complement proteins c1q, c2, c3, c3b, c4, c4b, c5, c5b, c6, c7, c8, c9 (CompTech Computer Technologies)

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CompTech Computer Technologies complement proteins c1q, c2, c3, c3b, c4, c4b, c5, c5b, c6, c7, c8, c9

SplB inhibits the alternative complement pathway. To probe the spontaneous activation of the alternative pathway, microtiter plates were coated with LPS. Increasing concentrations of SplB or BSA were incubated with appropriately diluted NHS as the source of complement for 1 h, and the mixtures were added to the microtiter plates. After incubation for 20 min at 37°C, the plates were washed, and deposited <t>C3b</t> or C5b-9 was determined with specific antisera or monoclonal antibodies. SplB but not BSA diminished the deposition of C3b (A) and C5b-9 (B).

Complement Proteins C1q, C2, C3, C3b, C4, C4b, C5, C5b, C6, C7, C8, C9, supplied by CompTech Computer Technologies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/complement+factor+c3/complement+factors+c1++c2++c3++c4/pmc08765433-254-7-24
Average 90 stars, based on 1 article reviews

complement proteins c1q, c2, c3, c3b, c4, c4b, c5, c5b, c6, c7, c8, c9 - by Bioz Stars, 2026-10

90/100 stars

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1) Product Images from "The Protease SplB of Staphylococcus aureus Targets Host Complement Components and Inhibits Complement-Mediated Bacterial Opsonophagocytosis"

Article Title: The Protease SplB of Staphylococcus aureus Targets Host Complement Components and Inhibits Complement-Mediated Bacterial Opsonophagocytosis

Journal: Journal of Bacteriology

doi: 10.1128/JB.00184-21

Figure Legend Snippet: SplB inhibits the alternative complement pathway. To probe the spontaneous activation of the alternative pathway, microtiter plates were coated with LPS. Increasing concentrations of SplB or BSA were incubated with appropriately diluted NHS as the source of complement for 1 h, and the mixtures were added to the microtiter plates. After incubation for 20 min at 37°C, the plates were washed, and deposited C3b or C5b-9 was determined with specific antisera or monoclonal antibodies. SplB but not BSA diminished the deposition of C3b (A) and C5b-9 (B).

Techniques Used: Activation Assay, Incubation, Bioprocessing

SplB inhibits the lectin and classical complement pathways. The effects of SplB on complement activation and the deposition of C3b and C5b-9 were analyzed as described in the legend to . (A and B) The lectin pathway was activated via mannan-coated microtiter plates. SplB interfered with the lectin pathway in a concentration-dependent manner, lowering the deposition of C3b (A) and C5b-9 (B). (C and D) To test for interference with the classical pathway, the microtiter wells were coated with IgM. Again, SplB reduced the classical pathway-mediated deposition of C3b (C) and C5b-9 (D) concentration dependently.

Figure Legend Snippet: SplB inhibits the lectin and classical complement pathways. The effects of SplB on complement activation and the deposition of C3b and C5b-9 were analyzed as described in the legend to . (A and B) The lectin pathway was activated via mannan-coated microtiter plates. SplB interfered with the lectin pathway in a concentration-dependent manner, lowering the deposition of C3b (A) and C5b-9 (B). (C and D) To test for interference with the classical pathway, the microtiter wells were coated with IgM. Again, SplB reduced the classical pathway-mediated deposition of C3b (C) and C5b-9 (D) concentration dependently.

Techniques Used: Activation Assay, Concentration Assay

SplB and aureolysin reduce the deposition of C3b and C5b-9 on the surface of S. aureus cells. (A) SplB or BSA (1 μM) was incubated with complement-competent NHS (5%) for 1 h, and the mixture was added to spa -deficient S. aureus cells (RN1HF Δ spa ) for 20 min at 37°C. C3b or C5b-9 on the bacterial cell surface was stained with specific fluorescent antibodies and evaluated by microscopy. In the control samples (BSA), there was abundant deposition of C3b (I, top, green) and C5b-9 (II, top, red) on the bacterial surfaces. SplB strongly interfered with complement deposition (C3b [I, bottom, green] and C5b-9 [II, bottom, red]). Panels III show bacterial DNA stained with 4′,6-diamidino-2-phenylindole (DAPI), and panels IV show the overlays of the three images. Bars, 100 μm. (B and C) SplB, aureolysin, or both were incubated with complement-active NHS (5%) for 1 h at the indicated concentrations. SplC and BSA served as controls. The resulting solutions were added to spa -deficient S. aureus cells (RN1HF Δ spa ) for 20 min at 37°C. After washing, the deposition of C3b (B) or C5b-9 (C) was stained with specific antibodies and fluorescent secondary reagents and evaluated by flow cytometry. SplB and aureolysin inhibited the deposition of C3b and C5b-9 on the bacterial surface in a concentration-dependent manner. The combination of SplB and aureolysin had the strongest effect, completely abolishing the deposition of C3b (B) and reducing the deposition of C5b-9 by 90% (C). SplC and BSA, the negative controls, had no influence on complement deposition (B and C). Depicted are means ± SD from three independent experiments.

