human terminal complement complex tcc  (Hycult Biotech)


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    Hycult Biotech human terminal complement complex tcc
    Human Terminal Complement Complex Tcc, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    human terminal complement complex tcc  (Hycult Biotech)


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    Hycult Biotech human terminal complement complex tcc
    Human Terminal Complement Complex Tcc, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    human terminal complement complex tcc elisa kit  (Hycult Biotech)


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    Hycult Biotech human terminal complement complex tcc elisa kit
    Human Terminal Complement Complex Tcc Elisa Kit, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    human terminal complement complex tcc  (Hycult Biotech)


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    Hycult Biotech human terminal complement complex tcc
    Evaluation of complement and coagulation proteins and responses on/to alginate microspheres. Detection of complement (C1q, C3c) and coagulation proteins (FXII) in human plasma by CLSM ( A-D ) and activation in human whole blood <t>by</t> <t>terminal</t> complement complex <t>(TCC)</t> and prothrombin fragment 1 ​+ ​2 (PTF1.2) ( E, F ). CLSM images show antibody-stained alginate microspheres HiG, SA, and AP after incubation (24 h) in lepirudin-anticoagulated human plasma. Microspheres were FITC-stained ( green ) against complement C1q ( A ) and C3c ( B ) and CF633-stained ( red ) against coagulation FXII ( C ), and non-specific antibody binding was assessed ( D ). Captured images include brightfield (BF), equatorial (2D)-sections and (3D)-projections of z-stacked images. Scale bar: 200 ​μm. Activation of complement by TCC-induction ( E ) and coagulation by PTF1.2 formation ( F ) was assessed after incubation (4 h) in lepirudin-anticoagulated human whole blood. Controls measured (median ​± ​SEM), but not shown, included positive control for PTF1.2 (glass): 759 ​954 ​± ​197 ​581 ​pmol/L, and saline control: 12.9 ​± ​5.2 AU/mL (TCC) and 401 ​± ​169 ​pmol/L (PTF1.2). Data are expressed in box plots with values from five donors. Significant values are given as p ​≤ ​0.05 (∗), p ​≤ ​0.01 (∗∗), p ​≤ ​0.001 (∗∗∗) between indicated sample groups. T0 represents the experimental baseline. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
    Human Terminal Complement Complex Tcc, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "MS-proteomics provides insight into the host responses towards alginate microspheres"

    Article Title: MS-proteomics provides insight into the host responses towards alginate microspheres

    Journal: Materials Today Bio

    doi: 10.1016/j.mtbio.2022.100490

    Evaluation of complement and coagulation proteins and responses on/to alginate microspheres. Detection of complement (C1q, C3c) and coagulation proteins (FXII) in human plasma by CLSM ( A-D ) and activation in human whole blood by terminal complement complex (TCC) and prothrombin fragment 1 ​+ ​2 (PTF1.2) ( E, F ). CLSM images show antibody-stained alginate microspheres HiG, SA, and AP after incubation (24 h) in lepirudin-anticoagulated human plasma. Microspheres were FITC-stained ( green ) against complement C1q ( A ) and C3c ( B ) and CF633-stained ( red ) against coagulation FXII ( C ), and non-specific antibody binding was assessed ( D ). Captured images include brightfield (BF), equatorial (2D)-sections and (3D)-projections of z-stacked images. Scale bar: 200 ​μm. Activation of complement by TCC-induction ( E ) and coagulation by PTF1.2 formation ( F ) was assessed after incubation (4 h) in lepirudin-anticoagulated human whole blood. Controls measured (median ​± ​SEM), but not shown, included positive control for PTF1.2 (glass): 759 ​954 ​± ​197 ​581 ​pmol/L, and saline control: 12.9 ​± ​5.2 AU/mL (TCC) and 401 ​± ​169 ​pmol/L (PTF1.2). Data are expressed in box plots with values from five donors. Significant values are given as p ​≤ ​0.05 (∗), p ​≤ ​0.01 (∗∗), p ​≤ ​0.001 (∗∗∗) between indicated sample groups. T0 represents the experimental baseline. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)
    Figure Legend Snippet: Evaluation of complement and coagulation proteins and responses on/to alginate microspheres. Detection of complement (C1q, C3c) and coagulation proteins (FXII) in human plasma by CLSM ( A-D ) and activation in human whole blood by terminal complement complex (TCC) and prothrombin fragment 1 ​+ ​2 (PTF1.2) ( E, F ). CLSM images show antibody-stained alginate microspheres HiG, SA, and AP after incubation (24 h) in lepirudin-anticoagulated human plasma. Microspheres were FITC-stained ( green ) against complement C1q ( A ) and C3c ( B ) and CF633-stained ( red ) against coagulation FXII ( C ), and non-specific antibody binding was assessed ( D ). Captured images include brightfield (BF), equatorial (2D)-sections and (3D)-projections of z-stacked images. Scale bar: 200 ​μm. Activation of complement by TCC-induction ( E ) and coagulation by PTF1.2 formation ( F ) was assessed after incubation (4 h) in lepirudin-anticoagulated human whole blood. Controls measured (median ​± ​SEM), but not shown, included positive control for PTF1.2 (glass): 759 ​954 ​± ​197 ​581 ​pmol/L, and saline control: 12.9 ​± ​5.2 AU/mL (TCC) and 401 ​± ​169 ​pmol/L (PTF1.2). Data are expressed in box plots with values from five donors. Significant values are given as p ​≤ ​0.05 (∗), p ​≤ ​0.01 (∗∗), p ​≤ ​0.001 (∗∗∗) between indicated sample groups. T0 represents the experimental baseline. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

