Analytical Data
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基因名
RSAD1
- Application
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别名
RSAD1; Radical S-adenosyl methionine domain-containing protein 1; mitochondrial; Putative heme chaperone
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9HA92
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表达区间
18-442 aa
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氨基酸序列
AQR RRRVENAGGS PSPEPAGRRA ALYVHWPYCE KRCSYCNFNK YIPRRLEEAA MQKCLVTEAQ TLLRLSGVQR VESVFFGGGT PSLASPHTVA AVLEAVAQAA HLPADLEVTL EANPTSAPGS RLAEFGAAGV NRLSIGLQSL DDTELRLLGR THSACDALRT LAEARRLFPG RVSVDLMLGL PAQQVGPWLG QLQELLHHCD DHLSLYQLSL ERGTALFAQV QRGALPAPDP ELAAEMYQRG RAVLREAGFH QYEVSNFARN GALSTHNWTY WQCGQYLGVG PGAHGRFMPQ GAGGHTREAR IQTLEPDNWM KEVMLFGHGT RKRVPLGRLE LLEEVLALGL RTDVGITHQH WQQFEPQLTL WDVFGANKEV QELLERGLLQ LDHRGLRCSW EGLAVLDSLL LTLLPQLQEA WQQRTPSPVP GG
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分子量
48.7 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
RSAD1 (Radical S-adenosyl methionine domain-containing protein 1) is a crucial protein involved in the innate immune response, especially in the context of viral infections. It was initially identified as an interferon-stimulated gene, suggesting that its expression is upregulated in response to viral pathogens. Research has shown that RSAD1 plays a significant role in antiviral defense by participating in the formation of protective structures called "vacuoles," which can sequester viral components and inhibit virus replication. Furthermore, RSAD1 has been implicated in various cellular processes, including apoptosis and autophagy, highlighting its multifaceted role in cellular homeostasis and immune regulation. Given its potential as a therapeutic target, studies have been focusing on the functional properties of RSAD1, particularly its ability to interact with cellular machinery to modulate immune responses and its implications in diseases linked to viral infections. Understanding the molecular mechanisms underlying RSAD1 function and its regulatory pathways can provide insights into novel antiviral strategies and enhance our knowledge of immune system dynamics. Therefore, the study of RSAD1 and its recombinant protein form has gained significant attention, as it could lead to new therapeutic interventions against viral diseases and further our understanding of immune modulation.
