Analytical Data
-
Gene name
CD59
- Application
-
Alternative Names
Protectin; MIC11; MIN1; MIN2; MIN3; MSK21; MAC-IP; MACIF; MIRL; HRF20; Complement Regulatory Protein; 20 kDa homologous restriction factor; Membrane attack complex inhibition factor
-
Species
Rabbit
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O77541
-
Expression Region
Ser25~Leu104
-
Molecular Weight
20kDa
-
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
CD59, a glycosylphosphatidylinositol (GPI)-anchored membrane protein, plays a crucial role in the regulation of the complement system, which is a vital part of the immune response. It inhibits the formation of the membrane attack complex (MAC), thereby protecting host cells from lysis by complement proteins. Abnormal expression or dysfunction of CD59 has been linked to various pathologies, including autoimmune diseases, cancer, and infectious diseases. Consequently, researchers have focused on the potential therapeutic applications of CD59, exploring its role not only in complement regulation but also in modulating immune responses. Recombinant CD59 proteins are being developed to better understand its functions and mechanisms, to design novel therapies that can enhance immune protection in patients with compromised immune systems, or to inhibit complement activation in conditions characterized by excessive complement activity. Additionally, CD59 is being investigated as a possible target for drug delivery systems and vaccine development. The study of CD59 recombinant proteins also provides insights into the structure-function relationships of membrane proteins, advancing our understanding of cell biology and immunology. Overall, the research on CD59 recombinant proteins holds promise for innovative therapeutic solutions while contributing to the broader field of immunology and molecular biology.
