Analytical Data
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基因名
ERMP1
- Application
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别名
ERMP1; FXNA; KIAA1815Endoplasmic reticulum metallopeptidase 1; EC 3.4.-.-; Felix-ina
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种属
Human
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表达系统
E. coli
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标签
GST-tag at N-terminal
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q7Z2K6
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表达区间
1-317aa
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氨基酸序列
MFIPYLYALYLIWAVFEMFTPILGRSGSEIPPDVVLASILAGCTMILSSYFINFIYLAKSTKKTMLTLTLVCAITFLLVCSGTFFPYSSNPANPKPKRVFLQHMTRTFHDLEGNAVKRDSGIWINGFDYTGISHITPHIPEINDSIRAHCEENAPLCGFPWYLPVHFLIRKNWYLPAPEVSPRNPPHFRLISKEQTPWDSIKLTFEATGPSHMSFYVRAHKGSTLSQWSLGNGTPVTSKGGDYFVFYSHGLQASAWQFWIEVQVSEEHPEGMVTVAIAAHYLSGEDKRSPQLDALKEKFPDWTFPSAWVCTYDLFVF
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分子量
62.4 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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.
