Analytical Data
-
Gene name
entC1
- Application
-
Alternative Names
entC1；HLA-DRA1；HLA class II histocompatibility antigen. DR alpha chain
-
Species
Staphylococcus aureus
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P01553
-
Expression Region
28-266aa
-
AA Sequence
ESQPDPTPDELHKASKFTGLMENMKVLYDDHYVSATKVKSVDKFLAHDLIYNISDKKLKNYDKVKTELLNEGLAKKYKDEVVDVYGSNYYVNCYFSSKDNVGKVTGGKTCMYGGITKHEGNHFDNGNLQNVLIRVYENKRNTISFEVQTDKKSVTAQELDIKARNFLINKKNLYEFNSSPYETGYIKFIENNGNTFWYDMMPAPGDKFDQSKYLMMYNDNKTVDSKSVKIEVHLTTKNG
-
Molecular Weight
43.5 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
EntC1 is a recombinant protein derived from the biosynthetic pathway of enterobactin, a siderophore produced by many Gram-negative bacteria for iron sequestration. The study of EntC1 has gained significant attention due to its critical role in bacterial iron transport and its implications for understanding microbial physiology and pathogenicity. Enterobactin and its derivatives are essential for bacterial survival in iron-limited environments, such as those encountered in host organisms. Research into EntC1 focuses on its enzymatic functions in the assembly of the enterobactin molecule, specifically its involvement in the condensation of 2,3-dihydroxybenzoate and its interactions with other enzymes in the biosynthetic pathway. Understanding the structure and function of EntC1 not only aids in unraveling the molecular mechanisms behind iron acquisition in bacteria but also opens avenues for the development of novel antimicrobial strategies, as targeting this pathway could hinder bacterial growth. Furthermore, insights into the recombinant production of EntC1 contribute to advancements in biotechnology and synthetic biology, where understanding and manipulating such biosynthetic pathways can lead to innovative applications in drug development and environmental bioremediation. As antibiotic resistance remains a pressing global health issue, exploring the unique features of EntC1 and its role in bacteria may provide critical information for designing new therapeutic approaches. Overall, the research on EntC1 represents a convergence of microbiology, biochemistry, and pharmacology, highlighting its potential importance in both fundamental and applied sciences.
