关键信息
-
基因名
FuR
- 应用
-
别名
FuR；FUR；PACE;Furin
-
种属
Human
-
表达系统
E. coli
-
标签
His tag N-Terminus
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
P09958
-
表达区间
131-715aa
-
氨基酸序列
DLNVKAAWAQ GYTGHGIVVS ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP DPQPRYTQMN DNRHGTRCAG EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL GLNPNHIHIY SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ IVTTDLRQKC TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT SKPAHLNAND WATNGVGRKV SHSYGYGLLD AGAMVALAQN WTTVAPQRKC IIDILTEPKD IGKRLEVRKT VTACLGEPNH ITRLEHAQAR LTLSYNRRGD LAIHLVSPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD EDPSGEWVLE IENTSEANNY GTLTKFTLVL YGTAPEGLPV PPESSGCKTL TSSQACVVCE EGFSLHQKSC VQHCPPGFAP QVLDTHYSTE NDVETIRASV CAPCHACSAT CQGPALTDCL SCPSHASLDP VEQTCSRQSQ SSRESPPQQQ PPRLPPEVEA GQRLRAGLLP SHLPEHHHHH HHH
-
分子量
64 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.
质检流程
相关产品
背景信息
FuR (Ferric Uptake Regulator) is a key protein involved in the regulation of iron metabolism in bacteria, particularly in response to varying iron levels in the environment. Research on FuR has gained significant attention due to its crucial role in bacterial virulence and pathogenesis. As an iron-responsive regulator, FuR modulates the expression of genes involved in iron acquisition, storage, and utilization, allowing bacteria to adapt to iron-limited conditions often encountered in host organisms. Understanding the structure and function of FuR can provide insights into bacterial survival mechanisms and the development of novel antibacterial strategies. The study of FuR as a recombinant protein has enabled scientists to investigate its biochemical properties, identify potential ligands, and explore its interactions with DNA. By characterizing the structure-function relationships of FuR, researchers aim to uncover its regulatory mechanisms, which could lead to novel approaches for targeting iron metabolism in pathogenic bacteria and enhancing our understanding of microbial evolution and ecology. Additionally, the recombinant expression of FuR facilitates large-scale production for functional assays and crystallographic studies, paving the way for the development of innovative therapeutic agents that disrupt iron homeostasis in bacteria.
