Analytical Data
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基因名
aMACR
- Application
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别名
aMACR；Alpha-methylacyl-CoA racemase
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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
Q9UHK6
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表达区间
2-382aa
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氨基酸序列
ALQGISVVE LSGLAPGPFC AMVLADFGAR VVRVDRPGSR YDVSRLGRGK RSLVLDLKQP RGAAVLRRLC KRSDVLLEPF RRGVMEKLQL GPEILQRENP RLIYARLSGF GQSGSFCRLA GHDINYLALS GVLSKIGRSG ENPYAPLNLL ADFAGGGLMC ALGIIMALFD RTRTGKGQVI DANMVEGTAY LSSFLWKTQK LSLWEAPRGQ NMLDGGAPFY TTYRTADGEF MAVGAIEPQF YELLIKGLGL KSDELPNQMS MDDWPEMKKK FADVFAEKTK AEWCQIFDGT DACVTPVLTF EEVVHHDHNK ERGSFITSEE QDVSPRPAPL LLNTPAIPSF KRDPFIGEHT EEILEEFGFS REEIYQLNSD KIIESNKVKA SL
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分子量
42.3 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
The study of aMACR (alpha-methylacyl-CoA racemase) recombinant proteins has gained significant attention in recent years due to their crucial role in fatty acid metabolism and the potential implications for various health conditions. aMACR is an enzyme involved in the metabolism of branched-chain fatty acids, facilitating the conversion of different isomers, which is essential for proper cellular function and energy production. Abnormalities in aMACR activity have been linked to various metabolic disorders, including certain types of cancer and neurodegenerative diseases. Furthermore, understanding the structure and function of aMACR at the molecular level can provide insights into the development of targeted therapies and novel biomarker identification. Recombinant protein technology allows for the production and purification of aMACR in a controlled environment, enabling precise studies of its enzymatic properties and interactions with other cellular components. This research aims to elucidate the biochemical pathways involving aMACR and explore its potential as a therapeutic target, ultimately contributing to advancements in metabolic disease management and personalized medicine. With ongoing investigations into its regulatory mechanisms and metabolic pathways, aMACR stands as a promising candidate for further research in the fields of biochemistry and pharmacology.
