C2b

Background

Creative Biolabs provides a wide range of validated C2b antibodies and assists researchers in experiments and research. Our dedication to quality ensures reliable results, improving researchers with accuracy and efficiency.

Introduction

The complement system consists of active enzymes found in the serum and tissue fluids of both humans and animals when it is activated. It is an essential component of intrinsic immunity and a complement to antibody-triggered responses. Antigen-antibody complexes or microorganisms can activate the complement pathway, leading to the eventual lysis or phagocytosis of pathogenic organisms.

C2 (complement component 2) is an intrinsic component of the classical complement activation pathway; it is a serine protease. The complement system is created to regulate self-protection against infection. The entire complement system consists of multiple protein groups that work together to eliminate foreign invaders and ultimately remove debris from cells and tissues. When the body detects a foreign invader, C2 proteins are stimulated to attach to the C4 (complement component 4), resulting in an immune response. C2 proteins are vital in regulating the body's immune responses.

In the classical complement activation pathway, C2 is cleaved by the C1s serine protease to generate two fragments, C2b and C2a. C2b contains an enzyme catalytic site that can bind to the C4b/C3b fragment and then form C3 convertase and C5 convertase. In the presence of Mg²⁺, C2 combines with C4b to form the C4bC2 complex. This complex can be cleaved to C2a and C2b by C1s or MASP2. The C2b fragment is small and is derived from the N-terminus of the C2 protein, which contains three CCP structural domains that can interact with C4b. The C-terminal region of the C2b fragment might play a role in vascular permeability in humans, as suggested.

Structure of C2b

Fig.1 Structure of complement C2 protein.Distributed under CC BY-SA 3.0, from Wiki, without modification.

The molecule consists of 233 amino acids and is folded into three domains that have a similar secondary structure-they are all elongated and contain five segments surrounding a hydrophobic core. The CCP1 domain in C2b contains a potential N-linked glycosylation site at Asn9, and the CCP2 domain contains another potential site at Asn92. A large amount of electron density is observed at these positions, indicating that these residues may be glycosylated in recombinant C2b.

Creative Biolabs provides diverse antibodies, assay kits, and proteins for you in C2b research, satisfying your various demands. We are dedicated to helping you improve your experiments and accelerate the R&D process in the field of complement.

C2b Functional Service

Creative Biolabs provides a diverse selection of C2b-targeted products, including C2b-specific antibodies and recombinant C2b proteins. These carefully crafted reagents are essential for uncovering the interactions between C2b proteins and different molecular entities, thus propelling research aimed at devising therapeutic approaches for numerous diseases.

Fig.2 Assembly of C4b2 and C4b2a complexes on the SPR sensorchip surface.¹

Researchers evaluated the effects of mutations and metal ion chelation by the MIDAS on the stability of C4b2 and C4b2a utilizing surface plasmon resonance (SPR) measurements. C4b was captured on a streptavidin SPR sensor chip using a site-specific biotin moiety, emulating C4b’s attachment to an activating surface. Following this, biotinylated C4b facilitated the formation of C4b2 upon C2 injection. Subsequent introduction of C1s led to a rapid dissociation of C2b and a slower dissociation of C2a. The termination of C2 and C1s injections were designated as “stop C2” and “stop C1s” respectively.

Creative Biolabs provides a comprehensive range of services centered on C2b functionality, including assays for C2b binding and other specific functional evaluations. These services are meticulously crafted to assist our valued clients in their clinical and research projects.

Reference

1. Mortensen, Sofia, Jan K. Jensen, and Gregers R. Andersen. "Solution structures of complement C2 and its C4 complexes propose pathway-specific mechanisms for control and activation of the complement proconvertases." Journal of Biological Chemistry 291.32 (2016): 16494-16507. Distributed under Open Access license CC BY 4.0, without modification.