iC3b Antibody (Monoclonal - neoantigen)
A murine monoclonal antibody to a neo-epitope expressed on iC3b.
Product Specifications
Citations | 26 |
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Clonality |
Monoclonal |
Immunogen | Purified human protein. |
Applications | See citations and technical data sheet for application info. |
Concentration | ≥ 1.0 mg/mL |
Conjugate | Unconjugated |
Cross Reactivity |
Human |
Ordering Information
Catalog Number | A209 |
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Catalog Number (CE) | N/A |
Size | 100 µl |
Price (USD) | $365.00 |
Price (EURO) | 330,00 € |
Contact us
US Phone | +1 (858) 552 1100 |
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EU Phone | +353 (91) 412 474 |
US Email | contact-us@quidelortho.com |
EU Email | contact-emea@quidelortho.com |
- Specifications
- Citations
- Certificate of Analysis
Specifications
Description |
A murine monoclonal antibody to a neo-epitope expressed on iC3b. |
---|---|
Size | 100 µl |
Concentration |
≥ 1.0 mg/mL |
Applications | See citations and technical data sheet for application info. |
Form | Liquid. Borate Buffered Saline (pH 8.4 ± 0.2), with ≤ 0.1% Sodium Azide. |
Clonality | Monoclonal |
Immunogen | Purified human protein. |
Conjugate | Unconjugated |
Cross Reactivity | Human |
Isotype | IgG2bk |
Purity | > 95% by SDS PAGE |
Source |
Mouse |
Specificity | This monoclonal antibody was raised against purified human iC3b. It is specific for a neo-antigen on iC3b. |
Storage |
Short term (30 days) 4˚C. Long term at or below –20˚C. |
Background |
Under normal conditions, activation of either of the complement pathways leads to the formation of C3 convertase enzymes which cleave C3 into two fragments C3a, an anaphylatoxin, and C3b.The C3b fragment has many biologic functions including promotion of phagocytosis and participation as a structural component in both the C3 and C5 convertase enzymes. These processes are under stringent control in vivo. One control mechanism involves a two-site cleavage of C3b by Factor I with the cooperation of Factor H or CR1 as cofactors. When cleaved in this way the biologic functions of C3b are lost. The resulting protein is termed iC3b.This fragment, in turn, has a host of new biologic activities. iC3b fragments, either in fluid phase or bound to biological surfaces, can interact with a variety of cell types expressing complement receptors (either CR2 or CR3). iC3b levels in fluid phase are elevated in a variety of disease states including Systemic Lupus Erythematosis, Rheumatoid Arthritis as well as in a variety of pathologic conditions including sepsis and Myocardial Infarct. Quidel’s monoclonal antibodies to complement antigens were prepared using standard techniques. They are purified from mouse ascites fluid via protein A affinity chromatography. 3 The specificity of the monoclonal antibody was established via a series of immunological techniques including ELISA, hemagglutination and RIA. Firstly, the antibody was shown by ELISA to bind to C3 antigens using highly pure, immobilized C3. Subsequent studies showed that this antibody agglutinates EC3bi but not EC3b or EC3d cells in an indirect hemagglutination assay. Further experiments showed that this antibody bound to radio-labeled purified iC3b but not to similarly labeled C3, C3b, C3d, or C3c. |
Citations
Title | Year | Applications | Sample Species | Sample | Sample Details |
---|---|---|---|---|---|
2007 | WB |
Bacteria |
Pneumococci |
||
2002 | Confocal Microscopy |
Cell Culture |
Jurkat Cells |
||
2021 | ELISA |
Human |
Plasma |
Sickel Cell Anemia |
|
2009 | ELISA |
Human |
Plasma |
||
Arabinosylation of recombinant human immunoglobulin-based protein therapeutics |
2017 | ELISA |
Human |
Serum |
|
2018 | ELISA |
Human |
Serum |
||
2018 | ELISA |
Human |
Plasma |
Age-Related Macular Degeneration |
|
2018 | ELISA |
Human |
Plasma |
Alzheimer's Disease |
|
Complement-dependent proinflammatory properties of the Alzheimer's disease beta-peptide. |
1998 | ELISA |
Human |
Amyloid-βeta peptides & NHS |
|
Complement activation by heme as a secondary hit for atypical hemolytic uremic syndrome. |
2013 | FC |
Human |
HUVEC Cells |
aHUS |
2016 | FC |
Human |
Serum |
B. anthracis incubated |
|
Eculizumab treatment: stochastic occurrence of C3 binding to individual PNH erythrocytes. |
2017 | FC |
Human |
Red Blood Cells |
PNH |
2017 | FC |
Human |
NK Cells |
||
Complement activation in the Parkinson’s disease substantia nigra: an immunocytochemical study. |
2006 | ICC, IHC |
Human |
Brain Tissue |
|
Plaque complement activation and cognitive loss in Alzheimer’s disease. |
2008 | ICC, IHC |
Human |
Brain Tissue |
|
2022 | IHC |
Human |
Skin Tissue |
Cutaneous Vasculitis |
|
2000 | IHC |
Human |
Brain Tissue |
Fetal |
|
2011 | IHC |
Human |
Lung Tissue |
Asthmatic Alzheimer's |
|
2011 | IHC |
Human |
Lung Tissue |
||
Tumor necrosis-initiated complement activation stimulates proliferation of medulloblastoma cells. |
2015 | IHC |
Human |
Brain Tissue |
Medullablastoma |
quantitative lateral flow assay to detect complement activation in blood. |
2015 | Lateral Flow Assay |
Human |
Plasma |
|
2021 | WB |
Human |
Serum |
Aspergillus incubated |
|
Efficient complement-mediated clearance of immunosuppressed T cells by macrophages. |
2023 | IF |
Human |
T Cells |
Immunosuppressed |
2024 | IHC |
Human |
Skin Tissue |
Psoriasis |
|
2024 | ICC |
Human |
Keratinocytes |
Psoriasis |
|
2012 | FC |
Parasite |
Entamoeba histolytica |