
The monoclonal antibody 16D2 recognizes mouse complement factor C4, formerly known as Gg protein, which consists of an alpha-, beta-, and gamma-chain. The classical pathway of complement and the Mannose binding lectin activation pathway converge at C4. C1s, MASP-1 and MASP-2 cleave C4 resulting in the formation of C4a and C4b. Subsequently, C4b can be cleaved to C4c and C4d by other serum enzymes. The monoclonal antibody 16D2 reacts with intact C4, C4b and C4d. C4 is an acute phase protein that is produced by hepatocytes, monocytes and intestinal epithelial cells and can be used- in experimental animals as a marker for activation of the classical complement pathway. Recent studies have demonstrated an association between graft rejection and C4d deposition in a mouse model for cardiac transplantation.
Host
Mouse
Reactivity
Applications
Conjugation

The polyclonal antibody reacts with Rat C4. Rat complement factor C4, formerly known as Gg protein, consists of an alpha-, beta-, and gamma-chain. The classical pathway of complement and the Mannose binding lectin activation pathway converge at C4. C1s, MASP-1 and MASP-2 cleave C4 resulting in the formation of C4a and C4b. The latter can be cleaved to result in C4c and C4d, in which step all functional sites are lost.
Host
Rat
Reactivity
Applications
Conjugation

Antibody clone 99-72-18 recognizes human complement fragment C4c and C4. C4c reflects the degree of complement activation via the classical and lectin pathway. The complement system plays important roles in both innate and adaptive immune response and can produce an inflammatory and protective reaction to challenges from pathogens before an adaptive response can occur. It consists of a complex family of proteins and receptors which are found in the circulation, in tissues and other body-fluids. There are three pathways of complement activation. The classical pathway is initiated by Immune complexes; the lectin pathway by surface bound lectins; and the AP by all the surfaces that are not specifically protected against it. The C3 and C5 convertases are enzymatic complexes that initiate and amplify the activity of the complement pathways and ultimately generate the cytolytic MAC. Initiation of the CP & LP leads to activation of C4 and C2. The arising anaphylotoxins activate the immune system. The larger fragments interact with cell surfaces, receptors, immune complexes or other complement proteins. This way among others the C3 convertase (C4b2b) is formed. The complement system is involved in a number of diseases like transplantation rejection, kidney diseases, AMD and inflammatory diseases. Therefor complement fragments serve as biomarkers for many of these diseases. C4 is a glycoprotein consisting of an alpha chain, beta chain and gamma chain. Activation yields C4a and C4b. C4b is inactivated by factor I in the presence of C4bp resulting in C4c and C4d. Thus soluble C4c is a measure of complement activation.
Host
Human
Reactivity
Applications
Conjugation

The monoclonal antibody 12D11 (also known as clone M4d3) recognizes an epitope on the alpha 2 chain of human C4d. Complement factor C4 (MW 41 kDa), formerly known as Gg protein, consists of an alpha-, beta- and gamma-chain. The classical pathway of complement and the mannose binding lectin (MBL) activation pathway converge at C4. Activated C1, MASP-1 and MASP-2 cleave C4 resulting in the formation of C4a and C4b. The latter can be cleaved by factor I resulting in C4c and C4d, in which step all functional sites are lost. The C4d activation fragment of C4 is an excellent marker for classical complement pathway and MBL pathway activation. The thioester formed between the side chains of Cys1010 and Gln1013 within the C4d region of the α-chain mediates covalent attachment to the target surface bearing activated forms of C1s or MASP. Furthermore, C4d is highly homologous to C3d with over 35% shared amino acid sequence. In a number of diseases such as rheumatoid arthritis (RA), hereditary angioedema (HAE), systemic lupus erythematosus (SLE) and chronic urticaria with hypercomplementemia levels of C4d are significantly elevated in serum or plasma. C4d levels may also be elevated in plasma from patients with a variety of humoral autoimmune diseases in which complement activation is known to occur. Deposition of C4d in peritubular capillaries has been shown to be a sensitive marker for antibody-mediated (humoral) rejection in renal transplant biopsies. The monoclonal antibody 12D11 recognizes C4, C4b and C4d. Antibody 12D11 cross reacts with pig, bovine, baboon and rhesus monkey.
Host
Human
Reactivity
Applications
Conjugation

