Analytical Data
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Gene name
RPS12
- Application
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Alternative Names
RPS12;Small ribosomal subunit Protein eS12
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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
P25398
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Expression Region
1-132aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAEEGIA AGGVMDVNTA LQEVLKTALI HDGLARGIRE AAKALDKRQA HLCVLASNCD EPMYVKLVEA LCAEHQINLI KVDDNKKLGE WVGLCKIDRE GKPRKVVGCS CVVVKDYGKE SQAKDVIEEY FKCKK
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Molecular Weight
17 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
RPS12, or ribosomal protein S12, is a crucial component of the ribosomal machinery, playing an essential role in protein synthesis within the cell. Research into RPS12 has gained significance due to its involvement in the ribosome's structural integrity and functionality. Alterations in RPS12 can affect ribosome biogenesis and stability, leading to various cellular dysfunctions and diseases, including certain types of cancer. The interest in RPS12 is further fueled by its potential as a therapeutic target, given that aberrations in ribosomal proteins are often linked to tumorigenesis. Protein engineering and recombinant protein techniques have allowed researchers to produce RPS12 in a controlled manner, providing insights into its structural and functional properties. This knowledge is pivotal for understanding its role in translation and its implications in disease pathology. Additionally, the study of RPS12 and its interactions with other ribosomal proteins is important for unraveling the complexities of ribosome assembly and the regulation of gene expression, making it a vital focus in molecular biology and biochemistry.
