Biosimilar Antibodies
C5aR, Human, mAb W17/1, Hycult Biotech, HM2095
The human anaphylatoxin C5a is a 74-residu glycopolypeptide which is generated by proteolytic cleavage of the complement factor C5 in the course of complement activation. A variety of biological effects evoked by C5a could be demonstrated, rendering this molecule an important mediator of inflammation, with granulocytes and macrophages as the main target cells. All cellular responses to C5a are specifically mediated by interactions with the membrane bound C5a receptor, a seven transmembrane GTP-binding-protein-coupled receptor that belongs to the rhodopsin supergene family. The C5a receptor is approximately 45 kDa.
Host
Human
Reactivity
Applications
Conjugation
C5aR, Mouse, mAb 10/92, Hycult Biotech, HM1077
The monoclonal antibody 10/92 recognizes the mouse receptor C5a (C5aR, CD88). The mouse anaphylatoxin C5a is a 74-residu glycopolypeptide which is generated by proteolytic cleavage of the complement factor C5 in the course of complement activation. A variety of biological effects evoked by C5a could be demonstrated, rendering this molecule an important mediator of inflammation, with granulocytes and macrophages as the main target cells. All cellular responses to C5a are specifically mediated by interactions with the membrane bound C5a receptor, a seven transmembrane GTP-binding-protein-coupled receptor that belongs to the rhodopsin supergene family. The 45 kDa C5a receptor is expressed by neutrophils, monocytes/macrophages, dendritic cells, astrocytes and microglia. In contrast, C5a receptor is not detectable on resting or stimulated murine T and B lymphocytes. The monoclonal antibody 10/92 does not inhibit the binding of C5a to its receptor.
Host
Mouse
Reactivity
Applications
Conjugation
C5aR, Mouse, mAb 20/70, Hycult Biotech, HM1076
The monoclonal antibody 20/70 recognizes the mouse receptor for C5a (CD88). The mouse anaphylatoxin complement factor C5a, a split product of C5, is one of the most potent inflammatory chemoattractants and interacts with two C51 receptors, C5aR and C5L2. Most of the C5a effects are mediated through C5aR. C5aR is known to be crucial in the initiation of acute inflammatory responses. C5a receptor is a seven transmembrane GTP-binding-protein-coupled receptor that belongs to the rhodopsin supergene family. The 45 kDa C5a receptor is expressed by leukocytes such as neutrophils, eosinophils, basophils, monocytes, dendritic cells and mast cells. C5aR can be expressed on both immune and nonimmune cells. Nonimmune cells expressing C5aR include vascular endothelial cells, cardiomyocytes and bronchial epithelial cells. Signaling of C5aR involves intracellular calcium mobilization and activation of among others protein kinase- B (PKB) and protein phospholipase D (PLD) pathways. High C5aR expression levels have been associated with the pathogenesis of many inflammatory conditions, autoimmune and neurodegenerative diseases like rheumatoid arthritis, multiple sclerosis, atherosclerosis and inflammatory bowel diseases. In vivo blockade of C5aR greatly reduces inflammatory injury. The monoclonal antibody 20/70 has been used in functional studies and is capable to prevent the binding of C5a to its receptor.
Host
Mouse
Reactivity
Applications
Conjugation
C5aR, Rat, mAb R63, Hycult Biotech, HM3017
The monoclonal antibody R63 reacts with the rat receptor for C5a (CD88). The rat anaphylatoxin C5a, a 77-amino acid glycopolypeptide generated by proteolytic cleavage of C5, is one of the most potent inflammatory chemo attractants and interacts with two C5a receptors, C5aR and C5L2.- Most of the C5a effects are mediated through C5aR. C5aR is known to be crucial in the initiation of acute inflammatory responses. C5a receptor is a seven transmembrane GTP-binding-protein-coupled receptor that belongs to the rhodopsin supergene family. The 45 kDa C5a receptor is expressed by leukocytes such as neutrophils, eosinophils, basophils, monocytes, dendritic cells and mast cells. C5aR can be expressed on both immune and non-immune cells. The latter, include vascular endothelial cells, cardiomyocytes and bronchial epithelial cells. Signaling of C5aR involves intracellular calcium mobilization and activation of among others protein kinase- B (PKB) and protein phospholipase D (PLD) pathways. High C5aR expression levels have been associated with the pathogenesis of many inflammatory conditions, autoimmune and neurodegenerative diseases like rheumatoid arthritis, multiple sclerosis, atherosclerosis and inflammatory bowel disease. In vivo blockade of C5aR greatly reduces inflammatory injury. Using immunohistology there is no evidence for non-myeloid expression in healthy control rats. However, under inflammatory situations, the C5aR was found to be upregulated in various organs and tissues including the liver.Antibody R63 is directed against the amino-terminal domain Ex1 of the rat C5aR.
Host
Rat
Reactivity
Applications
Conjugation
C5b-9, Rat, mAb 2A1, Hycult Biotech, HM3033
Monoclonal antibody 2A1 for detection of rat C5b-9/TCC. The monoclonal antibody 2A1 recognizes rat C5b-9 (TCC) and competes with human C9 antibodies for the C5b-9 epitope. Therefore, this implies that the reactive epitope is located on the C9 molecule. In serum, five precursor molecules cooperate to assemble C5b-9 membrane attack complexes. First, C5 convertase cleaves C5, forming C5b, which then triggers C5b-9 complex formation. Subsequently, in the final step, C9 polymerizes, enabling the complex to insert into the cell membrane. Simultaneously, during C5b-8 formation and C9 polymerization, specific neoantigens emerge that are not present on native complex components. To control this process, complement proteins such as CD59 and complement S-protein actively prevent C5b-9 from inserting into the cell membrane. Hence, the SC5b-9 complex remains cytolytically inactive and is unable to adhere to cells. Importantly, C5b-9 is crucial in chronic proteinuric renal disease by constantly driving tubulointerstitial damage. Therefore, reducing C5b-9 formation can significantly mitigate early tubulointerstitial injury in the remnant kidney. To address this, the monoclonal antibody 2A1 was specifically developed against a rat C5b-9 neoantigen. Due to its specificity, this antibody serves as a reliable antibody for detecting C5b-9 in plasma and urine samples. You may also find monoclonal antibody HM3034 clone 3G11 , which recognizes rat C6, to be of interest.
