Analytical Data
-
基因名
pyrF
- Application
-
别名
OMP decarboxylase
-
种属
Helicobacter pylori
-
表达系统
E. coli
-
标签
N- His
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
P56155
-
表达区间
1-227aa
-
分子量
29.4 kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
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
-
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.
-
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.
-
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
Related Products
Protein Description
PyrF, or Pyrimidine Auxotrophic-Related Factor, is a key protein involved in the pyrimidine biosynthetic pathway, particularly in microorganisms such as *Neisseria meningitidis*. Research on PyrF has gained momentum due to its crucial role in cellular metabolism and its potential as a target for antimicrobial drugs. PyrF is essential for the viability of organisms that lack certain pathways for pyrimidine synthesis, making it an attractive candidate for understanding pathogen biology and developing selective inhibitors. Studies have revealed that PyrF participates in complex regulatory mechanisms that control nucleotide synthesis, influencing cell growth and proliferation. Moreover, the structural characteristics of PyrF, including its binding affinities and interactions with other molecular components, provide insights into enzymatic function and the potential for engineering novel therapeutic strategies. As antibiotic resistance becomes an increasing concern in medicine, the exploration of PyrF and related proteins opens new avenues in drug discovery, particularly for targeting bacterial pathogens while minimizing effects on human cells. Additionally, characterizing the dynamics of PyrF can shed light on evolutionary adaptations in various microorganisms, offering a comprehensive understanding of fundamental biochemical processes. This ongoing research underlines the importance of PyrF not just in microbial metabolism, but also in the broader context of pharmaceutical development and microbiology.












