Analytical Data
-
Gene name
KMO
- Application
-
Alternative Names
KMO；Kynurenine 3-monooxygenase
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O15229
-
Expression Region
1-407aa
-
AA Sequence
MDSSVIQRKKVAVIGGGLVGSLQACFLAKRNFQIDVYEAREDTRVATFTR GRSINLALSHRGRQALKAVGLEDQIVSQGIPMRARMIHSLSGKKSAIPYG TKSQYILSVSRENLNKDLLTAAEKYPNVKMHFNHRLLKCNPEEGMITVLG SDKVPKDVTCDLIVGCDGAYSTVRSHLMKKPRFDYSQQYIPHGYMELTIP PKNGDYAMEPNYLHIWPRNTFMMIALPNMNKSFTCTLFMPFEEFEKLLTS NDVVDFFQKYFPDAIPLIGEKLLVQDFFLLPAQPMISVKCSSFHFKSHCV LLGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKFSNDLSLCLPVFSRLRI PDDHAISDLSMYNYIEKNMERFLHAIMPSTFIPLYTMVTFSRIRYHEAVQ RWHWQKR
-
Molecular Weight
71 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
KMO (kynurenine 3-monooxygenase) is an important enzyme in the kynurenine pathway, which is responsible for the metabolism of the amino acid tryptophan into several bioactive metabolites. The activity of KMO has significant implications in various physiological and pathological processes, including immune responses, neurodegenerative diseases, and mood disorders. Research has shown that the regulation of KMO can influence the balance between neuroprotective and neurotoxic metabolites, such as kynurenic acid and quinolinic acid, which are derived from the kynurenine pathway. Abnormal KMO activity has been implicated in conditions such as schizophrenia, depression, and Huntington’s disease, prompting interest in the enzyme as a potential therapeutic target. Furthermore, the study of KMO's structure and function will help to elucidate its role in these diseases, providing insights into novel treatment strategies. Recent advances in molecular biology and structural genomics have enabled researchers to explore the enzyme's mechanism of action, leading to the development of KMO inhibitors that may alleviate the adverse effects of its dysregulation. Overall, KMO research is a rapidly evolving field that bridges biochemistry, neuroscience, and pharmacology, aiming to better understand and manipulate the kynurenine pathway for therapeutic benefit.
