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human antibody capture kit tm  (Danaher Inc)
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Adiponectin binding analysis in T-cadFc <t>capture</t> and surface plasmon assays. A, representative immunoblot for adiponectin (APN) in bound fractions of T-cadFc capture assay using the strategy depicted in Fig. 2A. Increasing concentrations of purified adiponectin were applied as the input fraction. Trimer equivalents of adiponectin concentrations of all fractions were determined experimentally by ELISA. B and C, saturable binding curve (B) and its Scatchard plot of ELISA-based binding assay (C). The binding constant (KD) was calculated as the slope of the approximation straight line. D, SPR analysis of purified adiponectin (APN) and full-length T-cadFc. ∼100 response units of T-cad fused with <t>human</t> IgG-Fc were trapped by anti-human IgG Fc <t>antibody</t> immobilized on the sensor surface, and each concentration (333–1.1 nm trimer equivalent) of purified adiponectin was injected at time = 0. Each sensorgram was adjusted to that of purified adiponectin = 0 nm (not shown). Kinetics constants (ka and kd) were analyzed using BIACORE T200 evaluation software v1.0, assuming a 1:1 binding model.
Human Antibody Capture Kit Tm, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+antibody+capture+kit+tm/Human+Antibody+Capture+Kit/pmc05427265-272-12-17
Average 94 stars, based on 1 article reviews
human antibody capture kit tm - by Bioz Stars, 2026-10
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human antibody capture kit tm  (Cytiva Europe)
94
Cytiva Europe human antibody capture kit tm
Adiponectin binding analysis in T-cadFc <t>capture</t> and surface plasmon assays. A, representative immunoblot for adiponectin (APN) in bound fractions of T-cadFc capture assay using the strategy depicted in Fig. 2A. Increasing concentrations of purified adiponectin were applied as the input fraction. Trimer equivalents of adiponectin concentrations of all fractions were determined experimentally by ELISA. B and C, saturable binding curve (B) and its Scatchard plot of ELISA-based binding assay (C). The binding constant (KD) was calculated as the slope of the approximation straight line. D, SPR analysis of purified adiponectin (APN) and full-length T-cadFc. ∼100 response units of T-cad fused with <t>human</t> IgG-Fc were trapped by anti-human IgG Fc <t>antibody</t> immobilized on the sensor surface, and each concentration (333–1.1 nm trimer equivalent) of purified adiponectin was injected at time = 0. Each sensorgram was adjusted to that of purified adiponectin = 0 nm (not shown). Kinetics constants (ka and kd) were analyzed using BIACORE T200 evaluation software v1.0, assuming a 1:1 binding model.
Human Antibody Capture Kit Tm, supplied by Cytiva Europe, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+antibody+capture+kit+tm/Human+Antibody+Capture+Kit/pmc05427265-216-12-17
Average 94 stars, based on 1 article reviews
human antibody capture kit tm - by Bioz Stars, 2026-10
94/100 stars
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Adiponectin binding analysis in T-cadFc capture and surface plasmon assays. A, representative immunoblot for adiponectin (APN) in bound fractions of T-cadFc capture assay using the strategy depicted in Fig. 2A. Increasing concentrations of purified adiponectin were applied as the input fraction. Trimer equivalents of adiponectin concentrations of all fractions were determined experimentally by ELISA. B and C, saturable binding curve (B) and its Scatchard plot of ELISA-based binding assay (C). The binding constant (KD) was calculated as the slope of the approximation straight line. D, SPR analysis of purified adiponectin (APN) and full-length T-cadFc. ∼100 response units of T-cad fused with human IgG-Fc were trapped by anti-human IgG Fc antibody immobilized on the sensor surface, and each concentration (333–1.1 nm trimer equivalent) of purified adiponectin was injected at time = 0. Each sensorgram was adjusted to that of purified adiponectin = 0 nm (not shown). Kinetics constants (ka and kd) were analyzed using BIACORE T200 evaluation software v1.0, assuming a 1:1 binding model.

