Analytical Data
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Gene name
RBPMS
- Application
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Alternative Names
RBPMS；HERMES；RNA-binding Protein with multiple splicing
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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
Q93062
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Expression Region
1-196aa
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AA Sequence
MNNGGKAEKENTPSEANLQEEEVRTLFVSGLPLDIKPRELYLLFRPFKGYEGSLIKLTSKQPVGFVSFDSRSEAEAAKNALNGIRFDPEIPQTLRLEFAKANTKMAKNKLVGTPNPSTPLPNTVPQFIAREPYELTVPALYPSSPEVWAPYPLYPAELAPALPPPAFTYPASLHAQMRWLPPSEATSQGWKSRQFC
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Molecular Weight
28.8 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
RBPMS (RNA-binding protein with multiple splicing) is an important RNA-binding protein involved in various biological processes, including mRNA splicing, stability, and translation regulation. Its role has garnered significant attention in recent years due to its implication in diverse cellular functions and disease mechanisms, particularly in cancer. RBPMS participates in the regulation of gene expression and has been associated with mechanisms of tumorigenesis, where its expression levels can influence cell proliferation, differentiation, and apoptosis. Interestingly, RBPMS has been found to interact with various RNA molecules, modulating their metabolism and function. As a result, researchers have focused on the structure and function of RBPMS to understand its precise role at the molecular level. One key aspect of this research involves the production and characterization of recombinant RBPMS proteins, which serve as valuable tools for elucidating the protein's binding affinities, interaction partners, and functional implications in cellular pathways. Understanding the biochemical properties and functional mechanisms of RBPMS can provide insights into its potential as a therapeutic target and enhance our knowledge of RNA metabolism in health and disease contexts. In summary, the study of recombinant RBPMS not only enriches our understanding of RNA-binding proteins but also holds the promise for advancing therapeutic strategies against diseases where RBPMS plays a critical role.
