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Mirus Bio freestyle cho cells
(a) ELISA was used to measure the target-binding activity of anti-EGFR and anti-EpCAM IgA antibodies derived from the supernatants of transfected <t>CHO-S</t> cells. Recombinant IgA and IgG antibodies were used as positive controls (ctrl: 0.1 nM), and supernatants from mock-transfected cells served as negative controls. Binding specificity was confirmed by assessing the binding of each IgA antibody to its intended target (EGFR or EpCAM) and to the non-target protein. (b) Western blot analysis of anti-EGFR and anti-EpCAM IgA antibodies in the supernatant of transfected CHO-S cells (lane 1,3). Purified recombinant IgA antibodies were used as controls (lane 2,4). Note that the anti-EGFR IgA control shows incomplete antibody assembly. HC, heavy chain; LC, light chain. (c) Western blot analysis of dimeric IgA antibodies under non-reducing conditions, showing the presence of both the IgA heavy chain (HC), detected by a mouse anti-human kappa chain antibody, and the J-chain (JC), detected by a mouse anti-poly His-tag antibody, in supernatants of CHO-S transiently transfected with the respective expression vectors. 1: anti-EGFR; 2: anti-EpCAM. (d) ELISA was performed to measure SIRPα-Fc protein levels in the supernatant of transfected CHO-S cells, using CD47 as coating. A recombinant anti-CD47 IgG antibody (2.5 nM) was used as a positive control, and supernatant from mock-transfected cells served as a negative control. Wells with no CD47 coating served as additional controls. (e) Western blot analysis of the SIRPα-Fc protein, as detected by a mouse anti-γ heavy chain, in supernatants of CHO-S cells transiently transfected with the respective expression vector, under reducing (red.) and non-reducing (non-red.) conditions. (a-e): representative images from at least three independent experiments are shown.
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Beijing Wantai Biological hbsag in vitro cho ly75 expressing dec 205 cells
(a) ELISA was used to measure the target-binding activity of anti-EGFR and anti-EpCAM IgA antibodies derived from the supernatants of transfected <t>CHO-S</t> cells. Recombinant IgA and IgG antibodies were used as positive controls (ctrl: 0.1 nM), and supernatants from mock-transfected cells served as negative controls. Binding specificity was confirmed by assessing the binding of each IgA antibody to its intended target (EGFR or EpCAM) and to the non-target protein. (b) Western blot analysis of anti-EGFR and anti-EpCAM IgA antibodies in the supernatant of transfected CHO-S cells (lane 1,3). Purified recombinant IgA antibodies were used as controls (lane 2,4). Note that the anti-EGFR IgA control shows incomplete antibody assembly. HC, heavy chain; LC, light chain. (c) Western blot analysis of dimeric IgA antibodies under non-reducing conditions, showing the presence of both the IgA heavy chain (HC), detected by a mouse anti-human kappa chain antibody, and the J-chain (JC), detected by a mouse anti-poly His-tag antibody, in supernatants of CHO-S transiently transfected with the respective expression vectors. 1: anti-EGFR; 2: anti-EpCAM. (d) ELISA was performed to measure SIRPα-Fc protein levels in the supernatant of transfected CHO-S cells, using CD47 as coating. A recombinant anti-CD47 IgG antibody (2.5 nM) was used as a positive control, and supernatant from mock-transfected cells served as a negative control. Wells with no CD47 coating served as additional controls. (e) Western blot analysis of the SIRPα-Fc protein, as detected by a mouse anti-γ heavy chain, in supernatants of CHO-S cells transiently transfected with the respective expression vector, under reducing (red.) and non-reducing (non-red.) conditions. (a-e): representative images from at least three independent experiments are shown.