Figure Legend Snippet: SplB and aureolysin reduce the deposition of C3b and C5b-9 on the surface of S. aureus cells. (A) SplB or BSA (1 μM) was incubated with complement-competent NHS (5%) for 1 h, and the mixture was added to spa -deficient S. aureus cells (RN1HF Δ spa ) for 20 min at 37°C. C3b or C5b-9 on the bacterial cell surface was stained with specific fluorescent antibodies and evaluated by microscopy. In the control samples (BSA), there was abundant deposition of C3b (I, top, green) and C5b-9 (II, top, red) on the bacterial surfaces. SplB strongly interfered with complement deposition (C3b [I, bottom, green] and C5b-9 [II, bottom, red]). Panels III show bacterial DNA stained with 4′,6-diamidino-2-phenylindole (DAPI), and panels IV show the overlays of the three images. Bars, 100 μm. (B and C) SplB, aureolysin, or both were incubated with complement-active NHS (5%) for 1 h at the indicated concentrations. SplC and BSA served as controls. The resulting solutions were added to spa -deficient S. aureus cells (RN1HF Δ spa ) for 20 min at 37°C. After washing, the deposition of C3b (B) or C5b-9 (C) was stained with specific antibodies and fluorescent secondary reagents and evaluated by flow cytometry. SplB and aureolysin inhibited the deposition of C3b and C5b-9 on the bacterial surface in a concentration-dependent manner. The combination of SplB and aureolysin had the strongest effect, completely abolishing the deposition of C3b (B) and reducing the deposition of C5b-9 by 90% (C). SplC and BSA, the negative controls, had no influence on complement deposition (B and C). Depicted are means ± SD from three independent experiments.

Techniques Used: Incubation, Staining, Microscopy, Control, Flow Cytometry, Concentration Assay

Purification:

Article Title: Human Astrovirus Coat Protein Inhibits Serum Complement Activation via C1, the First Component of the Classical Pathway
Article Snippet: .. Duplicate aliquots (1 g) of the purified complement factors C1, C2, C3, and C4 (CompTech) were mixed with 1 PBS and an equal volume of 2 SDS sample buffer lacking reducing agents and loaded onto a 7.5% SDS-PAGE gel without being boiled. ..

Article Title: Human Astrovirus Coat Protein Inhibits Serum Complement Activation via C1, the First Component of the Classical Pathway
Article Snippet: .. Duplicate aliquots (1 μg) of the purified complement factors C1, C2, C3, and C4 (CompTech) were mixed with 1× PBS and an equal volume of 2× SDS sample buffer lacking reducing agents and loaded onto a 7.5% SDS-PAGE gel without being boiled. ..

Article Title: Heparan Sulfate, Including that in Bruch's Membrane, Inhibits the Complement Alternative Pathway: Implications for Age-related Macular Degeneration
Article Snippet: .. Human purified complement components C1, C2, C3, C3b, C4 and factors H and I were all obtained from CompTech, Inc (Tyler, TX). .. Sheep erythrocytes in Alsever’s solution were obtained from Lampire Biological Laboratories (Pipersville, PA).

Article Title: Methods for regulating complement cascade proteins using astrovirus coat protein and derivatives thereof
Article Snippet: .. In FIG. 12A, purified complement factors C1, C2, C3 and C4 (Comptech) were mixed with 1×PBS and an equal volume of 2×SDS sample buffer lacking reducing agents and loaded onto a 7.5% SDS-PAGE gel without boiling the samples. ..

SDS Page:

Article Title: Human Astrovirus Coat Protein Inhibits Serum Complement Activation via C1, the First Component of the Classical Pathway
Article Snippet: .. Duplicate aliquots (1 μg) of the purified complement factors C1, C2, C3, and C4 (CompTech) were mixed with 1× PBS and an equal volume of 2× SDS sample buffer lacking reducing agents and loaded onto a 7.5% SDS-PAGE gel without being boiled. ..

Clinical Proteomics:

Article Title: The Protease SplB of Staphylococcus aureus Targets Host Complement Components and Inhibits Complement-Mediated Bacterial Opsonophagocytosis
Article Snippet: .. Human plasma-purified complement proteins C1q, C2, C3, C3b, C4, C4b, C5, C5b, C6, C7, C8, and C9; factor H; and C4BP were purchased from CompTech (Complement Technology Inc.) (Tyler, TX, USA). .. Goat antisera against human C1q, C2, C3, C4, C5, C6, C7, C8, C9, and factor H were procured from CompTech (Tyler, TX, USA).

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