Analytical Data
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Gene name
Rpl7
- Application
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Species
Mouse
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P14148
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Expression Region
1-270aa
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Molecular Weight
38.9 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
Rpl7, a ribosomal protein, plays a crucial role in the assembly and function of the ribosome, the cellular machinery responsible for protein synthesis. Research on Rpl7 has garnered significant attention due to its implications in various biological processes, including cell growth, differentiation, and response to stress. Abnormal expression or mutations of Rpl7 have been linked to several diseases, including cancer, where altered ribosome biogenesis and function contribute to tumorigenesis. In addition, Rpl7 is involved in the regulation of mRNA translation, impacting the synthesis of proteins that govern key cellular pathways. Studies utilizing recombinant Rpl7 proteins aim to elucidate its structural and functional properties, allowing scientists to better understand its role in ribosome dynamics and its contribution to translational control. The development of recombinant Rpl7 offers valuable opportunities for biochemical assays and structural studies, providing insights into ribosomal assembly and function. Furthermore, this research can pave the way for novel therapeutic strategies targeting ribosome-related dysregulation in diseases, highlighting the importance of Rpl7 as a focal point in both fundamental and applied biomedical research.
