Analytical Data
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Gene name
RPP38
- Application
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Alternative Names
RPP38; Ribonuclease P protein subunit p38; RNaseP protein p38; EC 3.1.26.5
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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
P78345
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Expression Region
2-283 aa
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AA Sequence
AAAPQAPGR GSLRKTRPLV VKTSLNNPYI IRWSALESED MHFILQTLED RLKAIGLQKI EDKKKKNKTP FLKKESREKC SIAVDISENL KEKKTDAKQQ VSGWTPAHVR KQLAIGVNEV TRALERRELL LVLVCKSVKP AMITSHLIQL SLSRSVPACQ VPRLSERIAP VIGLKCVLAL AFKKNTTDFV DEVRAIIPRV PSLSVPWLQD RIEDSGENLE TEPLESQDRE LLDTSFEDLS KPKRKLADGR QASVTLQPLK IKKLIPNPNK IRKPPKSKKA TPK
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Molecular Weight
31.8 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
RPP38, also known as ribonuclease P protein subunit p38, is a crucial component of the ribonuclease P (RNase P) complex, which is responsible for generating mature tRNA molecules by cleaving precursor tRNA transcripts. Research on RPP38 has garnered attention due to its essential role in basic cellular processes, particularly in the maturation of tRNA, which is vital for protein synthesis and overall cellular function. The study of RPP38 is pivotal not only for understanding tRNA biosynthesis but also for exploring its implications in various diseases, including cancers and genetic disorders. Abnormal expression or mutations in RPP38 have been implicated in tumorigenesis, highlighting the importance of characterizing this protein for potential therapeutic interventions. Additionally, with advancements in recombinant protein technology, the production of RPP38 in a laboratory setting allows researchers to study its structure, function, and interaction with other RNase P components, paving the way for novel insights into tRNA processing and the regulation of gene expression. As a result, RPP38 serves as a significant model for understanding the mechanistic underpinnings of RNase P activity and its broader implications in cellular biology and disease.
