Analytical Data
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Gene name
RBPMS
- Application
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Alternative Names
Heart and RRM expressed sequence (Hermes) (RBP-MS) (HERMES)
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Species
Human
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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
Q93062
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Expression Region
1-196aa
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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 associated with a novel muscle-specific transcript) is a member of the RNA-binding protein family known for its involvement in various cellular processes, including RNA splicing, stability, and translation regulation. The study of RBPMS has garnered attention due to its significant role in muscle development and its potential implications in diseases such as cancer and neuromuscular disorders. Recent research has highlighted its function in modulating gene expression through interactions with specific RNA targets, which can influence cellular fate and differentiation. The investigation of RBPMS recombinant proteins allows for a deeper understanding of its biological activities and mechanisms, facilitating the exploration of its functions in both physiological and pathological contexts. Additionally, the expression and purification of RBPMS as a recombinant protein can provide valuable insights into its structure-function relationships, offering clues for therapeutic targeting in diseases associated with RNA dysregulation. Overall, the ongoing research into RBPMS is poised to elucidate critical aspects of RNA biology and its impact on health and disease.
