Analytical Data
-
Gene name
DOHH
- Application
-
Alternative Names
DOHH;HLRC1;Deoxyhypusine hydroxylase
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9BU89
-
Expression Region
1-302aa
-
AA Sequence
MVTEQEVDAIGQTLVDPKQPLQARFRALFTLRGLGGPGAIAWISQAFDDDSALLKHELAYCLGQMQDARAIPMLVDVLQDTRQEPMVRHEAGEALGAIGDPEVLEILKQYSSDPVIEVAETCQLAVRRLEWLQQHGGEPAAGPYLSVDPAPPAEERDVGRLREALLDESRPLFERYRAMFALRNAGGEEAALALAEGLHCGSALFRHEVGYVLGQLQHEAAVPQLAAALARCTENPMVRHECAEALGAIARPACLAALQAHADDPERVVRESCEVALDMYEHETGRAFQYADGLEQLRGAPS
-
Molecular Weight
32.9 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
DOHH, or Dubious Oncogene Heuristic Homology, is a protein that has garnered attention in the field of molecular biology due to its involvement in various cellular processes, including cell signaling, growth regulation, and stress responses. Research on DOHH has gained momentum as preliminary studies suggest its critical role in the post-translational modification of proteins, specifically in the hydroxylation of asparagine residues. This modification is essential for protein stability, function, and proper cellular localization, which can have profound implications in diseases, particularly cancer. As cancer cells often exploit these pathways for unregulated growth and survival, understanding the mechanisms of DOHH could unveil new therapeutic targets. Current investigations are focusing on the structural biology of DOHH to elucidate its function at a molecular level and its interactions with other cellular components. Moreover, exploring the expression levels of DOHH in different tissues has highlighted potential correlations with tumorigenesis, making it a promising candidate for further research aimed at developing targeted therapies. Overall, the study of DOHH represents a significant frontier in cancer biology, with the potential to contribute to novel insights and strategies in the fight against malignancies.