    Techniques Used: Coagulation, Activation Assay, Staining, Incubation, Binding Assay, Positive Control

    Proposed mechanisms of complement and coagulation responses on the alginate microspheres based on proteomic and CLSM analyses as well as functional data from human whole blood (hWB). The complement and coagulation systems are interconnected protein defence systems , consisting of sequential activation of zymogens to active proteinases during inflammatory responses. The complement system is activated by three distinct pathways: classical, lectin and alternative, which have been thoroughly described elsewhere [ , ]. HiG and SA are significantly enriched with proteins of both the classical (e.g. C1q and APCS) and lectin pathways (MBL/collectins/ficolins), which may suggest an initial complement activation. However, low levels of C3 indicate a prompt attenuation of this potential complement response through initial regulators. SA is unique in the high abundance of adsorbed complement inhibitors (C1IN, CFH, CFI, C4BP, CPN, CLU, VTN). HiG is enriched with fewer inhibitors (C1IN, CFH, CFI, CLU) and to a lesser extent. HiG, and especially SA, exhibit low terminal complement activity (fluid-phase TCC; sTCC) in hWB, despite being enriched with proteins involved in TCC formation, which suggest inactivation of TCC or adsorption of non-assembled TCC-components. AP displays pronounced enrichment of CFP and C3, indicating complement initiation and propagation through the alternative pathway. Moreover, enrichment of prothrombin/thrombin (FII [a]) and plasminogen/plasmin (PLG) also present the additional possibility of a complement-independent activation of C3 and C5. AP is distinct in the absence or low levels of initial complement inhibitors. This is in accordance with a persisting complement response and subsequent terminal complement activity, shown for these microspheres by the high levels of adsorbed proteins involved in TCC formation and the significant TCC response in hWB. The coagulation system is activated through two mechanisms: the extrinsic (tissue factor) pathway (not discussed here) and the intrinsic (contact activation) pathway, which has been described elsewhere [ , , , ]. All the microspheres activate coagulation to some extent, as seen by the functional hWB data. SA has an overall moderate coagulation reactivity but the highest coagulation (prothrombin fragment 1 ​+ ​2) response among the microspheres. Being highly enriched with proteins of the intrinsic pathway, such as FXII, suggests coagulation activation through the contact system. SA is also enriched with numerous coagulation inhibitors (AT3, HCF2, C1IN, PROC, ZPI), which likely diminishes this activation. HiG shares a similar coagulation profile to SA in types of enriched proteins, although at significantly lower abundances and with some variation in adsorbed inhibitors (i.e. PROC, TFPI). Distinctively, AP is enriched with all the contact system proteins, except for C1IN, which potentially allows for pro-inflammatory signalling by BK. Further enrichments include several coagulation inhibitors (AT3, HCF2, PROC, ZPI, TFPI). AP shows the highest enrichment of FII(a) yet distinctively lacks central proteins (FX, FV) of the intrinsic pathway. Hence, the observed coagulation reactivity in hWB indicates tissue factor-dependent initiation , closely linked to complement activation.
    Figure Legend Snippet: Proposed mechanisms of complement and coagulation responses on the alginate microspheres based on proteomic and CLSM analyses as well as functional data from human whole blood (hWB). The complement and coagulation systems are interconnected protein defence systems , consisting of sequential activation of zymogens to active proteinases during inflammatory responses. The complement system is activated by three distinct pathways: classical, lectin and alternative, which have been thoroughly described elsewhere [ , ]. HiG and SA are significantly enriched with proteins of both the classical (e.g. C1q and APCS) and lectin pathways (MBL/collectins/ficolins), which may suggest an initial complement activation. However, low levels of C3 indicate a prompt attenuation of this potential complement response through initial regulators. SA is unique in the high abundance of adsorbed complement inhibitors (C1IN, CFH, CFI, C4BP, CPN, CLU, VTN). HiG is enriched with fewer inhibitors (C1IN, CFH, CFI, CLU) and to a lesser extent. HiG, and especially SA, exhibit low terminal complement activity (fluid-phase TCC; sTCC) in hWB, despite being enriched with proteins involved in TCC formation, which suggest inactivation of TCC or adsorption of non-assembled TCC-components. AP displays pronounced enrichment of CFP and C3, indicating complement initiation and propagation through the alternative pathway. Moreover, enrichment of prothrombin/thrombin (FII [a]) and plasminogen/plasmin (PLG) also present the additional possibility of a complement-independent activation of C3 and C5. AP is distinct in the absence or low levels of initial complement inhibitors. This is in accordance with a persisting complement response and subsequent terminal complement activity, shown for these microspheres by the high levels of adsorbed proteins involved in TCC formation and the significant TCC response in hWB. The coagulation system is activated through two mechanisms: the extrinsic (tissue factor) pathway (not discussed here) and the intrinsic (contact activation) pathway, which has been described elsewhere [ , , , ]. All the microspheres activate coagulation to some extent, as seen by the functional hWB data. SA has an overall moderate coagulation reactivity but the highest coagulation (prothrombin fragment 1 ​+ ​2) response among the microspheres. Being highly enriched with proteins of the intrinsic pathway, such as FXII, suggests coagulation activation through the contact system. SA is also enriched with numerous coagulation inhibitors (AT3, HCF2, C1IN, PROC, ZPI), which likely diminishes this activation. HiG shares a similar coagulation profile to SA in types of enriched proteins, although at significantly lower abundances and with some variation in adsorbed inhibitors (i.e. PROC, TFPI). Distinctively, AP is enriched with all the contact system proteins, except for C1IN, which potentially allows for pro-inflammatory signalling by BK. Further enrichments include several coagulation inhibitors (AT3, HCF2, PROC, ZPI, TFPI). AP shows the highest enrichment of FII(a) yet distinctively lacks central proteins (FX, FV) of the intrinsic pathway. Hence, the observed coagulation reactivity in hWB indicates tissue factor-dependent initiation , closely linked to complement activation.

