complement protein c8 Search Results


purified human c7, c8, c9 proteins  (Complement Technology Inc)
90
Complement Technology Inc purified human c7, c8, c9 proteins
Overexpression of mortalin reduces the amount of bound C5b-9 on the cell surface. K562 cells, 48 h after transfection with a mortalin-EGFP plasmid, were treated with anti-K562 antibodies and then <t>with</t> <t>C9D-NHS</t> supplemented with <t>C9-AF555</t> for 10 min at 37 °C. Next, the cells were washed and observed under a confocal microscope, and 30 randomly selected cell images were taken. A, a representative image is shown. Levels of C9-AF555 bound to the cell surface (representing C5b-9) and of mortalin-EGFP in the cell images were quantified by densitometry and analyzed with ImageJ. B, regression analysis for estimating the relationship between C9 deposition and the level of mortalin is shown. A.U., arbitrary units. C, levels of C9 deposition in cells having low (0–5 A.U.) or high (>5 A.U.) mortalin-EGFP level are shown. *, p < 0.005. Error bars, S.D.
Purified Human C7, C8, C9 Proteins, supplied by Complement Technology 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/result/purified human c7, c8, c9 proteins/product/Complement Technology Inc
Average 90 stars, based on 1 article reviews
purified human c7, c8, c9 proteins - by Bioz Stars, 2026-05
90/100 stars
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nhs depleted of complement protein c8  (Quidel)
90
Quidel nhs depleted of complement protein c8
Overexpression of mortalin reduces the amount of bound C5b-9 on the cell surface. K562 cells, 48 h after transfection with a mortalin-EGFP plasmid, were treated with anti-K562 antibodies and then <t>with</t> <t>C9D-NHS</t> supplemented with <t>C9-AF555</t> for 10 min at 37 °C. Next, the cells were washed and observed under a confocal microscope, and 30 randomly selected cell images were taken. A, a representative image is shown. Levels of C9-AF555 bound to the cell surface (representing C5b-9) and of mortalin-EGFP in the cell images were quantified by densitometry and analyzed with ImageJ. B, regression analysis for estimating the relationship between C9 deposition and the level of mortalin is shown. A.U., arbitrary units. C, levels of C9 deposition in cells having low (0–5 A.U.) or high (>5 A.U.) mortalin-EGFP level are shown. *, p < 0.005. Error bars, S.D.
Nhs Depleted Of Complement Protein C8, supplied by Quidel, 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/result/nhs depleted of complement protein c8/product/Quidel
Average 90 stars, based on 1 article reviews
nhs depleted of complement protein c8 - by Bioz Stars, 2026-05
90/100 stars
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recombinant human complement component c8 gamma chain/c8g protein  (Elabscience Biotechnology)
N/A
Complement component C8 is a constituent of the membrane attack complex, C8 alpha, C8 beta and C8G. C8G is a secreted protein and comsists a disulfide-linked C8 alpha-gamma heterodimer and a non-covalently associated C8 beta
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complement c8 gamma protein, human, recombinant  (TargetMol)
N/A
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recombinant human complement component c8 gamma chain c8g protein  (Elabscience)
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human complement component c8 gamma recombinant protein n-6 his tag  (Innovative Research Inc)
N/A
Human Complement component C8 gamma Recombinant Protein N-6 His Tag from Innovative Research has been recombinantly produced in E. coli. This is a Liquid protein buffered in Supplied as a 0.2 um filtered solution of
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complement component c8 gamma recombinant protein  (ProSci Incorporated)
N/A
Human Complement component C8 gamma Recombinant Protein made in E. coli with N-6 His tag.
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Image Search Results


Overexpression of mortalin reduces the amount of bound C5b-9 on the cell surface. K562 cells, 48 h after transfection with a mortalin-EGFP plasmid, were treated with anti-K562 antibodies and then with C9D-NHS supplemented with C9-AF555 for 10 min at 37 °C. Next, the cells were washed and observed under a confocal microscope, and 30 randomly selected cell images were taken. A, a representative image is shown. Levels of C9-AF555 bound to the cell surface (representing C5b-9) and of mortalin-EGFP in the cell images were quantified by densitometry and analyzed with ImageJ. B, regression analysis for estimating the relationship between C9 deposition and the level of mortalin is shown. A.U., arbitrary units. C, levels of C9 deposition in cells having low (0–5 A.U.) or high (>5 A.U.) mortalin-EGFP level are shown. *, p < 0.005. Error bars, S.D.

Journal: The Journal of Biological Chemistry

Article Title: Mortalin/GRP75 Binds to Complement C9 and Plays a Role in Resistance to Complement-dependent Cytotoxicity *

doi: 10.1074/jbc.M114.552406

Figure Lengend Snippet: Overexpression of mortalin reduces the amount of bound C5b-9 on the cell surface. K562 cells, 48 h after transfection with a mortalin-EGFP plasmid, were treated with anti-K562 antibodies and then with C9D-NHS supplemented with C9-AF555 for 10 min at 37 °C. Next, the cells were washed and observed under a confocal microscope, and 30 randomly selected cell images were taken. A, a representative image is shown. Levels of C9-AF555 bound to the cell surface (representing C5b-9) and of mortalin-EGFP in the cell images were quantified by densitometry and analyzed with ImageJ. B, regression analysis for estimating the relationship between C9 deposition and the level of mortalin is shown. A.U., arbitrary units. C, levels of C9 deposition in cells having low (0–5 A.U.) or high (>5 A.U.) mortalin-EGFP level are shown. *, p < 0.005. Error bars, S.D.

