Analytical Data
-
Gene name
p37
- Application
-
Alternative Names
p37;UBX domain-containing Protein 2B
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P15363
-
Expression Region
24-403aa
-
AA Sequence
CSNTGVVKQEDVSVSQGQWDKSITFGVSEAWLNKKKGGEKVNKEVINTFLENFKKEFNKLKNANDKTKNFDDVDFKVTPIQDFTVLLNNLSTDNPELDFGINASGKLVEFLKNNPGIITPALETTTNSFVFDKEKDKFYVDGTDSDPLVKIAKEINKIFVETPYASWTDENHKWNGNVYQSVYDPTVQANFYRGMIWIKGNDETLAKIKKAWNDKDWNTFRNFGILHGKDNSFSKFKLEETILKNHFQNKFTTLNEDRSAHPNAYKQKSADTLGTLDDFHIAFSEEGSFAWTHNKSATKPFETKANEKMEALIVTNPIPYDVGVFRKSVNQLEQNLIVQTFINLAKNKQDTYGPLLGYNGYKKIDNFQKEIVEVYEKAIK
-
Molecular Weight
59.5 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
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.
-
Storage & Shelf Life
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.
-
Shipping
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.











