Analytical Data
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Gene name
rpmH
- Application
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Alternative Names
rpmH；Large ribosomal subunit Protein bL34m
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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
P0A7P5
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Expression Region
1-46aa
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AA Sequence
MKRTFQPSVLKRNRSHGFRARMATKNGRQVLARRRAKGRARLTVSK
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Molecular Weight
32.4 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
Recombinant protein production has become a pivotal approach in biotechnology and pharmaceutical industries, enabling the development of therapeutic proteins, vaccines, and diagnostic tools. Among various recombinant proteins, the rpmH protein, a crucial component of the ribonuclease P complex, has garnered attention due to its role in RNA processing and stability. Understanding the function and structure of rpmH is vital for elucidating the mechanisms of ribonucleoprotein complexes and their involvement in cellular processes. The study of rpmH also has implications for understanding bacterial pathogenesis, as many pathogenic bacteria rely on ribonuclease P for survival and virulence. Advances in molecular cloning techniques and expression systems have facilitated the efficient production of recombinant rpmH, allowing researchers to investigate its biochemical properties and interactions in detail. This research not only enhances our understanding of fundamental cellular mechanisms but also opens avenues for the development of novel therapeutic strategies targeting bacterial infections. Investigating rpmH and its associated pathways provides insight into potential drug targets and diagnostic biomarkers, highlighting the importance of recombinant protein studies in the context of both basic science and applied biomedical research.
