Analytical Data
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Gene name
MRPL37
- Application
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Alternative Names
MRPL37; MRPL2; RPML2; HSPC235; 39S ribosomal protein L37; mitochondrial; L37mt; MRP-L37; 39S ribosomal protein L2; mitochondrial; L2mt; MRP-L2; Mitochondrial large ribosomal subunit protein mL37
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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
Q9BZE1
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Expression Region
30-423 aa
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AA Sequence
A YEWGVRSTRK SEPPPLDRVY EIPGLEPITF AGKMHFVPWL ARPIFPPWDR GYKDPRFYRS PPLHEHPLYK DQACYIFHHR CRLLEGVKQA LWLTKTKLIE GLPEKVLSLV DDPRNHIENQ DECVLNVISH ARLWQTTEEI PKRETYCPVI VDNLIQLCKS QILKHPSLAR RICVQNSTFS ATWNRESLLL QVRGSGGARL STKDPLPTIA SREEIEATKN HVLETFYPIS PIIDLHECNI YDVKNDTGFQ EGYPYPYPHT LYLLDKANLR PHRLQPDQLR AKMILFAFGS ALAQARLLYG NDAKVLEQPV VVQSVGTDGR VFHFLVFQLN TTDLDCNEGV KNLAWVDSDQ LLYQHFWCLP VIKKRVVVEP VGPVGFKPET FRKFLALYLH GAA
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Molecular Weight
48.1 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
MRPL37, a mitochondrial ribosomal protein, plays a crucial role in the protein synthesis within mitochondria, which are essential for cellular respiration and energy production. The importance of mitochondrial function in cellular metabolism and the pathogenesis of various diseases, including neurodegenerative disorders and cancers, has drawn significant research interest towards the molecular mechanisms involving mitochondrial ribosomal proteins. Specifically, MRPL37 is part of the mitochondrial ribosomal large subunit and is thought to participate in the translation of mitochondrial mRNAs, influencing mitochondrial biogenesis and function. Alterations in MRPL37 expression or function can lead to impaired mitochondrial protein synthesis, contributing to mitochondrial dysfunction, which is a hallmark of several diseases. Recent studies have focused on characterizing MRPL37 through recombinant protein techniques to better understand its structure, function, and regulatory mechanisms. By producing MRPL37 as a recombinant protein, researchers aim to investigate its interactions with mitochondrial mRNAs and other ribosomal proteins, as well as its involvement in mitochondrial dynamics and stress responses. This research could provide valuable insights into the role of MRPL37 in health and disease, potentially unveiling new therapeutic targets for conditions linked to mitochondrial dysfunction. Understanding the intricacies of MRPL37’s function thus represents a significant avenue for advancing our knowledge of mitochondrial biology and its implications in human health.
