Analytical Data
-
Gene name
ADMA
- Application
-
Alternative Names
ADMA；DDAH；N(G).N(G)-dimethylarginine dimethylaminohydrolase 1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O94760
-
Expression Region
1-285aa
-
AA Sequence
MAGLGHPAAFGRATHAVVRALPESLGQHALRSAKGEEVDVARAERQHQLYVGVLGSKLGLQVVELPADESLPDCVFVEDVAVVCEETALITRPGAPSRRKEVDMMKEALEKLQLNIVEMKDENATLDGGDVLFTGREFFVGLSKRTNQRGAEILADTFKDYAVSTVPVADGLHLKSFCSMAGPNLIAIGSSESAQKALKIMQQMSDHRYDKLTVPDDIAANCIYLNIPNKGHVLLHRTPEEYPESAKVYEKLKDHMLIPVSMSELEKVDGLLTCCSVLINKKVDS
-
Molecular Weight
31.1 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
ADMA (asymmetric dimethylarginine) is an endogenous inhibitor of nitric oxide synthase, which plays a crucial role in cardiovascular physiology by regulating nitric oxide (NO) production. Elevated levels of ADMA have been associated with various cardiovascular diseases, including hypertension, atherosclerosis, and heart failure, highlighting its potential as a biomarker and therapeutic target. The study of recombinant ADMA proteins has gained traction as researchers seek to understand the mechanisms underlying its metabolic pathways and interactions with nitric oxide signaling. Recombinant protein technologies enable the production of ADMA in controlled environments, facilitating detailed analyses of its structure, function, and regulatory roles. By employing techniques such as site-directed mutagenesis, researchers can create specific variants of ADMA, allowing for the exploration of its biological implications and interactions at a molecular level. Additionally, recombinant ADMA proteins can serve as valuable tools in drug development, helping to identify potential inhibitors or modulators of the ADMA pathway. Ultimately, this line of research aims to deepen our understanding of ADMA's involvement in vascular health and disease, with the potential to pave the way for novel therapeutic strategies targeting the modulation of ADMA levels and its associated pathways in clinical settings.
