Analytical Data
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Gene name
ERLIN1
- Application
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Alternative Names
ERLIN1；C10orf69；KE04；KEO4；Erlin-1
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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
O75477
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Expression Region
1-348aa
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AA Sequence
MNMTQARVLVAAVVGLVAVLLYASIHKIEEGHLAVYYRGGALLTSPSGPGYHIMLPFITTFRSVQTTLQTDEVKNVPCGTSGGVMIYIDRIEVVNMLAPYAVFDIVRNYTADYDKTLIFNKIHHELNQFCSAHTLQEVYIELFDQIDENLKQALQKDLNLMAPGLTIQAVRVTKPKIPEAIRRNFELMEAEKTKLLIAAQKQKVVEKEAETERKKAVIEAEKIAQVAKIRFQQKVMEKETEKRISEIEDAAFLAREKAKADAEYYAAHKYATSNKHKLTPEYLELKKYQAIASNSKIYFGSNIPNMFVDSSCALKYSDIRTGRESSLPSKEALEPSGENVIQNKESTG
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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
Related Products
Protein Description
ERLIN1, or endoplasmic reticulum-enriched gene, is an important protein that has drawn attention due to its role in various cellular processes and diseases. Initially identified as a key player in endoplasmic reticulum (ER) function, ERLIN1 is involved in the regulation of protein quality control and ER-associated degradation pathways. Research suggests that it interacts with the E3 ubiquitin ligase complex, impacting the stability and turnover of misfolded proteins. Furthermore, ERLIN1 is implicated in the regulation of lipid metabolism and the immune response, making it a point of interest in studies related to metabolic disorders and autoimmune diseases. Recent investigations have also highlighted its potential association with cancer progression and the response to therapy, underscoring its relevance in oncological research. Given these roles, the expression, activity, and potential post-translational modifications of ERLIN1 have become key areas of study, with researchers exploring its full biological impact and possible therapeutic implications. Understanding the mechanisms underlying ERLIN1's function could provide insights into the development of novel treatment strategies for various diseases, making it a significant focus in the fields of molecular biology and medicine.
