Analytical Data
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Gene name
RPRM
- Application
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Alternative Names
RPRM；Protein reprimo
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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
Q9NS64
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Expression Region
1-109aa
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AA Sequence
MNPALGNQTDVAGLFLANSSEALERAVRCCTQASVVTDDGFAEGGPDERSLYIMRVVQIAVMCVLSLTVVFGIFFLGCNLLIKSEGMINFLVKDRRPSKEVEAVVVGPY
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Molecular Weight
11.7 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
RPRM (Reprogramming Protein) is an essential protein that has garnered significant interest in the field of molecular biology due to its role in cellular processes such as growth, differentiation, and apoptosis. Research has shown that RPRM is involved in the regulation of stem cell pluripotency and the reprogramming of differentiated cells back to a pluripotent state, making it a crucial factor in regenerative medicine and cancer research. Dysregulation of RPRM expression has been implicated in various malignancies, suggesting that it could serve as a potential biomarker for cancer diagnosis and prognosis. Furthermore, studies have indicated that RPRM interacts with several key signaling pathways, which makes it a suitable target for therapeutic interventions. Understanding the structure and function of RPRM at the molecular level is vital for harnessing its potential in developing novel treatments, particularly in targeting cancer stem cells that contribute to tumor recurrence and metastasis. With advancements in protein engineering techniques, researchers aim to explore the functional properties of RPRM in greater depth, paving the way for innovative strategies in cancer therapy and stem cell biology. Overall, the ongoing investigations into RPRM not only enhance our comprehension of fundamental biological processes but also hold promise for the future of personalized medicine.
