation of recombinant MRPL38, researchers can investigate its interactions with other mitochondrial components and its impact on mitochondrial protein synthesis. This research holds promise for uncovering novel mechanisms underlying mitochondrial dysfunction and opens avenues for the development of new strategies in disease prevention and treatment.