    Techniques Used: Coagulation, Functional Assay, Activation Assay, Activity Assay, Adsorption

    complement terminal complex tcc  (Hycult Biotech)


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    Hycult Biotech complement terminal complex tcc
    Complement Terminal Complex Tcc, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    complement terminal complex tcc  (Hycult Biotech)


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    Hycult Biotech complement terminal complex tcc
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    human terminal complement complex elisa kit  (Hycult Biotech)


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    Hycult Biotech human terminal complement complex elisa kit
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    human terminal complement complex specific mab ae11  (Hycult Biotech)


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    Hycult Biotech human terminal complement complex specific mab ae11
    Surface plasmon resonance analysis of polymerization. Preparations of C9 were polished by size exchange chromatography to remove aggregates and flowed slowly (5 μl/min) at 37°C across a Biacore chip that had been immobilized with <t>aE11</t> mAb specific for polymerized C9. Polymers of C9 formed by WT and P167S C9 were captured on the antibody. Solid line represents poly-C9 captured from the preparation of mutant P167S C9 and dashed line represents capture of poly-C9 in the WT preparation. The experiment was performed multiple times with different preparations of C9; a representative analysis is illustrated.
    Human Terminal Complement Complex Specific Mab Ae11, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "The rare C9 P167S risk variant for age-related macular degeneration increases polymerization of the terminal component of the complement cascade"

    Article Title: The rare C9 P167S risk variant for age-related macular degeneration increases polymerization of the terminal component of the complement cascade

    Journal: Human Molecular Genetics

    doi: 10.1093/hmg/ddab086

    Surface plasmon resonance analysis of polymerization. Preparations of C9 were polished by size exchange chromatography to remove aggregates and flowed slowly (5 μl/min) at 37°C across a Biacore chip that had been immobilized with aE11 mAb specific for polymerized C9. Polymers of C9 formed by WT and P167S C9 were captured on the antibody. Solid line represents poly-C9 captured from the preparation of mutant P167S C9 and dashed line represents capture of poly-C9 in the WT preparation. The experiment was performed multiple times with different preparations of C9; a representative analysis is illustrated.
    Figure Legend Snippet: Surface plasmon resonance analysis of polymerization. Preparations of C9 were polished by size exchange chromatography to remove aggregates and flowed slowly (5 μl/min) at 37°C across a Biacore chip that had been immobilized with aE11 mAb specific for polymerized C9. Polymers of C9 formed by WT and P167S C9 were captured on the antibody. Solid line represents poly-C9 captured from the preparation of mutant P167S C9 and dashed line represents capture of poly-C9 in the WT preparation. The experiment was performed multiple times with different preparations of C9; a representative analysis is illustrated.

