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产品介绍
Monoclonal Antibody to Human SC5b-9 (Neoantigen)
A239
100 µL
IgG2ak
> 1.0 mg/mL
≥ 95% by SDS PAGE
Borate Buffered Saline (pH 8.4 ± 0.2)
Human, baboon, Cynomologus macaque, Rhesus macaque.
≤ 30 Days 2-8˚C
> 30 Days ≤ –20˚C
EIA、FACS、IHC、WB、IF
For Research Use Only. Not for use in diagnostic procedures.
A murine monoclonal antibody to a neoantigen on the terminal complement complex.
This monoclonal antibody was raised against purified human C9. This antibody has been shown to bind to a neoantigen expressed on SC5b-9, TCC, MAC, poly- C9 and on denatured immobilized C9.
The Terminal Complement Complex (TCC, SC5b-9) is generated by the assembly of C5 through C9 as a consequence of activation of the complement system by either the classical, lectin or alternative pathway. The membrane attack complex (MAC), a form of TCC, is a stable complex that mediates the irreversible target cell membrane damage associated with complement activation. Complexes formed in the absence of a target membrane bind to naturally occurring regulatory serum proteins, e.g. the S protein, at the C5b-7 stage of assembly forming soluble, non-lytic TCC
The specificity of the monoclonal antibody was established via a series of immunoassays. First, the antibody was shown by ELISA to bind SC5b-9 and C9 immobilized in microtiter wells, but not to immobilized C3, C5, C6, C7, C8 or S protein. Immobilized C9 is known to express antigenic determinates in common with polymeric C9. Second, free (unbound) SC5b-9, free (unbound) C9 and zymosan-activated human serum were shown (via inhibition EIA) to inhibit the binding of this antibody to immobilized SC5b-9. Subsequently, the antibody was shown to bind complement lysed sheep and rabbit erythrocytes (both of which contain TCC). The antibody therefore binds polymerized C9 present in both SC5b-9 and MAC, the two major forms of TCC.
Merri, A., Junnikala, S. Exceptional Resistance of Human H2 Gioblastoma Cells to Complement Mediated Killing by Expression and Utilization of Factor H and Factor H Like Protein 1, J Immunol 164:11 6075-6081, 2000.
Stoltzner, S., Lemerre, C. et al. Temporal accrual of complement proteins in Amyloid plaques in patients with down's syndrome with Alzheimer's Disease, Am J Path 156:489-499, 2000.
Wright, A., Morrison, S. Effect of C2 Associated Carbohydrate structure of Ig Effector function: studies with chimeric mouse human IgG1 Antibodies in glycosylation mutants of chinese hamster ovary cells, J. Immunol 160:3393-3402, 1998.
Gemmell, C. A flow cytometric immunoassay to quantify adsorption of complement activation products on artificial surfaces, J Biomed Mater Res 37, 474-480, 1997.
Rogers, J., N. Cooper, et al. Complement Activation by ß-amyloid in Alzheimer disease, PNAS 89:10016-10020, 1992.
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