Analytical Data
-
Gene name
DDO
- Application
-
Alternative Names
DDO;D-aspartate oxidase
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q99489
-
Expression Region
1-341aa
-
AA Sequence
MDTARIAVVG AGVVGLSTAV CISKLVPRCS VTIISDKFTP DTTSDVAAGM LIPHTYPDTP IHTQKQWFRE TFNHLFAIAN SAEAGDAGVH LVSGWQIFQS TPTEEVPFWA DVVLGFRKMT EAELKKFPQY VFGQAFTTLK CECPAYLPWL EKRIKGSGGW TLTRRIEDLW ELHPSFDIVV NCSGLGSRQL AGDSKIFPVR GQVLQVQAPW VEHFIRDGSG LTYIYPGTSH VTLGGTRQKG DWNLSPDAEN SREILSRCCA LEPSLHGACN IREKVGLRPY RPGVRLQTEL LARDGQRLPV VHHYGHGSGG ISVHWGTALE AARLVSECVH ALRTPIPKSN L
-
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
DDO (Dipeptidyl Peptidase IV-Associated Protein) is a protein that has garnered attention in recent years due to its role in various biological processes, including immune response and cellular signaling. Found primarily in mammalian tissues, DDO is associated with the regulation of dipeptidyl peptidase IV (DPPIV), an enzyme that plays a critical role in glucose metabolism and the inactivation of several regulatory peptides. Research has indicated that DDO may influence the stability and activity of DPPIV, thereby impacting metabolic pathways and immune functions. Moreover, alterations in DDO expression have been implicated in conditions such as diabetes and cancer, making it a potential biomarker and therapeutic target. Studies exploring the structural and functional aspects of DDO are essential for understanding its mechanisms of action and how it interacts with other proteins. The ongoing investigation of DDO not only elucidates its biological significance but also holds promise for developing novel strategies in disease management and treatment, highlighting the importance of comprehensive research into this intriguing protein.