Article Snippet: Heat inactivation of NHS (HIS) was performed at 56 °C for 30 min. Purified human C7, C8, and C9 proteins and complement C9-depleted human serum (C9D-NHS) were purchased from Complement Technology Inc. (Tyler, TX).

Techniques: Over Expression, Transfection, Plasmid Preparation, Microscopy

Mortalin inhibition by siRNA increases the amount of cell bound C9. K562 cells were transfected with specific siRNA directed to mortalin. Cells treated with nonspecific control siRNA (NS) or without siRNA (NT) were used as control. A, 48 h after transfection, the cells were lysed with sample buffer and analyzed by SDS-PAGE and Western blotting with anti-mortalin or anti-actin antibodies. K562 cells transfected with mortalin-siRNA were treated, 48 h after transfection, with anti-K562 antibodies and then with C9D-NHS supplemented with C9-AF488 for 10 min at 37 °C. B, next, the cells were washed, fixed, permeabilized, and labeled with anti-mortalin antibody and a secondary Cy3-labeled antibody. The cells were observed under a confocal microscope. C, levels of C9-AF488 on the cell surface and of mortalin-Cy3 were quantified by densitometry and analyzed with ImageJ in 30 randomly selected cell images. The level of C9-AF488 in cells having low (0–5 arbitrary units (A.U.)) and high (>5 arbitrary units) mortalin-Cy3 is shown. *, p < 0.005. Error bars, S.D.

Journal: The Journal of Biological Chemistry

Article Title: Mortalin/GRP75 Binds to Complement C9 and Plays a Role in Resistance to Complement-dependent Cytotoxicity *

doi: 10.1074/jbc.M114.552406

Figure Lengend Snippet: Mortalin inhibition by siRNA increases the amount of cell bound C9. K562 cells were transfected with specific siRNA directed to mortalin. Cells treated with nonspecific control siRNA (NS) or without siRNA (NT) were used as control. A, 48 h after transfection, the cells were lysed with sample buffer and analyzed by SDS-PAGE and Western blotting with anti-mortalin or anti-actin antibodies. K562 cells transfected with mortalin-siRNA were treated, 48 h after transfection, with anti-K562 antibodies and then with C9D-NHS supplemented with C9-AF488 for 10 min at 37 °C. B, next, the cells were washed, fixed, permeabilized, and labeled with anti-mortalin antibody and a secondary Cy3-labeled antibody. The cells were observed under a confocal microscope. C, levels of C9-AF488 on the cell surface and of mortalin-Cy3 were quantified by densitometry and analyzed with ImageJ in 30 randomly selected cell images. The level of C9-AF488 in cells having low (0–5 arbitrary units (A.U.)) and high (>5 arbitrary units) mortalin-Cy3 is shown. *, p < 0.005. Error bars, S.D.

Article Snippet: Heat inactivation of NHS (HIS) was performed at 56 °C for 30 min. Purified human C7, C8, and C9 proteins and complement C9-depleted human serum (C9D-NHS) were purchased from Complement Technology Inc. (Tyler, TX).

Techniques: Inhibition, Transfection, SDS Page, Western Blot, Labeling, Microscopy

C9 binds to the ATPase domain of mortalin-ELISA. A, C9, C8, and C7 adsorbed onto microtiter plate wells were incubated with His-tagged recombinant full-length mortalin, SBD, or ATPase domain. The wells were washed, treated with anti-His antibody, and peroxidase-labeled second antibody, developed with OPD and analyzed in an ELISA reader. *, p < 0.005; **, p < 0.001 between ATPase domain and SBD. Error bars, S.D. B, microtiter plate wells were coated with C9 overnight at 4 °C. His-tagged mortalin or its domains were preincubated with C8 or C9 (0.25 μm, C81 and C91 or 0.5 μm, C82 and C92) for 1 h at 37 °C. The mixtures were then added to the C9-coated wells. Binding of His-tagged mortalin and its domains was quantified with anti-His antibody as in A. *, p < 0.05; **, p < 0.005; ***, p < 0.001 relative to control (− competitor).

Journal: The Journal of Biological Chemistry

Article Title: Mortalin/GRP75 Binds to Complement C9 and Plays a Role in Resistance to Complement-dependent Cytotoxicity *

doi: 10.1074/jbc.M114.552406

Figure Lengend Snippet: C9 binds to the ATPase domain of mortalin-ELISA. A, C9, C8, and C7 adsorbed onto microtiter plate wells were incubated with His-tagged recombinant full-length mortalin, SBD, or ATPase domain. The wells were washed, treated with anti-His antibody, and peroxidase-labeled second antibody, developed with OPD and analyzed in an ELISA reader. *, p < 0.005; **, p < 0.001 between ATPase domain and SBD. Error bars, S.D. B, microtiter plate wells were coated with C9 overnight at 4 °C. His-tagged mortalin or its domains were preincubated with C8 or C9 (0.25 μm, C81 and C91 or 0.5 μm, C82 and C92) for 1 h at 37 °C. The mixtures were then added to the C9-coated wells. Binding of His-tagged mortalin and its domains was quantified with anti-His antibody as in A. *, p < 0.05; **, p < 0.005; ***, p < 0.001 relative to control (− competitor).

Article Snippet: Heat inactivation of NHS (HIS) was performed at 56 °C for 30 min. Purified human C7, C8, and C9 proteins and complement C9-depleted human serum (C9D-NHS) were purchased from Complement Technology Inc. (Tyler, TX).

Techniques: Enzyme-linked Immunosorbent Assay, Incubation, Recombinant, Labeling, Binding Assay