Analytical Data
-
基因名
lecA
- Application
-
别名
lecA;KIAA0973;SAST;Microtubule-associated serine/threonine-Protein kinase 1
-
种属
E.coli
-
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
Q05097
-
表达区间
2-122aa
-
氨基酸序列
AWKGEVLANNEAGQVTSIIYNPGDVITIVAAGWASYGPTQKWGPQGDREHPDQGLICHDAFCGALVMKIGNSGTIPVNTGLFRWVAPNNVQGAITLIYNDVPGTYGNNSGSFSVNIGKDQS
-
分子量
16.8 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
LecA is a lectin protein derived from the pathogenic bacterium Pseudomonas aeruginosa, which plays a significant role in the organism's ability to adhere to and invade host tissues. This protein specifically binds to galactosides, a property that facilitates bacterial colonization and enhances virulence in infections, particularly in immunocompromised individuals. Research into LecA has gained prominence due to its potential as a target for therapeutic interventions, particularly in developing novel anti-adhesive strategies to combat bacterial infections. Understanding the molecular mechanisms of LecA's interactions with host cells is crucial for designing new antimicrobial agents or preventive measures against P. aeruginosa infections, which are notoriously difficult to treat due to antibiotic resistance. Additionally, LecA's unique properties make it a candidate for use in drug delivery systems and as a biomarker in diagnostic tools. Recent studies have focused on characterizing LecA's structural features, binding affinities, and the signaling pathways activated upon its interaction with host cells. As the global threat of antibiotic-resistant pathogens continues to escalate, LecA and its recombinant forms represent a promising area of research, offering insights into potential interventions that could mitigate the impact of infections caused by this versatile and opportunistic pathogen.