Host
Rat
Reactivity
Applications
Conjugation
C5L2, Human, pAb, Hycult Biotech, HP9036
The orphan receptor C5L2/pgpr77, which shares 35% amino identity with CD88, is a promiscuous complement fragment-binding protein. C5L2 binds C5a with high affinity but has a 10-fold higher affinity for C5adR than CD88. C5L2 also has an affinity for C4a and C3a, and their metabolites C4a des-Arg, and C3a des-Arg. C3a binds at a site distinct from the C5a binding site. C5L2 transfected into cells does not support degranulation or increases in intracellular [Ca2+] and is not rapidly internalized in response to ligand binding. However, ligation of C5L2 by anaphylatoxin potentiates the degranulation response to cross-linkage of the high affinity IgE receptor suggesting that C5L2 is an anaphylatoxin-binding protein with unique ligand binding and signalling properties. C5L2 is proposed to mediate the acylation-stimulating properties of C3a des-Arg/ASP. C5L2 is expressed in granulocytes, in mature dendritic cells, adipose tissue and fibroblasts.
Host
Human
Reactivity
Applications
Conjugation
C5L2, Mouse, pAb, Hycult Biotech, HP8015
The orphan receptor C5L2/pgpr77, which shares 35% amino identity with CD88, is a promiscuous complement fragment-binding protein. C5L2 binds C5a with high affinity but has a 10-fold higher affinity for C5adR than CD88. C5L2 also has an affinity for C4a and C3a, and their metabolites C4a des-Arg, and C3a des-Arg. C3a binds at a site distinct from the C5a binding site. C5L2 transfected into cells does not support degranulation or increases in intracellular [Ca2+] and is not rapidly internalized in response to ligand binding. However, ligation of C5L2 by anaphylatoxin potentiates the degranulation response to cross-linkage of the high affinity IgE receptor suggesting that C5L2 is an anaphylatoxin-binding protein with unique ligand binding and signalling properties. C5L2 is proposed to mediate the acylation-stimulating properties of C3a des-Arg/ASP. C5L2 is expressed in granulocytes, in mature dendritic cells, adipose tissue and fibroblasts.
Host
Mouse
Reactivity
Applications
Conjugation
C6, Human, mAb WU 6-4, Hycult Biotech, HM2276
The monoclonal antibody WU 6-4 recognizes C6, one of the components of the terminal complement complex (TCC), also know as the membrane attack complex (MAC). Proteolytic cleavage of C5 by C5 convertase generates C5b which initiates assembly of the C5b-9 MAC. This complex is assembled from five precursor molecules in the serum, finalized with the polymerization of C9 which accompanies insertion of the complex into the cell membrane causing cellular lysis. Polymorphonuclear leukocytes represent a major source of C6. The monoclonal antibody WU 6-4 recognizes native C6 but not C6 after incorporation into the TCC. Furthermore, WU 6-4 is capable of inhibiting C5b6 and TCC formation in the fluid phase and to a lesser extent, haemolysis. Haemolytic activity could be inhibited only when WU 6-4 was introduced before C5b6 formation.
Host
Human
Reactivity
Applications
Conjugation
C6, Mouse, pAb, Hycult Biotech, HP8014
During complement activation the circulating complement compound C6 is bound by the C3b5b complex to form the first stage of the membrane attack complex. The formed C5b6 complex binds to C7 where after C8 binds, followed by binding of a variable amount of C9 molecules. The complement factor C6 is an acute-phase reactant for which a CCAAT enhancer binding site essential is.
Host
Mouse
Reactivity
Applications
Conjugation
C6, Rat, mAb 3G11, Hycult Biotech, HM3034
Monoclonal antibody 3G11 for detection of rat C6. This monoclonal antibody clone 3G11 recognizes rat C6. Complement component C6 is a key part of the C5b-9 membrane attack complex (MAC/TCC). In serum, five precursor molecules cooperate to assemble C5b-9 membrane attack complexes. First, C5 convertase cleaves C5, forming C5b, which then triggers C5b-9 complex formation. Subsequently, in the final step, C9 polymerizes, enabling the complex to insert into the cell membrane. Simultaneously, during C5b-8 formation and C9 polymerization, specific neoantigens emerge that are not present on native complex components. The rat remnant kidney model has been widely used to study mechanisms underlying renal disease progression. Proteinuria demonstrates nephrotoxic properties and contributes to renal injury. Complement activation in proteinuric urine results in tubular and interstitial damage. However, in C6-deficient rats, acute interstitial changes resolved despite persistent proteinuria. This finding suggests that C6 plays an important role in mediating chronic tubulointerstitial damage in remnant kidney models. To address this, the monoclonal antibody 3G11 was specifically developed by immunizing mice with C6 isolated from rat serum. Due to its specificity, this antibody serves as a reliable antibody for detecting C6 in both serum and urine samples antibody in immunoassays to measure C5b-9 in both serum and urine samples. You may also find monoclonal antibody HM3033 clone 2A1 which recognizes rat C5b-9, to be of interest.
Host
Rat
Reactivity
Applications
Conjugation
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