Analytical Data
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基因名
POR
- Application
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别名
VDAC3;Voltage-dependent anion-selective channel Protein 3
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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
P16435
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表达区间
2-671aa
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氨基酸序列
INMGDSHVDTSSTVSEAVAEEVSLFSMTDMILFSLIVGLLTYWFLFRKKKEEVPEFTKIQTLTSSVRESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAHRYGMRGMSADPEEYDLADLSSLPEIDNALVVFCMATYGEGDPTDNAQDFYDWLQETDVDLSGVKFAVFGLGNKTYEHFNAMGKYVDKRLEQLGAQRIFELGLGDDDGNLEEDFITWREQFWLAVCEHFGVEATGEESSIRQYELVVHTDIDAAKVYMGEMGRLKSYENQKPPFDAKNPFLAAVTTNRKLNQGTERHLMHLELDISDSKIRYESGDHVAVYPANDSALVNQLGKILGADLDVVMSLNNLDEESNKKHPFPCPTSYRTALTYYLDITNPPRTNVLYELAQYASEPSEQELLRKMASSSGEGKELYLSWVVEARRHILAILQDCPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVHICAVVVEYETKAGRINKGVATNWLRAKEPVGENGGRALVPMFVRKSQFRLPFKATTPVIMVGPGTGVAPFIGFIQERAWLRQQGKEVGETLLYYGCRRSDEDYLYREELAQFHRDGALTQLNVAFSREQSHKVYVQHLLKQDREHLWKLIEGGAHIYVCGDARNMARDVQNTFYDIVAELGAMEHAQAVDYIKKLMTK
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分子量
102.9kDa
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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
POR (P450 oxidoreductase) is a critical enzyme that plays an essential role in the electron transfer process required for the activity of various cytochrome P450 enzymes, which are involved in the metabolism of drugs, steroids, and xenobiotics. Given the importance of these metabolic pathways in pharmacology and toxicology, research on POR has garnered significant interest. Mutations in the POR gene can lead to disorders affecting drug metabolism and steroidogenesis, resulting in clinical manifestations such as adrenal insufficiency or altered drug responses. Understanding the structural and functional aspects of POR is crucial for elucidating its role in metabolic diseases and for developing better therapeutic strategies. Recent studies have focused on the expression and purification of recombinant POR to investigate its interaction with P450 enzymes and explore its enzymatic properties. Advances in this area could provide insights into the mechanisms of drug metabolism and the potential for personalized medicine approaches that account for individual variations in metabolic responses. Moreover, the use of recombinant POR in biotechnological applications, such as the bioconversion of organic compounds or in the production of pharmaceuticals, is also an emerging field of interest. Overall, the study of POR and its recombinant forms has far-reaching implications for both basic and applied sciences, making it a significant area of ongoing research.