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DSMZ culture cat acc110 cho k1 at2b2 4 cho cells stably expressing cav2 2 channels cell lines were not authenticated
(a) ELISA was used to measure the target-binding activity of anti-EGFR and anti-EpCAM IgA antibodies derived from the supernatants of transfected <t>CHO-S</t> cells. Recombinant IgA and IgG antibodies were used as positive controls (ctrl: 0.1 nM), and supernatants from mock-transfected cells served as negative controls. Binding specificity was confirmed by assessing the binding of each IgA antibody to its intended target (EGFR or EpCAM) and to the non-target protein. (b) Western blot analysis of anti-EGFR and anti-EpCAM IgA antibodies in the supernatant of transfected CHO-S cells (lane 1,3). Purified recombinant IgA antibodies were used as controls (lane 2,4). Note that the anti-EGFR IgA control shows incomplete antibody assembly. HC, heavy chain; LC, light chain. (c) Western blot analysis of dimeric IgA antibodies under non-reducing conditions, showing the presence of both the IgA heavy chain (HC), detected by a mouse anti-human kappa chain antibody, and the J-chain (JC), detected by a mouse anti-poly His-tag antibody, in supernatants of CHO-S transiently transfected with the respective expression vectors. 1: anti-EGFR; 2: anti-EpCAM. (d) ELISA was performed to measure SIRPα-Fc protein levels in the supernatant of transfected CHO-S cells, using CD47 as coating. A recombinant anti-CD47 IgG antibody (2.5 nM) was used as a positive control, and supernatant from mock-transfected cells served as a negative control. Wells with no CD47 coating served as additional controls. (e) Western blot analysis of the SIRPα-Fc protein, as detected by a mouse anti-γ heavy chain, in supernatants of CHO-S cells transiently transfected with the respective expression vector, under reducing (red.) and non-reducing (non-red.) conditions. (a-e): representative images from at least three independent experiments are shown.
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Greiner Bio pathhunter express glp1r discover x 93 0300e2cp0m cho k1 β arrestin gpcr greiner 781098 assay kit 384
(a) ELISA was used to measure the target-binding activity of anti-EGFR and anti-EpCAM IgA antibodies derived from the supernatants of transfected <t>CHO-S</t> cells. Recombinant IgA and IgG antibodies were used as positive controls (ctrl: 0.1 nM), and supernatants from mock-transfected cells served as negative controls. Binding specificity was confirmed by assessing the binding of each IgA antibody to its intended target (EGFR or EpCAM) and to the non-target protein. (b) Western blot analysis of anti-EGFR and anti-EpCAM IgA antibodies in the supernatant of transfected CHO-S cells (lane 1,3). Purified recombinant IgA antibodies were used as controls (lane 2,4). Note that the anti-EGFR IgA control shows incomplete antibody assembly. HC, heavy chain; LC, light chain. (c) Western blot analysis of dimeric IgA antibodies under non-reducing conditions, showing the presence of both the IgA heavy chain (HC), detected by a mouse anti-human kappa chain antibody, and the J-chain (JC), detected by a mouse anti-poly His-tag antibody, in supernatants of CHO-S transiently transfected with the respective expression vectors. 1: anti-EGFR; 2: anti-EpCAM. (d) ELISA was performed to measure SIRPα-Fc protein levels in the supernatant of transfected CHO-S cells, using CD47 as coating. A recombinant anti-CD47 IgG antibody (2.5 nM) was used as a positive control, and supernatant from mock-transfected cells served as a negative control. Wells with no CD47 coating served as additional controls. (e) Western blot analysis of the SIRPα-Fc protein, as detected by a mouse anti-γ heavy chain, in supernatants of CHO-S cells transiently transfected with the respective expression vector, under reducing (red.) and non-reducing (non-red.) conditions. (a-e): representative images from at least three independent experiments are shown.
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Eurofins cho-k1 cell lines stably expressing either human pac1, vpac1 or vpac2 receptors
(a) ELISA was used to measure the target-binding activity of anti-EGFR and anti-EpCAM IgA antibodies derived from the supernatants of transfected <t>CHO-S</t> cells. Recombinant IgA and IgG antibodies were used as positive controls (ctrl: 0.1 nM), and supernatants from mock-transfected cells served as negative controls. Binding specificity was confirmed by assessing the binding of each IgA antibody to its intended target (EGFR or EpCAM) and to the non-target protein. (b) Western blot analysis of anti-EGFR and anti-EpCAM IgA antibodies in the supernatant of transfected CHO-S cells (lane 1,3). Purified recombinant IgA antibodies were used as controls (lane 2,4). Note that the anti-EGFR IgA control shows incomplete antibody assembly. HC, heavy chain; LC, light chain. (c) Western blot analysis of dimeric IgA antibodies under non-reducing conditions, showing the presence of both the IgA heavy chain (HC), detected by a mouse anti-human kappa chain antibody, and the J-chain (JC), detected by a mouse anti-poly His-tag antibody, in supernatants of CHO-S transiently transfected with the respective expression vectors. 1: anti-EGFR; 2: anti-EpCAM. (d) ELISA was performed to measure SIRPα-Fc protein levels in the supernatant of transfected CHO-S cells, using CD47 as coating. A recombinant anti-CD47 IgG antibody (2.5 nM) was used as a positive control, and supernatant from mock-transfected cells served as a negative control. Wells with no CD47 coating served as additional controls. (e) Western blot analysis of the SIRPα-Fc protein, as detected by a mouse anti-γ heavy chain, in supernatants of CHO-S cells transiently transfected with the respective expression vector, under reducing (red.) and non-reducing (non-red.) conditions. (a-e): representative images from at least three independent experiments are shown.
