Analytical Data
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Gene name
RER1
- Application
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Alternative Names
RER1; Protein RER1
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O15258
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Expression Region
1-196 aa
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AA Sequence
MSEGDSVGESVHGKPSVVYRFFTRLGQIYQSWLDKSTPYTAVRWVVTLGLSFVYMIRVYLLQGWYIVTYALGIYHLNLFIAFLSPKVDPSLMEDSDDGPSLPTKQNEEFRPFIRRLPEFKFWHAATKGILVAMVCTFFDAFNVPVFWPILVMYFIMLFCITMKRQIKHMIKYRYIPFTHGKRRYRGKEDAGKAFAS
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Molecular Weight
47.19 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
RER1 (Retention in Endoplasmic Reticulum 1) is a protein that plays a crucial role in the quality control of protein trafficking within cells. Located in the endoplasmic reticulum (ER), RER1 is responsible for retaining unassembled or misfolded proteins, thus ensuring that only properly folded proteins are transported to their final destinations. The study of RER1 has garnered increasing interest due to its implications in various cellular processes and disease states. For instance, aberrations in the function of RER1 can lead to the accumulation of dysfunctional proteins, contributing to disorders such as neurodegenerative diseases and certain types of cancer. Researchers have been exploring the mechanisms by which RER1 interacts with other chaperone proteins and its role in the UPR (unfolded protein response) pathway, which is activated under stress conditions. Recombinant RER1 proteins are being developed and analyzed to better understand their structure-function relationships and to identify potential therapeutic targets for diseases arising from protein misfolding and trafficking defects. Understanding RER1's exact functions and interactions within the cell could pave the way for novel strategies in the treatment and prevention of related diseases, making it a significant focus in molecular and cell biology research.
