关键信息
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基因名
purD
- 应用
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别名
purD；PGFT；PRGS；Trifunctional purine biosynthetic Protein adenosine-3
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种属
E.coli
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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
Q8X612
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表达区间
1-429aa
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氨基酸序列
MKVLVIGNGGREHALAWKAAQSPLVETVFVAPGNAGTALEPTLQNVAIGVTDIPALLDFAQNEKVDLTIVGPEAPLVKGVVDTFRAAGMKIFGPTAGAAQLEGSKAFTKDFLARHNIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTLEEAEAAVHDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGDKDTGPNTGGMGAYSPAPVVTDDVHQRTMERIIWPTVKGMASEGNTYTGFLYAGLMIDKQGNPKVIEFNCRFGDPETQPIMLRMKSDLVELCLAACEGKLDEKTSEWDERASLGVVMAAGGYPGDYRTGDVIHGLPLEEVEDGKVFHAGTKLADDEQVVTSGGRVLCVTALGHTVAEAQKRAYALMTDIHWDDCFCRKDIGWRAIEREQN
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分子量
62.0 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.
质检流程
相关产品
背景信息
The purD gene encodes an enzyme involved in the de novo synthesis of purines, specifically catalyzing the conversion of phosphoribosylamine to 5-amino-1-(5-phospho-D-ribosyl)imidazole. Research on purD recombinant protein has gained significant attention due to its essential role in the purine biosynthetic pathway, which is crucial for nucleotide production and cellular function in various organisms. Understanding the structure and function of purD can provide insights into the regulation of purine metabolism and its implications in microbial growth and pathogenicity. Moreover, purD and its associated pathways present potential targets for the development of antimicrobial agents, as inhibiting purine synthesis can effectively stifle the growth of pathogenic bacteria and protozoa. Studies have focused not only on characterizing the enzyme's kinetic properties and substrate specificity but also on developing expression systems for large-scale production of the recombinant protein. Molecular techniques, including site-directed mutagenesis, have been employed to dissect the enzyme's functional domains, contributing to a deeper understanding of the mechanisms governing purine metabolism. Furthermore, by utilizing purD as a model, researchers aim to elucidate broader metabolic networks and their regulatory mechanisms, fostering advances in biochemistry, pharmacology, and synthetic biology. Overall, recombinant purD protein research holds promise for both theoretical insights and practical applications in health and disease.