The monoclonal antibody 7H4 (also known as clone M4d2) recognizes an epitope on the alpha 2 chain of human C4d. Complement factor C4 (MW 41 kDa), formerly known as Gg protein, consists of an alpha-, beta- and gamma-chain. The classical pathway of complement and the mannose binding lectin (MBL) activation pathway converge at C4. Activated C1, MASP-1 and MASP-2 cleave C4 resulting in the formation of C4a and C4b. The latter can be cleaved by factor I resulting in C4c and C4d, in which step all functional sites are lost. The C4d activation fragment of C4 is an excellent marker for classical complement pathway and MBL pathway activation. The thioester formed between the side chains of Cys1010 and Gln1013 within the C4d region of the α-chain mediates covalent attachment to the target surface bearing activated forms of C1s or MASP. Furthermore, C4d is highly homologous to C3d with over 35% shared amino acid sequence. In a number of diseases such as rheumatoid arthritis (RA), hereditary angioedema (HAE), systemic lupus erythematosus (SLE) and chronic urticaria with hypercomplementemia levels of C4d are significantly elevated in serum or plasma. C4d levels may also be elevated in plasma from patients with a variety of humoral autoimmune diseases in which complement activation is known to occur. Deposition of C4d in peritubular capillaries has been shown to be a sensitive marker for antibody-mediated (humoral) rejection in renal transplant biopsies. The monoclonal antibody 7H4 recognizes C4, C4b and C4d. Antibody 7H4 cross reacts with guinea pig.
Host
Human
Reactivity
Applications
Conjugation

The polyclonal antibody recognizes mouse C4d. Complement factor C4 (MW 41 kDa), formerly known as Gg protein, consists of an alpha-, beta- and gamma-chain. The classical pathway of complement and the mannose binding lectin (MBL) activation pathway converge at C4. Activated C1, MASP-1 and MASP-2 cleave C4 resulting in the formation of C4a and C4b. The latter can be cleaved by factor I resulting in C4c and C4d, in which step all functional sites are lost. The C4d activation fragment of C4 is an excellent marker for classical complement pathway and MBL pathway activation. The thioester formed between the side chains of Cys1010 and Gln1013 within the C4d region of the α-chain mediates covalent attachment to the target surface bearing activated forms of C1s or MASP. Furthermore, C4d is highly homologous to C3d with over 35% shared amino acid sequence. In a number of diseases such as rheumatoid arthritis (RA), hereditary angioedema (HAE), systemic lupus erythematosus (SLE) and chronic urticaria with hypercomplementemia levels of C4d are significantly elevated in serum or plasma. C4d levels may also be elevated in plasma from patients with a variety of humoral autoimmune diseases in which complement activation is known to occur. Deposition of C4d in peritubular capillaries has been shown to be a sensitive marker for antibody-mediated (humoral) rejection in renal transplant biopsies.
Host
Mouse
Reactivity
Applications
Conjugation

The polyclonal antibody recognizes rat C4d. Complement factor C4 (MW 41 kDa), formerly known as Gg protein, consists of an alpha-, beta- and gamma-chain. The classical pathway of complement and the mannose binding lectin (MBL) activation pathway converge at C4. Activated, MASP-1 and MASP-2 cleave C4 resulting in the formation of C4a and C4b. The latter can be cleaved by factor I resulting in C4c and C4d, in which step all functional sites are lost. The C4d activation fragment of C4 is an excellent marker for classical complement pathway and MBL pathway activation. The thioester formed between the side chains of Cys1010 and Gln1013 within the C4d region of the α-chain mediates covalent attachment to the target surface bearing activated forms of C1s or MASP. Furthermore, C4d is highly homologous to C3d with over 35% shared amino acid sequence. In a number of diseases such as rheumatoid arthritis (RA), hereditary angioedema (HAE), systemic lupus erythematosus (SLE) and chronic urticaria with hypercomplementemia levels of C4d are significantly elevated in serum or plasma. C4d levels may also be elevated in plasma from patients with a variety of humoral autoimmune diseases in which complement activation is known to occur. Deposition of C4d in peritubular capillaries has been shown to be a sensitive marker for antibody-mediated (humoral) rejection in renal transplant biopsies.
Host
Rat
Reactivity
Applications
Conjugation