Journal:

Article Title:

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Figure Lengend Snippet: Adiponectin binding analysis in T-cadFc capture and surface plasmon assays. A, representative immunoblot for adiponectin (APN) in bound fractions of T-cadFc capture assay using the strategy depicted in Fig. 2A. Increasing concentrations of purified adiponectin were applied as the input fraction. Trimer equivalents of adiponectin concentrations of all fractions were determined experimentally by ELISA. B and C, saturable binding curve (B) and its Scatchard plot of ELISA-based binding assay (C). The binding constant (KD) was calculated as the slope of the approximation straight line. D, SPR analysis of purified adiponectin (APN) and full-length T-cadFc. ∼100 response units of T-cad fused with human IgG-Fc were trapped by anti-human IgG Fc antibody immobilized on the sensor surface, and each concentration (333–1.1 nm trimer equivalent) of purified adiponectin was injected at time = 0. Each sensorgram was adjusted to that of purified adiponectin = 0 nm (not shown). Kinetics constants (ka and kd) were analyzed using BIACORE T200 evaluation software v1.0, assuming a 1:1 binding model.

Article Snippet: Anti-human IgG-Fc antibody was immobilized over all four flow cells using the Human Antibody Capture Kit TM (GE Healthcare) according to the instructions supplied by the manufacturer.

Techniques: Binding Assay, Western Blot, Purification, Enzyme-linked Immunosorbent Assay, Concentration Assay, Injection, Software

Adiponectin binding analysis in T-cadFc capture and surface plasmon assays. A, representative immunoblot for adiponectin (APN) in bound fractions of T-cadFc capture assay using the strategy depicted in Fig. 2A. Increasing concentrations of purified adiponectin were applied as the input fraction. Trimer equivalents of adiponectin concentrations of all fractions were determined experimentally by ELISA. B and C, saturable binding curve (B) and its Scatchard plot of ELISA-based binding assay (C). The binding constant (KD) was calculated as the slope of the approximation straight line. D, SPR analysis of purified adiponectin (APN) and full-length T-cadFc. ∼100 response units of T-cad fused with human IgG-Fc were trapped by anti-human IgG Fc antibody immobilized on the sensor surface, and each concentration (333–1.1 nm trimer equivalent) of purified adiponectin was injected at time = 0. Each sensorgram was adjusted to that of purified adiponectin = 0 nm (not shown). Kinetics constants (ka and kd) were analyzed using BIACORE T200 evaluation software v1.0, assuming a 1:1 binding model.

Journal: The Journal of Biological Chemistry

Article Title: The unique prodomain of T-cadherin plays a key role in adiponectin binding with the essential extracellular cadherin repeats 1 and 2

doi: 10.1074/jbc.M117.780734

Figure Lengend Snippet: Adiponectin binding analysis in T-cadFc capture and surface plasmon assays. A, representative immunoblot for adiponectin (APN) in bound fractions of T-cadFc capture assay using the strategy depicted in Fig. 2A. Increasing concentrations of purified adiponectin were applied as the input fraction. Trimer equivalents of adiponectin concentrations of all fractions were determined experimentally by ELISA. B and C, saturable binding curve (B) and its Scatchard plot of ELISA-based binding assay (C). The binding constant (KD) was calculated as the slope of the approximation straight line. D, SPR analysis of purified adiponectin (APN) and full-length T-cadFc. ∼100 response units of T-cad fused with human IgG-Fc were trapped by anti-human IgG Fc antibody immobilized on the sensor surface, and each concentration (333–1.1 nm trimer equivalent) of purified adiponectin was injected at time = 0. Each sensorgram was adjusted to that of purified adiponectin = 0 nm (not shown). Kinetics constants (ka and kd) were analyzed using BIACORE T200 evaluation software v1.0, assuming a 1:1 binding model.

Article Snippet: Anti-human IgG-Fc antibody was immobilized over all four flow cells using the Human Antibody Capture Kit TM (GE Healthcare) according to the instructions supplied by the manufacturer.

Techniques: Binding Assay, Western Blot, Purification, Enzyme-linked Immunosorbent Assay, Concentration Assay, Injection, Software