Analytical Data
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基因名
ERLIN2
- Application
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别名
Erlin-2; SPFH2; NET32; C8orf2; ER Lipid Raft Associated Protein 2; Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 2
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种属
Human
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表达系统
E. coli
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标签
N-His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
O94905
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表达区间
Pro47~Asn339
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分子量
37kDa
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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
ERLIN2, a member of the ERLIN family, is a protein initially identified for its role in the endoplasmic reticulum (ER) and its involvement in various cellular processes, including protein quality control and the regulation of ER-associated degradation (ERAD). Research on ERLIN2 has gained traction due to its potential implications in several physiological and pathological conditions, particularly its association with neurodegenerative diseases and cancer. Studies have indicated that ERLIN2 interacts with specific proteins within the ER, influencing their stability and function, which is critical for maintaining cellular homeostasis. Furthermore, emerging evidence suggests that ERLIN2 may play a significant role in modulating autophagy and the stress response of cells, making it a crucial player in various stress-related signaling pathways. Despite these insights, the precise molecular mechanisms governing ERLIN2's functions and its role in different cellular contexts remain poorly understood. Continued investigation into ERLIN2's interactions and regulatory functions is essential for elucidating its contribution to health and disease, offering potential avenues for therapeutic interventions targeting ERLIN2-related pathways.