Cho K1 Cell Lines Stably Expressing Either Human Pac1, Vpac1 Or Vpac2 Receptors, supplied by Eurofins, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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DiscoverX corporation pathhuntertm express hglp-1r cho cells
(a) ELISA was used to measure the target-binding activity of anti-EGFR and anti-EpCAM IgA antibodies derived from the supernatants of transfected <t>CHO-S</t> cells. Recombinant IgA and IgG antibodies were used as positive controls (ctrl: 0.1 nM), and supernatants from mock-transfected cells served as negative controls. Binding specificity was confirmed by assessing the binding of each IgA antibody to its intended target (EGFR or EpCAM) and to the non-target protein. (b) Western blot analysis of anti-EGFR and anti-EpCAM IgA antibodies in the supernatant of transfected CHO-S cells (lane 1,3). Purified recombinant IgA antibodies were used as controls (lane 2,4). Note that the anti-EGFR IgA control shows incomplete antibody assembly. HC, heavy chain; LC, light chain. (c) Western blot analysis of dimeric IgA antibodies under non-reducing conditions, showing the presence of both the IgA heavy chain (HC), detected by a mouse anti-human kappa chain antibody, and the J-chain (JC), detected by a mouse anti-poly His-tag antibody, in supernatants of CHO-S transiently transfected with the respective expression vectors. 1: anti-EGFR; 2: anti-EpCAM. (d) ELISA was performed to measure SIRPα-Fc protein levels in the supernatant of transfected CHO-S cells, using CD47 as coating. A recombinant anti-CD47 IgG antibody (2.5 nM) was used as a positive control, and supernatant from mock-transfected cells served as a negative control. Wells with no CD47 coating served as additional controls. (e) Western blot analysis of the SIRPα-Fc protein, as detected by a mouse anti-γ heavy chain, in supernatants of CHO-S cells transiently transfected with the respective expression vector, under reducing (red.) and non-reducing (non-red.) conditions. (a-e): representative images from at least three independent experiments are shown.
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DiscoverX corporation cho cells stably expressing human mglur7 95-0174c2
(a) ELISA was used to measure the target-binding activity of anti-EGFR and anti-EpCAM IgA antibodies derived from the supernatants of transfected <t>CHO-S</t> cells. Recombinant IgA and IgG antibodies were used as positive controls (ctrl: 0.1 nM), and supernatants from mock-transfected cells served as negative controls. Binding specificity was confirmed by assessing the binding of each IgA antibody to its intended target (EGFR or EpCAM) and to the non-target protein. (b) Western blot analysis of anti-EGFR and anti-EpCAM IgA antibodies in the supernatant of transfected CHO-S cells (lane 1,3). Purified recombinant IgA antibodies were used as controls (lane 2,4). Note that the anti-EGFR IgA control shows incomplete antibody assembly. HC, heavy chain; LC, light chain. (c) Western blot analysis of dimeric IgA antibodies under non-reducing conditions, showing the presence of both the IgA heavy chain (HC), detected by a mouse anti-human kappa chain antibody, and the J-chain (JC), detected by a mouse anti-poly His-tag antibody, in supernatants of CHO-S transiently transfected with the respective expression vectors. 1: anti-EGFR; 2: anti-EpCAM. (d) ELISA was performed to measure SIRPα-Fc protein levels in the supernatant of transfected CHO-S cells, using CD47 as coating. A recombinant anti-CD47 IgG antibody (2.5 nM) was used as a positive control, and supernatant from mock-transfected cells served as a negative control. Wells with no CD47 coating served as additional controls. (e) Western blot analysis of the SIRPα-Fc protein, as detected by a mouse anti-γ heavy chain, in supernatants of CHO-S cells transiently transfected with the respective expression vector, under reducing (red.) and non-reducing (non-red.) conditions. (a-e): representative images from at least three independent experiments are shown.
