Analytical Data
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Gene name
ERLIN1
- Application
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Alternative Names
Endoplasmic reticulum lipid raft-associated protein 1 Protein KE04 Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 1 Short name: SPFH domain-containing protein 1
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O75477
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Expression Region
1-348aa
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Molecular Weight
42.0 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
ERLIN1 (Endoplasmic Reticulum Lingual 1) is a protein that plays a significant role in cellular processes, particularly in the regulation of endoplasmic reticulum (ER) functions and associated pathways. Recent studies have highlighted its involvement in modulating the ER stress response, which is crucial for maintaining cellular homeostasis, particularly in conditions of metabolic stress or pathological states. The protein has been implicated in several cellular mechanisms, including lipid metabolism, protein folding, and apoptosis, suggesting that it may have broader implications in diseases such as neurodegeneration and metabolic disorders. Recombining ERLIN1 allows researchers to produce large quantities of the protein for detailed functional studies, facilitating the exploration of its molecular mechanisms, interactions, and potential therapeutic targets. Understanding ERLIN1's precise biochemical roles could result in novel insights into how cells adapt to stress and may pave the way for developing strategies to mitigate diseases associated with ER dysfunction. Given the protein's relevance in health and disease, ERLIN1 remains an important subject of research in cellular biology and therapeutic development.
