Analytical Data
-
Gene name
C4b
- Application
-
Alternative Names
C4b；C3BR；Complement receptor type 1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P0C0L5
-
Expression Region
774-873aa
-
AA Sequence
VRSFFPENWLWRVETVDRFQILTLWLPDSLTTWEIHGLSLSKTKGLCVAT PVQLRVFREFHLHLRLPMSVRRFEQLELRPVLYNYLDKNLTVSVHVSPVE
-
Molecular Weight
37 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
C4b recombinant protein has garnered significant attention in immunology and biochemistry due to its central role in the complement system, a critical component of the innate immune response. The complement system consists of a series of proteins that, when activated, work collaboratively to opsonize pathogens, promote inflammation, and facilitate the clearance of immune complexes. C4b, generated from the cleavage of the C4 protein, functions as an opsonin, enhancing the recognition and uptake of pathogens by phagocytic cells. Research into C4b recombinant protein is driven by its potential applications in therapeutic interventions for various immune-related disorders, including autoimmune diseases and infections. Its ability to modulate immune responses makes it a candidate for developing novel treatments, such as complement inhibitors or immunotherapies. Moreover, understanding the structural and functional dynamics of C4b can provide insights into the regulation of the complement pathway and its implications in diseases. Recent advances in recombinant DNA technology have enabled the production of C4b in significant quantities, facilitating detailed studies on its properties and interactions with other complement components. Consequently, C4b recombinant protein continues to be a subject of extensive research, aiming to elucidate its mechanisms of action and therapeutic potential in clinical settings.
