complement factors c1, c2, c3 and c4 Search Results


complement proteins c1q, c2, c3, c3b, c4, c4b, c5, c5b, c6, c7, c8, c9  (CompTech Computer Technologies)
90
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+factors+c1%2C+c2%2C+c3+and+c4/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, 2026-09
90/100 stars
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capacitance sensors c1, c2, c3, and c4  (VSense Inc)
90
VSense Inc capacitance sensors c1, c2, c3, and c4
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).
Capacitance Sensors C1, C2, C3, And C4, supplied by VSense Inc, 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+factors+c1%2C+c2%2C+c3+and+c4/capacitance+sensors+c1++c2++c3++and+c4/us09741375-221-9-33
Average 90 stars, based on 1 article reviews
capacitance sensors c1, c2, c3, and c4 - by Bioz Stars, 2026-09
90/100 stars
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complement components c2, c3, c5, and  (MBL Life science)
90
MBL Life science complement components c2, c3, c5, and
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 Components C2, C3, C5, And, supplied by MBL Life science, 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+factors+c1%2C+c2%2C+c3+and+c4/complement+factors+c2++c3++c4++c5++c9++c1+inhibitor++c4+binding+protein++mannose+binding+lectin/pm35740382-123-16-22
Average 90 stars, based on 1 article reviews
complement components c2, c3, c5, and - by Bioz Stars, 2026-09
90/100 stars
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bm-moricina1, gm-mlpa, b, c1, c2, c3, c4, d and an (residues 1–28 of gm-mlpa)  (Auspep Pty)
90
Auspep Pty bm-moricina1, gm-mlpa, b, c1, c2, c3, c4, d and an (residues 1–28 of gm-mlpa)
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).
Bm Moricina1, Gm Mlpa, B, C1, C2, C3, C4, D And An (Residues 1–28 Of Gm Mlpa), supplied by Auspep Pty, 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+factors+c1%2C+c2%2C+c3+and+c4/bm+moricina1++gm+mlpa++b++c1++c2++c3++c4++d+and+an++residues+1+28+of+gm+mlpa+/pm18207081-84-13-17
Average 90 stars, based on 1 article reviews
bm-moricina1, gm-mlpa, b, c1, c2, c3, c4, d and an (residues 1–28 of gm-mlpa) - by Bioz Stars, 2026-09
90/100 stars
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palmitic acid 13c c1 c2 c3 and c4  (Cayman Chemical)
N/A
Palmitic Acid 13C C1 C2 C3 and C4 labeled
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Image Search Results


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).

Journal: Journal of Bacteriology

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

doi: 10.1128/JB.00184-21

Figure Lengend 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).

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).

Techniques: 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.

Journal: Journal of Bacteriology

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

doi: 10.1128/JB.00184-21

Figure Lengend 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.

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).

Techniques: 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.

Journal: Journal of Bacteriology

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

doi: 10.1128/JB.00184-21

Figure Lengend 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.

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).

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