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This mouse monoclonal Anti-Complement C3b/iC3b Antibody, clone 5G9, Cat. No. MABF961 is a neutralizing antibody validated for use in Flow Cytometry, for the detection of C3b.
More>>This mouse monoclonal Anti-Complement C3b/iC3b Antibody, clone 5G9, Cat. No. MABF961 is a neutralizing antibody validated for use in Flow Cytometry, for the detection of C3b. Less<<
SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1
Complement C3 beta chain
C3-beta-c
C3bc
Complement C3 alpha chain
C3a anaphylatoxin
Acylation stimulating protein
ASP
C3adesArg
Complement C3b alpha' chain
Complement C3c alpha' chain fragment 1
Complement C3dg fragment
Complement C3g fragment
Complement C3d fragment
Complement C3f fragment
Complement C3c alpha' chain fragment 2
Complement C3b/iC3b
Background Information
Complement C3 (UniProt P01024; also known as C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1) is encoded by the C3 (also known as CPAMD1) gene (Gene ID 718) in human. C3 is initially translated with an N-terminal 22-amino acid signal peptide sequence, which is then removed to produce the 1641-amino acid mature C3. It plays a central role in the activation of the complement system. Its activation is required for the activation of both classical and alternative pathways of complement (CPC and APC, respectively). C3 is cleaved into C3a and C3b during CPC activation by the C3-convertase C4b2a composed of the activated C4 and C2. In APC, C3 is cleaved by the C3-convertase C3bBb composed C3b and the activated form of factor B (Bb). C3b serves as an opsonizing agent, and can be further cleaved by Factor I into C3c and C3d. iC3b is a proteolytically inactive C3b fragment that still opsonizes target microbes or cells, but cannot further amplify/activate the complement cascade through APC. iC3b can be further cleaved to C3dg, and finally to C3d. Unregulated activation of APC can result in paroxysmal nocturnal hemoglobinuria (PNH) that is characterized by chronic intravascular hemolysis. Clinical C5-neutralizing mAb treatment prevents the formation of cytolytic membrane attack complex (MAC) of complement, but does not block APC activation. Consequently, PNH patients are left with immune-mediated hemolytic anemia and their erythrocytes become opsonized with complement C3. Monoclonal antibodies (mAbs) against C3b/iC3b are useful for monitoring and studying C3b/iC3b deposit on PNH blood cells and mAbs with neutralizing activities are useful tools for studying C3-mediated CPC and APC.
References
Product Information
Format
Purified
Presentation
Purified mouse monoclonal IgG2aκ antibody in buffer containing PBS without preservatives.
This mouse monoclonal Anti-Complement C3b/iC3b Antibody, clone 5G9, Cat. No. MABF961 is a neutralizing antibody validated for use in Flow Cytometry, for the detection of C3b.
Key Applications
Flow Cytometry
Neutralizing
Application Notes
Neutralizing Analysis: This clone has been shown to prevent alternative pathway of complement (APC) activation-mediated hemolysis of IgM-opsinized paroxysmal nocturnal hemoglobinuria (PNH) erthyrocytes (Lindorfer, M.A., et al. (2010). Blood. 115(11):2283-2291).
Biological Information
Immunogen
Sepharose 4B beads with surface C3b/C3bi deposits via APC in normal human serum corresponding to the iC3b of human Complement C3b/iC3b.
Epitope
iC3b
Clone
5G9
Concentration
Please refer to lot specific datasheet.
Host
Mouse
Specificity
This clone blocks the activation of classical pathway of complement (CPC) by binding C3b and iC3b.
Flow Cytometry Analysis: This antibody (200 ug mAb/5 x 10e6 cells/mL) detected C3b/iC3b deposit on human Burkett's lymphoma Raji B cells opsonized with anti-CD20 mAb Rituximab (RTX) in the presence of 50% normal human serum (NHS).
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Stable for 1 year at -20°C from date of receipt. Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
A novel approach to preventing the hemolysis of paroxysmal nocturnal hemoglobinuria: both complement-mediated cytolysis and C3 deposition are blocked by a monoclonal antibody specific for the alternative pathway of complement. Lindorfer, MA; Pawluczkowycz, AW; Peek, EM; Hickman, K; Taylor, RP; Parker, CJ Blood
115
2283-91
2009
The clinical hallmark of paroxysmal nocturnal hemoglobinuria (PNH) is chronic intravascular hemolysis that is a consequence of unregulated activation of the alternative pathway of complement (APC). Intravascular hemolysis can be inhibited in patients by treatment with eculizumab, a monoclonal antibody that binds complement C5 thereby preventing formation of the cytolytic membrane attack complex of complement. However, in essentially all patients treated with eculizumab, persistent anemia, reticulocytosis, and biochemical evidence of hemolysis are observed; and in a significant proportion, their PNH erythrocytes become opsonized with complement C3. These observations suggest that PNH patients treated with eculizumab are left with clinically significant immune-mediated hemolytic anemia because the antibody does not block APC activation. With a goal of improving PNH therapy, we characterized the activity of anti-C3b/iC3b monoclonal antibody 3E7 in an in vitro model of APC-mediated hemolysis. We show that 3E7 and its chimeric-deimmunized derivative H17 block both hemolysis and C3 deposition on PNH erythrocytes. The antibody is specific for the APC C3/C5 convertase because classical pathway-mediated hemolysis is unaffected by 3E7/H17. These findings suggest an approach to PNH treatment in which both intravascular and extravascular hemolysis can be inhibited while preserving important immune functions of the classical pathway of complement.
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