Cat: PA2000-7405

Recombinant Human ERO1L Protein,GST

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Analytical Data

  • Gene name

    ERO1L

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Endoplasmic oxidoreductin 1 like protein; Endoplasmic oxidoreductin-1-like protein; Endoplasmic reticulum oxidoreductase 1 alpha; Endoplasmic reticulum oxidoreductin 1-like; ERO1 alpha; ERO1 L; ERO1 Lalpha; ERO1 like protein alpha; ERO1-alpha; ERO1-L; ERO1-L-alpha; ERO1-like (S. cerevisiae); ERO1-like alpha; ERO1-like protein alpha; ERO1-like

  • Species

    Human

  • Source

    E. coli

  • Tag

    GST-tag at N-terminal

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q96HE7

  • Expression Region

    1-468aa

  • AA Sequence

    MGRGWGFLFGLLGAVWLLSSGHGEEQPPETAAQRCFCQVSGYLDDCTCDVETIDRFNNYRLFPRLQKLLESDYFRYYKVNLKRPCPFWNDISQCGRRDCAVKPCQSDEVPDGIKSASYKYSEEANNLIEECEQAERLGAVDESLSEETQKAVLQWTKHDDSSDNFCEADDIQSPEAEYVDLLLNPERYTGYKGPDAWKIWNVIYEENCFKPQTIKRPLNPLASGQGTSEENTFYSWLEGLCVEKRAFYRLISGLHASINVHLSARYLLQETWLEKKWGHNITEFQQRFDGILTEGEGPRRLKNLYFLYLIELRALSKVLPFFERPDFQLFTGNKIQDEENKMLLLEILHEIKSFPLHFDENSFFAGDKKEAHKLKEDFRLHFRNISRIMDCVGCFKCRLWGKLQTQGLGTALKILFSEKLIANMPESGPSYEFHLTRQEIVSLFNAFGRISTSVKKLENFRNLLQNIH

  • Molecular Weight

    80.8 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • 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.

  • 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.

  • 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

ERO1L, or Eukaryotic Oxidoreductin 1-Like, is a crucial protein involved in the formation and maintenance of disulfide bonds in the endoplasmic reticulum (ER), which is essential for the proper folding and maturation of secretory and membrane proteins. The ER is a critical organelle in eukaryotic cells, responsible for protein synthesis and processing. ERO1L facilitates oxidative protein folding by transferring electrons from protein disulfide isomerase (PDI) to molecular oxygen, leading to the production of reactive oxygen species (ROS). This process is vital for cellular homeostasis, and dysfunction in ERO1L has been linked to various diseases, including neurodegenerative disorders and cancer. Research on ERO1L recombinant protein has gained momentum due to its potential therapeutic implications and its role in understanding ER stress response mechanisms. Scientists are investigating the structural and functional properties of ERO1L to gain insights into its enzymatic activity and regulation, aiming to explore its potential as a biomarker or therapeutic target in diseases associated with ER stress. Moreover, ERO1L's involvement in redox biology highlights its significance in cellular signaling and metabolic pathways, marking it as a protein of interest in both basic and applied research contexts. Understanding the intricate workings of ERO1L could pave the way for innovative strategies to mitigate diseases stemming from ER dysfunction, solidifying its position as a critical focus in molecular and cellular biology research.

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