Anti c5b 9 clone ae11

Manufactured by Agilent Technologies

The Anti-C5b-9 (clone AE11) is a monoclonal antibody that specifically binds to the C5b-9 membrane attack complex (MAC) of the complement system. This antibody can be used for the detection and quantification of the C5b-9 complex in various biological samples.

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Lab products found in correlation

Anti apoe, by Merck Group (2 mentions) Recombinant apoe isoforms, by BioCat (2 mentions) Apoe3, by Romer Labs (2 mentions) Apoe 75 85, by Cell Biolabs (2 mentions) Apoe 139 152, by Cell Biolabs (2 mentions) Apoe 210 232, by Cell Biolabs (2 mentions) Mda ldl, by Cell Biolabs (2 mentions) Copper oxidized ldl oxldl, by Thermo Fisher Scientific (2 mentions) Anti aβ clone32a1, by AbFrontier (2 mentions) Alexa fluor 488 goat anti mouse igg, by Jackson ImmunoResearch (1 mentions) Facscalibur, by BD (1 mentions)

Close spelling variants of this product

Murine anti-human C5b-9 antibody (clone aE11, Anti-C5b-9 Anti-TM

3 protocols using anti c5b 9 clone ae11

Characterization of Complement-ApoE Interactions

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Complement components C2, C3, C3b, C4, C4b, C1q, C1s, Factor H, Factor
I, and C4BP as well as all primary antibodies (anti C1q, A200/3b; anti C2,
A212/18b; anti C3, A213/5a; anti C4, A201/3a; anti factor H, A237/4) were
purchased from Complement Technology. Recombinant ApoE isoforms from BioCat;
plasma-purified ApoE3 from Biopure. ApoE peptides were generated by Peptide 2.0:
ApoE 30-40 LGRFWDYLRWV; ApoE 75-85 YKSELEEQLTPV; ApoE 139-152 SHLRKLRKRLLRDA;
ApoE 210-232 WGERLRARMEEMGSRTRDRLDEV. LDL and malondialdehyde-modified LDL
(MDA-LDL) were from Cell Biolabs, copper oxidized LDL (oxLDL) from Thermo Fisher
(L34357), ApoA from Athens Research&Technology, vitronectin (Vnt) from
Corning. Aβ and Aβ fibrils from GenSript. Recombinant EfB was
expressed as described65 . Additional
antisera used were: anti-C5b-9 (clone AE11-MO777-Dako), anti C1s
(11951-05011-AssaybioTch), anti ApoE ((178479-Calbiochem), anti ApoE (Merck,
178479), anti LDLR (HB04JL2204-B-SinoBiological), anti Aβ (clone
32A1-Abfrontier), anti goat IgG (13C0836-Sigma Aldrich) and anti rabbit IgG
(13C0529-Sima Aldrich), IgM (120228-Jackson ImmunoResearch Laboratories).

Yin C., Ackermann S., Ma Z., Mohanta S.K., Zhang C., Li Y., Nietzsche S., Westermann M., Peng L., Hu D., Bontha S.V., Srikakulapu P., Beer M., Megens R.T., Steffens S., Hildner M., Halder L.D., Eckstein H.H., Pelisek J., Herms J., Roeber S., Arzberger T., Borodovsky A., Habenicht L., Binder C.J., Weber C., Zipfel P.F., Skerka C, & Habenicht A.J. (2019). ApoE attenuates unresolvable inflammation by complex formation with activated C1q. Nature medicine, 25(3), 496-506.

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Complement Deposition on Neisseria Meningitidis

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Strains were grown on GC chocolate agar plates overnight at 37 °C, 5% CO₂. 2 × 10⁸ cells were incubated in VBS/BSA with 5% or 10% NHS or heat-inactivated (56 °C at 30 min) NHS (HIS) as negative control for ten minutes at 37 °C while shaking (200 rpm). The reaction was stopped on ice by addition of 400 µl of cold Hank’s Balanced salt solution containing 1 mM Ca²⁺, 0.15 mM Mg²⁺ and 1% BSA (HBSS⁺⁺/BSA). Bacteria were washed twice with HBSS⁺⁺/BSA. Antibody incubations were done in a final volume of 50 µl in HBSS⁺⁺/BSA at 37 °C for 30 minutes and shaking at 700 rpm. Monoclonal antibody anti-C5b9 (clone aE11; Dako cytomation) was used to detect terminal complex of complement deposited onto the N. meningitidis surface. After washing, AlexaFluor488 goat anti-mouse IgG (Jackson ImmunoResearch) was used as secondary antibody. Bacteria were fixed in PBS with 1% formaldehyde for 1 h, then pelleted and resuspended in 400 µl PBS before analysing samples on a FACS Calibur (Becton Dickinson).

Claus H., Hubert K., Becher D., Otto A., Pawlik M.C., Lappann I., Strobel L., Vogel U, & Johswich K. (2019). A homopolymeric adenosine tract in the promoter region of nspA influences factor H-mediated serum resistance in Neisseria meningitidis. Scientific Reports, 9, 2736.

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Characterization of Complement-ApoE Interactions

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