Analytical Data
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Gene name
RPP30
- Application
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Alternative Names
RPP30;RNASEP2;Ribonuclease P Protein subunit p30
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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
P78346
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Expression Region
1-268aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMAVFADLDLRAGSDLKALRGLVETAAH LGYSVVAINHIVDFKEKKQEIEKPVAVSELFTTLPIVQGKSRPIKILTRL TIIVSDPSHCNVLRATSSRARLYDVVAVFPKTEKLFHIACTHLDVDLVCI TVTEKLPFYFKRPPINVAIDRGLAFELVYSPAIKDSTMRRYTISSALNLM QICKGKNVIISSAAERPLEIRGPYDVANLGLLFGLSESDAKAAVSTNCRA ALLHGETRKTAFGIISTVKKPRPSEGDEDCLPASKKAKCEG
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Molecular Weight
32 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
RPP30, or ribonuclease P protein subunit 30, is a crucial component of ribonuclease P, an essential endonuclease involved in the processing of precursor tRNA molecules. The significance of RPP30 in various biochemical pathways highlights its role in cellular function and gene expression regulation. Research has shown that abnormalities in RPP30 can be associated with several diseases, including autoimmune disorders and certain cancers, making it a potential biomarker for disease progression and a target for therapeutic intervention. Moreover, recombinant versions of RPP30 have been developed to facilitate detailed studies of its folding, interaction with RNA substrates, and functional assays, aiding our understanding of its role in tRNA maturation and ribonucleoprotein complex formation. Investigating the structural and functional properties of RPP30 through recombinant protein studies can provide insights into the mechanisms underlying its enzymatic activity and regulation, paving the way for novel approaches to target related diseases. The ongoing research into RPP30 and its implications in health and disease underscores the importance of this protein in molecular biology and biomedicine.