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FUJIFILM cho dg44-igg-expressing cell line
(a) ELISA was used to measure the target-binding activity of anti-EGFR and anti-EpCAM IgA antibodies derived from the supernatants of transfected <t>CHO-S</t> cells. Recombinant IgA and IgG antibodies were used as positive controls (ctrl: 0.1 nM), and supernatants from mock-transfected cells served as negative controls. Binding specificity was confirmed by assessing the binding of each IgA antibody to its intended target (EGFR or EpCAM) and to the non-target protein. (b) Western blot analysis of anti-EGFR and anti-EpCAM IgA antibodies in the supernatant of transfected CHO-S cells (lane 1,3). Purified recombinant IgA antibodies were used as controls (lane 2,4). Note that the anti-EGFR IgA control shows incomplete antibody assembly. HC, heavy chain; LC, light chain. (c) Western blot analysis of dimeric IgA antibodies under non-reducing conditions, showing the presence of both the IgA heavy chain (HC), detected by a mouse anti-human kappa chain antibody, and the J-chain (JC), detected by a mouse anti-poly His-tag antibody, in supernatants of CHO-S transiently transfected with the respective expression vectors. 1: anti-EGFR; 2: anti-EpCAM. (d) ELISA was performed to measure SIRPα-Fc protein levels in the supernatant of transfected CHO-S cells, using CD47 as coating. A recombinant anti-CD47 IgG antibody (2.5 nM) was used as a positive control, and supernatant from mock-transfected cells served as a negative control. Wells with no CD47 coating served as additional controls. (e) Western blot analysis of the SIRPα-Fc protein, as detected by a mouse anti-γ heavy chain, in supernatants of CHO-S cells transiently transfected with the respective expression vector, under reducing (red.) and non-reducing (non-red.) conditions. (a-e): representative images from at least three independent experiments are shown.
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Astellas human cd46-expressing cho cells
(a) ELISA was used to measure the target-binding activity of anti-EGFR and anti-EpCAM IgA antibodies derived from the supernatants of transfected <t>CHO-S</t> cells. Recombinant IgA and IgG antibodies were used as positive controls (ctrl: 0.1 nM), and supernatants from mock-transfected cells served as negative controls. Binding specificity was confirmed by assessing the binding of each IgA antibody to its intended target (EGFR or EpCAM) and to the non-target protein. (b) Western blot analysis of anti-EGFR and anti-EpCAM IgA antibodies in the supernatant of transfected CHO-S cells (lane 1,3). Purified recombinant IgA antibodies were used as controls (lane 2,4). Note that the anti-EGFR IgA control shows incomplete antibody assembly. HC, heavy chain; LC, light chain. (c) Western blot analysis of dimeric IgA antibodies under non-reducing conditions, showing the presence of both the IgA heavy chain (HC), detected by a mouse anti-human kappa chain antibody, and the J-chain (JC), detected by a mouse anti-poly His-tag antibody, in supernatants of CHO-S transiently transfected with the respective expression vectors. 1: anti-EGFR; 2: anti-EpCAM. (d) ELISA was performed to measure SIRPα-Fc protein levels in the supernatant of transfected CHO-S cells, using CD47 as coating. A recombinant anti-CD47 IgG antibody (2.5 nM) was used as a positive control, and supernatant from mock-transfected cells served as a negative control. Wells with no CD47 coating served as additional controls. (e) Western blot analysis of the SIRPα-Fc protein, as detected by a mouse anti-γ heavy chain, in supernatants of CHO-S cells transiently transfected with the respective expression vector, under reducing (red.) and non-reducing (non-red.) conditions. (a-e): representative images from at least three independent experiments are shown.
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(a) ELISA was used to measure the target-binding activity of anti-EGFR and anti-EpCAM IgA antibodies derived from the supernatants of transfected <t>CHO-S</t> cells. Recombinant IgA and IgG antibodies were used as positive controls (ctrl: 0.1 nM), and supernatants from mock-transfected cells served as negative controls. Binding specificity was confirmed by assessing the binding of each IgA antibody to its intended target (EGFR or EpCAM) and to the non-target protein. (b) Western blot analysis of anti-EGFR and anti-EpCAM IgA antibodies in the supernatant of transfected CHO-S cells (lane 1,3). Purified recombinant IgA antibodies were used as controls (lane 2,4). Note that the anti-EGFR IgA control shows incomplete antibody assembly. HC, heavy chain; LC, light chain. (c) Western blot analysis of dimeric IgA antibodies under non-reducing conditions, showing the presence of both the IgA heavy chain (HC), detected by a mouse anti-human kappa chain antibody, and the J-chain (JC), detected by a mouse anti-poly His-tag antibody, in supernatants of CHO-S transiently transfected with the respective expression vectors. 1: anti-EGFR; 2: anti-EpCAM. (d) ELISA was performed to measure SIRPα-Fc protein levels in the supernatant of transfected CHO-S cells, using CD47 as coating. A recombinant anti-CD47 IgG antibody (2.5 nM) was used as a positive control, and supernatant from mock-transfected cells served as a negative control. Wells with no CD47 coating served as additional controls. (e) Western blot analysis of the SIRPα-Fc protein, as detected by a mouse anti-γ heavy chain, in supernatants of CHO-S cells transiently transfected with the respective expression vector, under reducing (red.) and non-reducing (non-red.) conditions. (a-e): representative images from at least three independent experiments are shown.
