Analytical Data
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Gene name
RPL23
- Application
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Alternative Names
60S ribosomal protein L17; 60S ribosomal protein L23; L23; MGC111167; MGC117346; MGC72008; OTTHUMP00000164151; OTTHUMP00000164153; RL23_HUMAN; rpl23
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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
P62829
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Expression Region
1-140 aa
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AA Sequence
MSKRGRGGSS GAKFRISLGL PVGAVINCAD NTGAKNLYII SVKGIKGRLN RLPAAGVGDM VMATVKKGKP ELRKKVHPAV VIRQRKSYRR KDGVFLYFED NAGVIVNNKG EMKGSAITGP VAKECADLWP RIASNAGSIA
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Molecular Weight
14.8 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
RPL23, a key component of the ribosomal protein family, plays a crucial role in ribosome biogenesis and protein synthesis. Its involvement in these fundamental cellular processes has drawn significant attention in the field of molecular biology. Research indicates that RPL23 not only contributes to structural integrity of the ribosome but also participates in the regulation of various cellular functions, including cell cycle progression and apoptosis. Mutations or dysregulation of RPL23 have been implicated in several diseases, particularly cancer, where altered ribosome function can lead to uncontrolled cell proliferation. Consequently, scientists have been focusing on the recombinant expression of RPL23 to study its functional characteristics and interactions within the ribosomal assembly. By generating recombinant RPL23 protein, researchers aim to elucidate its precise role in translation and its potential as a therapeutic target. Furthermore, understanding the molecular mechanisms governing RPL23 could provide insights into ribosomal biogenesis and its implications in disease states, paving the way for novel strategies in cancer treatment and other disorders linked to ribosomal dysfunction. This research is vital, given the increasing recognition of the ribosome's role beyond protein synthesis, highlighting its importance in maintaining cellular homeostasis.