Monoclonal antibody 557 specifically recognizes an epitope of complement factor 5 (C5) and its active fragment, C5a. The complement system, comprising over 30 proteins, is activated in response to tissue injury, invading pathogens, or foreign surfaces. It plays a critical role in both the activation and lytic pathways of the immune response. In the complement activation pathways, C5 is cleaved after C3, producing C5a—a well-characterized cleavage product with potent chemotactic and anaphylatoxic properties. C5a is essential for the innate immune response and is increasingly recognized for its role in adaptive immunity as well. C5a is a 74-residue pro-inflammatory polypeptide that triggers various immune functions, including smooth muscle contraction, increased vascular permeability, and the release of lysosomal enzymes. It also promotes the directed migration of neutrophils, eosinophils, basophils, and monocytes. C5a exerts its effects primarily through two receptors: C5aR (also known as C5R1 or CD88) and C5L2 (gpr77). These seven-transmembrane domain receptors are widely expressed, especially on immune cells such as macrophages, neutrophils, and T cells. C5aR is well-known for initiating G-protein-coupled signaling pathways that stimulate the production of cytokines like TNF-alpha, IL-1beta, IL-6, and IL-8. Blocking C5aR has been shown to significantly reduce inflammatory damage in vivo. In contrast, the function of C5L2 is less understood, as its interaction with C5a does not trigger calcium signaling. The widespread presence of C5a receptors throughout the body allows C5a to mediate a broad range of effects. Consequently, C5a is a key pathogenic factor in various immuno-inflammatory diseases and has been implicated in non-immunological processes like CNS development, neurodegeneration, tissue regeneration, and hematopoiesis. Monoclonal antibody 557 effectively inhibits the binding of C5a to the C5a receptor through a competitive mechanism, preventing receptor activation. However, it does not interfere with the cleavage of C5 into C5a and C5b. The inhibition of the classical pathway can be measured with the human classical pathway assay ( HK3010 ).
Host
Human
Reactivity
Applications
Conjugation

Monoclonal antibody 561 specifically recognizes the N-terminus of complement component C5. This antibody reacts with both intact C5 (190 kDa) and its cleavage product, C5a (115 kDa). C5a, originally identified as a cleavage product of C5, is now known for its significant chemotactic and anaphylatoxic properties. It plays a key role in the innate immune response and is increasingly recognized for its potential involvement in adaptive immunity. C5a is a 74-residue pro-inflammatory polypeptide that induces smooth muscle contraction, increases vascular permeability, triggers the release of lysosomal enzymes, and causes degranulation of mast cells and basophils. Additionally, C5a directs the migration of immune cells such as neutrophils, eosinophils, basophils, and monocytes. C5a binds to two primary receptors: C5aR (C5R1, CD88) and C5L2 (gpr77). These receptors are widely expressed across various cell types, particularly on immune cells like macrophages, neutrophils, and T cells. C5aR is a well-characterized receptor that triggers G-protein-coupled signaling pathways, which lead to the production of cytokines such as TNF-alpha, IL-1beta, IL-6, and IL-8. Blocking C5aR has been shown to significantly reduce inflammatory damage in vivo. While less is known about C5L2, it is understood that C5a binding to this receptor does not initiate calcium signaling. The widespread expression of C5a receptors enables C5a to influence a wide range of physiological processes. As a result, C5a has emerged as a key pathogenic factor in numerous immuno-inflammatory diseases. Beyond its immunological roles, C5a is now also associated with non-immunological processes, such as developmental biology, CNS development, neurodegeneration, tissue regeneration, and hematopoiesis. The monoclonal antibody 561 can inhibit the classical pathway by targeting C5 and C5a, this can be measured utilizing the classical pathway assay ( HK3010 ).
Host
Human
Reactivity
Applications
Conjugation

Monoclonal antibody 568 reacts with an epitope on C5 and on C5b. C5 is involved in the activation of the lythic pathway within the complement system which is an important factor in innate immunity. The complement pathways can be divided in the activation pathways and lytic pathway. The activation pathways lead via C3 to the cleavage of the fifth complement component C5 into C5a and C5b. C5b initiates the assembly of the membrane attack complex (MAC) that mediates cytolysis.
Host
Human
Reactivity
Applications
Conjugation
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