Analytical Data
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Gene name
ERMP1
- Application
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Alternative Names
ERMP1; FXNA; KIAA1815Endoplasmic reticulum metallopeptidase 1; EC 3.4.-.-; Felix-ina
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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
Q7Z2K6
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Expression Region
1-317aa
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AA Sequence
MFIPYLYALYLIWAVFEMFTPILGRSGSEIPPDVVLASILAGCTMILSSYFINFIYLAKSTKKTMLTLTLVCAITFLLVCSGTFFPYSSNPANPKPKRVFLQHMTRTFHDLEGNAVKRDSGIWINGFDYTGISHITPHIPEINDSIRAHCEENAPLCGFPWYLPVHFLIRKNWYLPAPEVSPRNPPHFRLISKEQTPWDSIKLTFEATGPSHMSFYVRAHKGSTLSQWSLGNGTPVTSKGGDYFVFYSHGLQASAWQFWIEVQVSEEHPEGMVTVAIAAHYLSGEDKRSPQLDALKEKFPDWTFPSAWVCTYDLFVF
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Molecular Weight
62.4 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
ERMP1 (Endoplasmic Reticulum Membrane Protein 1) is a member of the family of endoplasmic reticulum (ER) associated proteins that have garnered attention due to their potential roles in various cellular processes, including stress responses, protein folding, and immune modulation. Research indicates that ERMP1 is involved in the regulation of protein quality control mechanisms in the ER, which is crucial for maintaining cellular homeostasis. Dysregulation of ER-associated proteins has been linked to various diseases, including neurodegenerative disorders and cancers, making the study of ERMP1 particularly relevant in understanding these pathologies. Furthermore, ERMP1 has been implicated in the modulation of inflammatory responses, suggesting its involvement in immune regulation. The recombinant expression of ERMP1 allows for detailed investigation of its biochemical properties, functional roles, and potential therapeutic applications. By producing and characterizing this protein in a controlled environment, researchers can elucidate its mechanism of action, interactions with other cellular components, and potential as a target for drug development. Given the increasing importance of ER stress and protein misfolding in disease contexts, the study of ERMP1 presents an opportunity to explore novel pathways and strategies for intervention, making it a promising candidate for future biomedical research.
