Analytical Data
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Gene name
RBM38
- Application
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Alternative Names
RNPC1; SEB4
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Species
Human
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Source
E. coli
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Tag
His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H0Z9-1
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Expression Region
G26-G121
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Protein Length
Partial
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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
RBM38, or RNA-binding motif protein 38, is a member of the RNA-binding protein family that plays a crucial role in post-transcriptional gene regulation. It is known for its involvement in mRNA stability, splicing, and translation modulation, thus influencing various cellular processes such as proliferation, differentiation, and stress responses. Recent studies have highlighted RBM38's potential implications in various diseases, including cancer, where its altered expression levels are associated with tumorigenesis and poor prognosis. Researchers are particularly interested in the recombinant protein form of RBM38, which allows for in-depth investigations into its functional mechanisms and interactions with other RNA-binding proteins. By producing RBM38 as a recombinant protein, scientists can better understand its structural characteristics, binding affinities, and the specific mRNA targets it interacts with. Furthermore, this research can pave the way for therapeutic applications, potentially enabling the development of strategies to manipulate RBM38 activity in disease contexts. Ongoing studies aim to elucidate the precise pathways mediated by RBM38 in cellular contexts, contributing to a deeper understanding of its biological significance and providing insights for potential biomedical interventions.
