Analytical Data
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Gene name
ERO1A
- Application
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Alternative Names
ERO1A；ERO1L；ERO1-like Protein alpha
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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
Q96HE7
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Expression Region
24-468aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSEEQPPETAAQRCFCQVSGYLDDCTCDV ETIDRFNNYRLFPRLQKLLESDYFRYYKVNLKRPCPFWNDISQCGRRDCA VKPCQSDEVPDGIKSASYKYSEEANNLIEECEQAERLGAVDESLSEETQK AVLQWTKHDDSSDNFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIW NVIYEENCFKPQTIKRPLNPLASGQGTSEENTFYSWLEGLCVEKRAFYRL ISGLHASINVHLSARYLLQETWLEKKWGHNITEFQQRFDGILTEGEGPRR LKNLYFLYLIELRALSKVLPFFERPDFQLFTGNKIQDEENKMLLLEILHE IKSFPLHFDENSFFAGDKKEAHKLKEDFRLHFRNISRIMDCVGCFKCRLW GKLQTQGLGTALKILFSEKLIANMPESGPSYEFHLTRQEIVSLFNAFGRI STSVKELENFRNLLQNIH
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Molecular Weight
54 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
ERO1A, or Eukaryotic Ribosome Biogenesis 1A, is a crucial enzyme involved in the oxidative folding of proteins within the endoplasmic reticulum. Its primary function is to facilitate the formation of disulfide bonds in nascent polypeptides, which is essential for the proper folding and functionality of many secretory and membrane proteins. The study of ERO1A has garnered significant attention due to its implications in various biological processes and diseases, including cancer, neurodegenerative disorders, and metabolic syndromes. Recent research has revealed that dysregulation of ERO1A can lead to an accumulation of misfolded proteins, contributing to cellular stress responses and inflammation. Furthermore, ERO1A's role in maintaining redox homeostasis within the endoplasmic reticulum has positioned it as a potential therapeutic target for enhancing protein function or alleviating stress in cells. Investigating the mechanisms of ERO1A and its interactions with other molecular chaperones provides insights into the intricate balance of protein folding and quality control within the cell. Scientists are now utilizing recombinant DNA technology to produce ERO1A protein in various systems to study its biophysical properties and functional dynamics, aiming to unlock understanding that could lead to novel treatments for diseases associated with protein misfolding or ER stress. Overall, the exploration of ERO1A serves as a vital intersection of biochemistry, cell biology, and therapeutic development, highlighting the importance of protein homeostasis in health and disease.