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(a) ELISA was used to measure the target-binding activity of anti-EGFR and anti-EpCAM IgA antibodies derived from the supernatants of transfected CHO-S cells. Recombinant IgA and IgG antibodies were used as positive controls (ctrl: 0.1 nM), and supernatants from mock-transfected cells served as negative controls. Binding specificity was confirmed by assessing the binding of each IgA antibody to its intended target (EGFR or EpCAM) and to the non-target protein. (b) Western blot analysis of anti-EGFR and anti-EpCAM IgA antibodies in the supernatant of transfected CHO-S cells (lane 1,3). Purified recombinant IgA antibodies were used as controls (lane 2,4). Note that the anti-EGFR IgA control shows incomplete antibody assembly. HC, heavy chain; LC, light chain. (c) Western blot analysis of dimeric IgA antibodies under non-reducing conditions, showing the presence of both the IgA heavy chain (HC), detected by a mouse anti-human kappa chain antibody, and the J-chain (JC), detected by a mouse anti-poly His-tag antibody, in supernatants of CHO-S transiently transfected with the respective expression vectors. 1: anti-EGFR; 2: anti-EpCAM. (d) ELISA was performed to measure SIRPα-Fc protein levels in the supernatant of transfected CHO-S cells, using CD47 as coating. A recombinant anti-CD47 IgG antibody (2.5 nM) was used as a positive control, and supernatant from mock-transfected cells served as a negative control. Wells with no CD47 coating served as additional controls. (e) Western blot analysis of the SIRPα-Fc protein, as detected by a mouse anti-γ heavy chain, in supernatants of CHO-S cells transiently transfected with the respective expression vector, under reducing (red.) and non-reducing (non-red.) conditions. (a-e): representative images from at least three independent experiments are shown.

Journal: bioRxiv

Article Title: Retargeted adenoviruses for local IgA and CD47 blocker production as a novel cancer therapy

doi: 10.1101/2025.11.07.686998

Figure Lengend Snippet: (a) ELISA was used to measure the target-binding activity of anti-EGFR and anti-EpCAM IgA antibodies derived from the supernatants of transfected CHO-S cells. Recombinant IgA and IgG antibodies were used as positive controls (ctrl: 0.1 nM), and supernatants from mock-transfected cells served as negative controls. Binding specificity was confirmed by assessing the binding of each IgA antibody to its intended target (EGFR or EpCAM) and to the non-target protein. (b) Western blot analysis of anti-EGFR and anti-EpCAM IgA antibodies in the supernatant of transfected CHO-S cells (lane 1,3). Purified recombinant IgA antibodies were used as controls (lane 2,4). Note that the anti-EGFR IgA control shows incomplete antibody assembly. HC, heavy chain; LC, light chain. (c) Western blot analysis of dimeric IgA antibodies under non-reducing conditions, showing the presence of both the IgA heavy chain (HC), detected by a mouse anti-human kappa chain antibody, and the J-chain (JC), detected by a mouse anti-poly His-tag antibody, in supernatants of CHO-S transiently transfected with the respective expression vectors. 1: anti-EGFR; 2: anti-EpCAM. (d) ELISA was performed to measure SIRPα-Fc protein levels in the supernatant of transfected CHO-S cells, using CD47 as coating. A recombinant anti-CD47 IgG antibody (2.5 nM) was used as a positive control, and supernatant from mock-transfected cells served as a negative control. Wells with no CD47 coating served as additional controls. (e) Western blot analysis of the SIRPα-Fc protein, as detected by a mouse anti-γ heavy chain, in supernatants of CHO-S cells transiently transfected with the respective expression vector, under reducing (red.) and non-reducing (non-red.) conditions. (a-e): representative images from at least three independent experiments are shown.

Article Snippet: FreeStyle CHO cells were maintained in suspension in CHOgro expression medium (Mirus Bio, Madison, Wisconsin, USA) supplemented with 20 mM glutamine and 0.3% poloxamer 188 (Mirus Bio), on an orbital shaker at 180 rpm (diameter 50 mm).

Techniques: Enzyme-linked Immunosorbent Assay, Binding Assay, Activity Assay, Derivative Assay, Transfection, Recombinant, Western Blot, Purification, Control, Expressing, Positive Control, Negative Control, Plasmid Preparation