Analytical Data
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Gene name
RPL35A
- Application
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Alternative Names
Cell growth-inhibiting gene 33 protein
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P18077
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Expression Region
1-110aa
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Molecular Weight
28.5 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
RPL35A, a key component of the ribosomal large subunit, plays a critical role in ribosome biogenesis and protein synthesis in eukaryotic cells. Research on RPL35A has gained significant attention due to its involvement in various cellular processes, including cell growth, proliferation, and response to stress. Mutations or dysregulation of RPL35A have been linked to several diseases, including cancer, underscoring its potential as a therapeutic target. The study of RPL35A recombinant proteins has emerged as a valuable tool for elucidating its biological functions and interactions within the ribosomal complex. By expressing and purifying RPL35A in various systems, researchers aim to investigate its structural properties, binding affinities, and functional roles in translation. Understanding the dynamics of RPL35A at the molecular level could provide insights into the ribosomal assembly process and the mechanistic basis of its involvement in disease states. In addition, characterizing RPL35A in the context of ribosomal biogenesis could pave the way for the development of novel strategies to manipulate its function for therapeutic purposes, making it a focal point of modern molecular biology and biomedical research.
