Analytical Data
-
Gene name
MC
- Application
-
Alternative Names
RNase MC
-
Species
Momordica charantia
-
Source
E. coli
-
Tag
N- His & C- Myc
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P23540
-
Expression Region
1-191aa
-
Molecular Weight
28.7 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
In recent years, the study of recombinant proteins, particularly those derived from the MC (Mycobacterium tuberculosis) family, has garnered significant attention due to their potential applications in biotechnology and medicine. MC recombinant proteins are essential for understanding the pathogenic mechanisms of Mycobacterium tuberculosis and other related species. They play crucial roles in immune responses and serve as potential targets for vaccine development and immunodiagnostic tests. The ability to produce these proteins in heterologous systems allows researchers to study their structure and function in detail, facilitating insights into mycobacterial biology and host-pathogen interactions. Moreover, the use of recombinant DNA technology has enabled scientists to engineer these proteins for enhanced stability, efficacy, and immunogenicity, making them valuable tools for both basic research and the development of new therapeutic strategies. As the incidence of tuberculosis and antibiotic-resistant strains of mycobacteria continues to rise globally, the importance of understanding and manipulating MC recombinant proteins becomes increasingly critical in the quest for innovative solutions to combat these public health challenges.
