Analytical Data
-
Gene name
arsR
- Application
-
Alternative Names
arsR；Transcriptional regulatory Protein ArsR
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P37309
-
Expression Region
1-117aa
-
AA Sequence
MSFLLPIQLFKILADETRLGIVLLLSELGELCVCDLCTALDQSQPKISRHLALLRESGLLLDRKQGKWVHYRLSPHIPAWAAKIIDEAWRCEQEKVQAIVRNLARQNCSGDSKNICS
-
Molecular Weight
19.0 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
ArsR is a regulatory protein that plays a crucial role in the response to arsenic and antimony stress in various microorganisms. As a member of the ArsR/SmtB family of transcriptional regulators, ArsR binds to metal ions, particularly arsenic, leading to conformational changes that modulate gene expression related to metal detoxification and homeostasis. The study of recombinant ArsR proteins has gained significance due to their potential applications in bioremediation and environmental biotechnology. Understanding the mechanisms by which ArsR senses and responds to toxic metals aids in elucidating microbial adaptation strategies in contaminated environments. Moreover, the structural characterization of recombinant ArsR provides insights into metal binding sites and the regulatory pathways involved in arsenic resistance. This research can also contribute to the development of biosensors for detecting arsenic levels in environmental samples. Overall, the investigation of ArsR not only deepens our comprehension of microbial metal metabolism but also holds promise for addressing global challenges related to arsenic contamination and public health.
