Analytical Data
-
基因名
omp1B
- Application
-
别名
Major outer membrane porin, serovar B; MOMP; ompA; omp1B; Chlamydia trachomatis
-
种属
Others
-
表达系统
E. coli
-
标签
C-Myc;N-10*His
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
P23421
-
表达区间
L23-F394
-
蛋白长度
Full Length of Mature Protein
-
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
OMP1B (Outer Membrane Protein 1B) is a significant protein found in the outer membrane of certain gram-negative bacteria, including pathogenic strains that are of considerable interest in medical microbiology. The research on OMP1B has gained traction due to its potential role in bacterial virulence, adherence, and immune evasion. Understanding the structure and function of OMP1B is crucial for unraveling the mechanisms by which these bacteria interact with their hosts and establish infections. Furthermore, OMP1B presents opportunities for vaccine development and therapeutic interventions, as it may serve as a target for neutralizing antibodies or an antigen for vaccine formulation. Studies have highlighted its ability to elicit immune responses, suggesting its importance in the development of strategies to combat bacterial infections. Recent advances in recombinant protein technology have facilitated the production and characterization of OMP1B, allowing researchers to explore its properties and interactions in detail. This research not only contributes to our fundamental understanding of bacterial pathogens but also has practical implications for public health, particularly in devising novel approaches to tackle antibiotic resistance and improve infection control measures. Overall, ongoing investigations into OMP1B hold promise for advancing both basic and applied sciences in the field of infectious diseases.












