Analytical Data
-
Gene name
ykuP
- Application
-
Alternative Names
ykuP; BSU14170; Probable flavodoxin 2
-
Species
Bacillus subtilis
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O34589
-
Expression Region
1-151aa
-
Molecular Weight
32.6 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
ykuP is a protein found in various bacteria, particularly within the Bacillus subtilis species, and is believed to play a significant role in cellular processes such as stress response and protein synthesis. The interest in ykuP has grown due to its potential implications in understanding bacterial survival mechanisms, especially under unfavorable environmental conditions. Research has shown that ykuP may be involved in the regulation of gene expression and the maintenance of cellular homeostasis. Studies on its structure and function suggest that ykuP might interact with other cellular components, influencing metabolic pathways and contributing to the organism's adaptability. In addition, the investigation of ykuP as a recombinant protein has gained traction in the field of biotechnology, as it holds promise for applications in developing novel antibacterial agents and enhancing the efficacy of existing treatments. By exploring the intricate pathways and interactions involving ykuP, researchers aim to uncover new insights into bacterial physiology and potentially inform strategies for combating antibiotic resistance. Thus, the study of ykuP not only enriches our understanding of microbial biology but also opens avenues for innovative therapeutic advancements.
