Analytical Data
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Gene name
rgpA
- Application
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Alternative Names
rgpA；C20orf74；KIAA1272；Ral GTPase-activating Protein subunit alpha-2
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Species
E.coli
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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
P28784
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Expression Region
228-720aa
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AA Sequence
YTPVEEKQNGRMIVIVAKKYEGDIKDFVDWKNQRGLRTEVKVAEDIASPVTANAIQQFVKQEYEKEGNDLTYVLLVGDHKDIPAKITPGIKSDQVYGQIVGNDHYNEVFIGRFSCESKEDLKTQIDRTIHYERNITTEDKWLGQALCIASAEGGPSADNGESDIQHENVIANLLTQYGYTKIIKCYDPGVTPKNIIDAFNGGISLVNYTGHGSETAWGTSHFGTTHVKQLTNSNQLPFIFDVACVNGDFLFSMPCFAEALMRAQKDGKPTGTVAIIASTINQSWASPMRGQDEMNEILCEKHPNNIKRTFGGVTMNGMFAMVEKYKKDGEKMLDTWTVFGDPSLLVRTLVPTKMQVTAPAQINLTDASVNVSCDYNGAIATISANGKMFGSAVVENGTATINLTGLTNESTLTLTVVGYNKETVIKTINTNGEPNPYQPVSNLTATTQGQKVTLKWDAPSTKTNATTNTARSVDGIRELVLLSVSDAPELLRS
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Molecular Weight
56.0 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
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Protein Description
RgpA, or ribonuclease G (RnpA), is a protein of significant interest in molecular biology due to its role as a key enzyme in ribonucleic acid (RNA) processing and degradation in various prokaryotic organisms. The study of RgpA has gained traction due to its potential implications in understanding bacterial physiology, pathogenesis, and the development of new antimicrobial agents. RgpA is involved in the maturation of ribonuclease P, an essential enzyme required for the processing of precursor tRNA molecules, which are critical for protein synthesis. The investigation of RgpA through recombinant protein technology allows researchers to produce and characterize the protein in vitro, enabling detailed studies of its structure, function, and regulatory mechanisms. Additionally, understanding the enzymatic activity of RgpA can provide insights into its role in bacterial RNA metabolism, which may lead to novel therapeutic strategies targeting bacterial infections. The recombinant expression of RgpA facilitates high-yield production for biophysical techniques like X-ray crystallography and nuclear magnetic resonance (NMR), thereby advancing our knowledge of RNA-protein interactions. Furthermore, elucidating the mechanisms by which RgpA and similar enzymes function can enhance our comprehension of RNA degradation pathways, ultimately contributing to the broader field of molecular genetics and biotechnology. As antibiotic resistance becomes a growing concern in clinical settings, exploring the dynamics and interactions of RgpA's role in bacterial systems underscores the importance of this research in developing innovative solutions to combat resistant bacterial strains and improve therapeutic outcomes.
