Analytical Data
-
Gene name
NIT2
- Application
-
Alternative Names
NIT2;Omega-amidase NIT2
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9NQR4
-
Expression Region
1-276aa
-
AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMTSFRLALIQLQISSIKSDNVTRACSF IREAATQGAKIVSLPECFNSPYGAKYFPEYAEKIPGESTQKLSEVAKECS IYLIGGSIPEEDAGKLYNTCAVFGPDGTLLAKYRKIHLFDIDVPGKITFQ ESKTLSPGDSFSTFDTPYCRVGLGICYDMRFAELAQIYAQRGCQLLVYPG AFNLTTGPAHWELLQRSRAVDNQVYVATASPARDDKASYVAWGHSTVVNP WGEVLAKAGTEEAIVYSDIDLKKLAEIRQQIPVFRQKRSDLYAVEMKKP
-
Molecular Weight
33 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
NIT2, a member of the transition metal-dependent nitroreductase family, has garnered significant interest in recent years due to its potential applications in bioremediation and biotechnology. This enzyme is known for its ability to catalyze the reduction of nitro compounds, which are prevalent environmental pollutants arising from industrial activities and agricultural runoff. In bacterial systems, NIT2 plays a critical role in the metabolism of these compounds, necessitating a deeper understanding of its biochemical properties and mechanisms of action. Research into NIT2 has aimed to elucidate its structure-function relationship, thereby providing insights into its catalytic activity and substrate specificity. Advances in techniques such as recombinant DNA technology have facilitated the production of NIT2 as a recombinant protein, allowing for more detailed studies using various biophysical and biochemical methods. Moreover, as environmental concerns regarding nitro compound pollution continue to rise, NIT2's potential applications offer promising avenues for developing bioremediation strategies. By harnessing the unique properties of this enzyme, researchers aspire to create bio-based solutions that can effectively mitigate the adverse effects of nitro pollutants, contributing to a cleaner and more sustainable environment. This area of research highlights the intersection of protein engineering, environmental science, and biotechnology, making NIT2 a focal point in the quest for effective biodegradation technologies. As studies progress, the findings may lead to novel applications that extend beyond environmental remediation, potentially impacting areas such as pharmaceuticals and industrial processes.











