Analytical Data
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Gene name
KDELR2
- Application
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Alternative Names
KDELR2; ERD2.2; ER lumen protein-retaining receptor 2; ERD2-like protein 1; ELP-1; KDEL endoplasmic reticulum protein retention receptor 2; KDEL receptor 2
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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
P33947
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Expression Region
1-212aa
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AA Sequence
MNIFRLTGDLSHLAAIVILLLKIWKTRSCAGISGKSQLLFALVFTTRYLDLFTSFISLYNTSMKVIYLACSYATVYLIYLKFKATYDGNHDTFRVEFLVVPVGGLSFLVNHDFSPLEILWTFSIYLESVAILPQLFMISKTGEAETITTHYLFFLGLYRALYLVNWIWRFYFEGFFDLIAVVAGVVQTILYCDFFYLYITKVLKGKKLSLPA
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Molecular Weight
50.8 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
KDELR2, or KDEL receptor 2, is a crucial component of the cellular quality control system, primarily involved in the retrieval of misfolded proteins from the endoplasmic reticulum (ER) back to the ER for proper folding. This receptor plays a vital role in maintaining cellular homeostasis and protein stability, making it a key subject of study in the field of molecular biology and biochemistry. Understanding its function and mechanism is particularly important in the context of various diseases, including neurodegenerative disorders and certain cancers, where protein misfolding and accumulation are prominent features. Research on KDELR2 has expanded to explore its structural properties, ligand interactions, and signaling pathways, which are essential for its function. Insights gained from such studies could lead to novel therapeutic approaches targeting protein misfolding diseases by enhancing ER quality control mechanisms or by developing small molecules that modulate KDELR2 activity. Thus, the investigation of KDELR2 recombinant proteins not only enriches our understanding of intracellular transport systems but also holds potential for significant biomedical applications.
