Analytical Data
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Gene name
RPL26L1
- Application
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Alternative Names
RPL26L1;RPL26P1;Ribosomal Protein uL24-like
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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
Q9UNX3
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Expression Region
1-145aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMKFNPFV TSDRSKNRKR HFNAPSHVRR KIMSSPLSKE LRQKYNVRSM PIRKDDEVQV VRGHYKGQQI GKVVQVYRKK YVIYIERVQR EKANGTTVHV GIHPSKVVIT RLKLDKDRKK ILERKAKSRQ VGKEKGKYKE ELIEKMQE
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Molecular Weight
20 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
RPL26L1, a member of the ribosomal protein family, has garnered significant attention in recent years due to its pivotal role in ribosome biogenesis and protein synthesis. This protein is integral to the assembly of the ribosomal subunits and is implicated in the regulation of various cellular processes, including cell growth and apoptosis. Research has shown that RPL26L1 is not only essential for maintaining the structural integrity of ribosomes but also plays a crucial part in the cellular response to stress, as it can influence the translation of specific mRNAs. Dysregulation of RPL26L1 has been associated with several diseases, particularly cancer, where altered ribosomal protein expression can contribute to tumorigenesis. As a result, the development of recombinant RPL26L1 proteins has become a focal point for studies aiming to elucidate its functional mechanisms and potential therapeutic implications. Through advanced techniques such as site-directed mutagenesis and protein purification, researchers explore how variations in RPL26L1 affect ribosomal activity and influence cellular responses. Additionally, understanding the interactions of RPL26L1 with other ribosomal proteins and RNA sequences is vital for unraveling its broader role in ribosomal function and gene expression regulation. The ongoing research not only highlights the importance of RPL26L1 in fundamental cellular processes but also its potential as a target for novel therapeutic strategies aimed at combatting diseases associated with ribosomal dysfunction.
