Analytical Data
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Gene name
ERH
- Application
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Alternative Names
ERH;Enhancer of rudimentary homolog
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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
P84090
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Expression Region
1-104aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMSHTILLVQPTKRPEGRTYADYESVNE CMEGVCKMYEEHLKRMNPNSPSITYDISQLFDFIDDLADLSCLVYRADTQ TYQPYNKDWIKEKIYVLLRRQAQQAGK
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Molecular Weight
15 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
The study of ERH (Enhancer of Rudimentary Homolog) recombinant protein is rooted in its crucial role in various biological processes, including RNA metabolism, cellular proliferation, and differentiation. ERH is a highly conserved protein across species, suggesting its fundamental importance in cellular functions. Recent research has highlighted its involvement in the regulation of gene expression and the potential mechanism of action related to cancer development and other diseases. The recombinant form of ERH facilitates detailed biochemical studies, allowing researchers to investigate its interactions with other proteins and cellular components. This research is essential for understanding the precise functions of ERH and its implications in human health. Furthermore, characterizing ERH in a recombinant form provides a valuable tool for drug discovery and the development of novel therapeutic strategies. By studying ERH, scientists aim to uncover potential biomarkers for disease progression and identify new targets for intervention, ultimately paving the way for advances in molecular medicine.
