Analytical Data
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Gene name
RPLP2
- Application
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Alternative Names
RPLP2；D11S2243E；RPP2；Large ribosomal subunit Protein P2
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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
P05387
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Expression Region
1-115aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMRYVAS YLLAALGGNS SPSAKDIKKI LDSVGIEADD DRLNKVISEL NGKNIEDVIA QGIGKLASVP AGGAVAVSAA PGSAAPAAGS APAAAEEKKD EKKEESEESD DDMGFGLFD
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Molecular Weight
14 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
RPLP2, or Ribosomal Protein Lateral Stalk Subunit P2, is a critical component of the ribosomal stalk complex, which plays a vital role in the translation process of protein synthesis in cells. Recent research has highlighted its importance in regulating ribosomal function and its potential implications in various diseases, including cancer. Understanding the structure and function of RPLP2, especially through the study of its recombinant protein, is crucial for elucidating its role in the ribosomal machinery. Recombinant RPLP2 can be expressed and purified for detailed biochemical and biophysical characterization, enabling researchers to investigate its interactions with other ribosomal proteins and translation factors. Additionally, studies on RPLP2 can provide insights into post-translational modifications and how they affect ribosome activity. Given that alterations in ribosomal proteins like RPLP2 have been linked to tumorigenesis and other pathological conditions, this research has the potential to contribute to the development of novel therapeutic strategies. The exploration of RPLP2 and its recombinant forms thus represents a significant field of study with implications for both fundamental biology and clinical applications.
