Analytical Data
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Gene name
RPL10A
- Application
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Alternative Names
RPL10A；NEDD6；Large ribosomal subunit Protein uL1
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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
P62906
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Expression Region
1-217aa
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AA Sequence
MSSKVSRDTLYEAVREVLHGNQRKRRKFLETVELQISLKNYDPQKDKRFS GTVRLKSTPRPKFSVCVLGDQQHCDEAKAVDIPHMDIEALKKLNKNKKLV KKLAKKYDAFLASESLIKQIPRILGPGLNKAGKFPSLLTHNENMVAKVDE VKSTIKFQMKKVLCLAVAVGHVKMTDDELVYNIHLAVNFLVSLLKKNWQN VRALYIKSTMGKPQRLY
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Molecular Weight
51 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
RPL10A, a member of the ribosomal protein L10 family, is crucial for ribosome biogenesis and protein synthesis in eukaryotic cells. Recent studies have highlighted its role not only in maintaining ribosomal structure but also in influencing cellular processes such as growth, proliferation, and stress responses. Genetic mutations and alterations in the expression levels of RPL10A have been linked to various diseases, including cancer, where it may contribute to tumorigenesis through its impact on the translational landscape. Moreover, RPL10A has been implicated in neurodegenerative disorders, suggesting a broader significance in cellular homeostasis. Research into RPL10A recombinant proteins has gained traction, facilitating the study of its structural and functional properties, interactions with other ribosomal components, and its role in disease mechanisms. This area of study is particularly noteworthy given the potential for RPL10A-targeted therapies, as understanding its function at a molecular level could lead to novel interventions in conditions where its dysregulation plays a key role. Thus, investigating RPL10A recombinant proteins not only enhances our fundamental understanding of ribosome function but also holds promise for therapeutic advancements in various diseases linked to its dysfunction.
