Analytical Data
-
Gene name
mocarhagin
- Application
-
Alternative Names
Zinc metalloproteinase mocarhagin
-
Species
Naja mossambica
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q10749
-
Expression Region
192-609aa
-
Molecular Weight
50.7 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
Mocarhagin is a recombinant protein derived from the venom of certain snake species, particularly known for its potential therapeutic applications. Research into mocarhagin has gained momentum due to its unique structure and biological activities, particularly its anticoagulant properties, which make it a promising candidate for the development of novel anticoagulant drugs. Traditional anticoagulant therapies often have limitations, such as risk of bleeding or the need for frequent monitoring, which has spurred interest in alternative agents like mocarhagin. Studies have shown that mocarhagin acts through specific mechanisms that inhibit blood clot formation while maintaining hemostasis, making it a safer option. The recombinant production of mocarhagin in laboratory settings presents advantages in terms of yield, purity, and reproducibility compared to extraction from natural sources. Furthermore, the insights gained from understanding its interaction with coagulation factors could lead to the design of more targeted therapies for a range of thrombotic disorders. Ongoing research is focused on elucidating the detailed mechanisms of mocarhagin's action, assessing its efficacy in preclinical models, and exploring its potential in clinical settings. The promising findings thus far highlight mocarhagin as a significant player in the field of anticoagulant research, with the potential to address limitations of current therapies and improve patient outcomes in thromboembolic diseases.
