关键信息
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基因名
pyrG
- 应用
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别名
pyrG；CTPS；CTP synthase 1
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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
P65925
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表达区间
1-267aa
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氨基酸序列
MTKYIFVTGGVVSSIGKGIVAASLGRLLKNRGLKVTIQKFDPYINIDPGTMSPYQHGEVYVTDDGAETDLDLGHYERFIDINLNKYSNVTTGKIYSEVLRKERKGEYLGATVQVIPHITDALKEKIKRAASTTDSDVIITEVGGTVGDIESLPFLEALRQMKADVGSENVMYIHTTLLPYLKAAGEMKTKPTQHSVKELRGLGIQPNMLVIRTEEPVEQGIKNKLAQFCDVNSEAVIESRDVEHLYQIPLNLQAQSMDQIVCDHLKL
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分子量
49.6 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 pyrG gene, found in various organisms, encodes a key enzyme involved in the purine biosynthetic pathway, specifically regulating guanine nucleotide synthesis. Research on pyrG recombinant proteins has gained significant attention due to their potential applications in biotechnology and medicine. By using recombinant DNA technology, scientists can produce large quantities of pyrG proteins, which can then be utilized to better understand the enzyme's structure, function, and regulatory mechanisms. Additionally, the study of pyrG has implications for genetic engineering and metabolic engineering, enabling the development of strains with improved growth characteristics or enhanced production of valuable metabolites. Furthermore, the exploration of pyrG in pathogenic organisms can aid in the identification of novel drug targets, contributing to the fight against infectious diseases. Investigating pyrG proteins helps to unravel the complexities of nucleotide metabolism, offering insights that could lead to innovative strategies for disease treatment and the optimization of industrial bioprocesses. Consequently, the ongoing research on recombinantly expressed pyrG proteins is pivotal for advancing our understanding of fundamental biological processes and developing practical applications in various fields, including pharmaceuticals, agriculture, and energy production.
