Analytical Data
-
基因名
p37
- Application
-
别名
p37;UBX domain-containing Protein 2B
-
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
P15363
-
表达区间
24-403aa
-
氨基酸序列
CSNTGVVKQEDVSVSQGQWDKSITFGVSEAWLNKKKGGEKVNKEVINTFLENFKKEFNKLKNANDKTKNFDDVDFKVTPIQDFTVLLNNLSTDNPELDFGINASGKLVEFLKNNPGIITPALETTTNSFVFDKEKDKFYVDGTDSDPLVKIAKEINKIFVETPYASWTDENHKWNGNVYQSVYDPTVQANFYRGMIWIKGNDETLAKIKKAWNDKDWNTFRNFGILHGKDNSFSKFKLEETILKNHFQNKFTTLNEDRSAHPNAYKQKSADTLGTLDDFHIAFSEEGSFAWTHNKSATKPFETKANEKMEALIVTNPIPYDVGVFRKSVNQLEQNLIVQTFINLAKNKQDTYGPLLGYNGYKKIDNFQKEIVEVYEKAIK
-
分子量
59.5 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
P37 recombinant protein research has garnered significant attention in recent years due to its potential applications in various fields, such as biotechnology, medicine, and vaccine development. The P37 protein, originally identified in specific pathogenic organisms, plays a crucial role in microbial virulence and host-pathogen interactions. Understanding its structure and function can provide insights into disease mechanisms, paving the way for novel therapeutic strategies. Researchers have focused on the expression and purification of P37 in different host systems, including bacteria, yeast, and mammalian cells, to facilitate functional studies and vaccine design. Furthermore, studies have indicated that P37 may evoke strong immune responses, making it a candidate for use in recombinant vaccines. By exploring its antigenic properties and mechanisms of action, scientists aim to leverage P37 for improving vaccine efficacy and developing diagnostic tools for infectious diseases. Overall, the investigation of P37 recombinant protein is crucial for advancing our knowledge of microbial pathology and enhancing public health outcomes.












