Rat Plasma.
Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.
Sterile filtered solution.
Greater than 95.0% as determined by SDS-PAGE.
Rat Complement C3b produced in Rat plasma having a molecular weight of 175kDa.
C3b, a key component of the complement system, is generated when native C3 is cleaved by the alternative pathway C3 convertase. This process releases C3a and leaves C3b, which is vital for all three complement pathways. These pathways use C3 convertases to cleave C3, producing C3a and activating C3b. Surface-bound C3b is crucial for activating C5, leading to the formation of C5b-9 complexes that lyse target cells. Additionally, C3b, along with its breakdown products iC3b and C3d, are recognized by receptors on immune cells, facilitating antigen presentation and stimulating the immune response.
Rat Complement C3b is a protein with a molecular weight of 175kDa, produced from Rat plasma.
The product is a sterile, filtered solution.
The C3b solution is formulated in phosphate buffered saline at a pH of 7.2.
Rat C3b remains stable for 2-4 weeks when stored at 4°C. For prolonged storage, freezing below -20°C is recommended. Adding a carrier protein (0.1% HSA or BSA) can further enhance stability during long-term storage. To maintain product integrity, avoid repeated freeze-thaw cycles.
The purity of Rat C3b is greater than 95%, as determined by SDS-PAGE analysis.
Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.
Rat Plasma.
Complement C3 is a large protein that, upon activation, is cleaved into two fragments: C3a and C3b. The cleavage occurs through the action of C3 convertases, which are enzyme complexes formed during the activation of the complement pathways . The C3b fragment contains a reactive thioester bond that allows it to covalently attach to the surface of pathogens or other target cells. This process is known as opsonization, which tags the target for destruction by immune cells .
C3b plays a multifaceted role in the immune system:
The activity of C3b is tightly regulated to prevent damage to host tissues. Regulatory proteins such as Factor H and Factor I inactivate C3b by cleaving it into inactive fragments (iC3b, C3c, and C3d) . These fragments can still bind to complement receptors and play roles in immune regulation, but they do not form C5 convertase or participate in the formation of the MAC .
Research on complement C3b has significant clinical implications. Dysregulation of the complement system, including excessive activation or insufficient regulation of C3b, is associated with various diseases such as autoimmune disorders, infections, and inflammatory conditions . Understanding the mechanisms of C3b activation and regulation can lead to the development of therapeutic interventions targeting the complement system.