    Techniques Used: SPR Assay, Chromatography, Mutagenesis

    complement terminal complex tcc  (Hycult Biotech)


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    Hycult Biotech complement terminal complex tcc
    Complement Terminal Complex Tcc, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    human terminal complement complex elisa kit  (Hycult Biotech)


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    Hycult Biotech human terminal complement complex elisa kit
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    mouse anti human terminal complement complex tcc abs  (Hycult Biotech)


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    Hycult Biotech mouse anti human terminal complement complex tcc abs
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    Hycult Biotech human terminal complement complex tcc
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    Hycult Biotech human terminal complement complex tcc elisa kit
    Human Terminal Complement Complex Tcc Elisa Kit, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Hycult Biotech complement terminal complex tcc
    Complement Terminal Complex Tcc, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Human Terminal Complement Complex Elisa Kit, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Hycult Biotech human terminal complement complex specific mab ae11
    Surface plasmon resonance analysis of polymerization. Preparations of C9 were polished by size exchange chromatography to remove aggregates and flowed slowly (5 μl/min) at 37°C across a Biacore chip that had been immobilized with <t>aE11</t> mAb specific for polymerized C9. Polymers of C9 formed by WT and P167S C9 were captured on the antibody. Solid line represents poly-C9 captured from the preparation of mutant P167S C9 and dashed line represents capture of poly-C9 in the WT preparation. The experiment was performed multiple times with different preparations of C9; a representative analysis is illustrated.
    Human Terminal Complement Complex Specific Mab Ae11, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Hycult Biotech mouse anti human terminal complement complex tcc abs
    Surface plasmon resonance analysis of polymerization. Preparations of C9 were polished by size exchange chromatography to remove aggregates and flowed slowly (5 μl/min) at 37°C across a Biacore chip that had been immobilized with <t>aE11</t> mAb specific for polymerized C9. Polymers of C9 formed by WT and P167S C9 were captured on the antibody. Solid line represents poly-C9 captured from the preparation of mutant P167S C9 and dashed line represents capture of poly-C9 in the WT preparation. The experiment was performed multiple times with different preparations of C9; a representative analysis is illustrated.
    Mouse Anti Human Terminal Complement Complex Tcc Abs, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Surface plasmon resonance analysis of polymerization. Preparations of C9 were polished by size exchange chromatography to remove aggregates and flowed slowly (5 μl/min) at 37°C across a Biacore chip that had been immobilized with aE11 mAb specific for polymerized C9. Polymers of C9 formed by WT and P167S C9 were captured on the antibody. Solid line represents poly-C9 captured from the preparation of mutant P167S C9 and dashed line represents capture of poly-C9 in the WT preparation. The experiment was performed multiple times with different preparations of C9; a representative analysis is illustrated.

    Journal: Human Molecular Genetics

    Article Title: The rare C9 P167S risk variant for age-related macular degeneration increases polymerization of the terminal component of the complement cascade

    doi: 10.1093/hmg/ddab086

    Figure Lengend Snippet: Surface plasmon resonance analysis of polymerization. Preparations of C9 were polished by size exchange chromatography to remove aggregates and flowed slowly (5 μl/min) at 37°C across a Biacore chip that had been immobilized with aE11 mAb specific for polymerized C9. Polymers of C9 formed by WT and P167S C9 were captured on the antibody. Solid line represents poly-C9 captured from the preparation of mutant P167S C9 and dashed line represents capture of poly-C9 in the WT preparation. The experiment was performed multiple times with different preparations of C9; a representative analysis is illustrated.

    Article Snippet: Flat-bottomed 96-well plates (Maxisorp, ThermoFisher) were coated with 0.5 μg/ml human terminal complement complex-specific mAb aE11 (Hycult, HM2167, Uden, The Netherlands) in 200 m m bicarbonate/carbonate buffer pH 9.6 and incubated overnight at 4°C.

    Techniques: SPR Assay, Chromatography, Mutagenesis