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TaKaRa talon cobalt resin
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Cytiva Europe hitrap n hydroxysuccinimide nhs activated high performance hp affinity column
Characterization of novel anti‐clusterin mAbs. (A) Representative sandwich ELISA testing compatibility of mAb 2D5 as capture with all eight clusterin mAbs as detection. Purified clusterin was used as standard (1–0.0625 µg/ml), 2D5 and biotinylated detection mAbs were used at 2 µg/ml. Error bars represent standard error of duplicates; data for other capture mAbs can be found in Figure . (B) Western blot showing detection with mAbs 2D5 and 4C7 (2 µg/ml) of purified clusterin (80 ng/lane) and clusterin in serum <t>(NHS;</t> 1 µl/lane) run under NR (single band at 70 kDa) and R (double band at 40 kDa) conditions. Secondary only and other mAb blots are shown in Figure . (C–D) Representative SPR sensorgrams showing mAbs 2D5 and 4C7 (100–6.25 nM) binding clusterin immobilized on the surface. Gray and colored lines represent raw and fitted data, respectively. (E) Binding kinetics were calculated from three independent experiments; KD, k a , and k d are the equilibrium dissociation constant, association rate constant, and dissociation rate constant, respectively. mAb, monoclonal antibody; ELISA, enzyme‐linked immunosorbent assay; NHS, <t>N‐hydroxysuccinimide;</t> NR, non‐reducing; R, reducing; SPR, surface plasmon resonance.
Hitrap N Hydroxysuccinimide Nhs Activated High Performance Hp Affinity Column, supplied by Cytiva Europe, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Cytiva Europe metal affinity chromatography
Characterization of novel anti‐clusterin mAbs. (A) Representative sandwich ELISA testing compatibility of mAb 2D5 as capture with all eight clusterin mAbs as detection. Purified clusterin was used as standard (1–0.0625 µg/ml), 2D5 and biotinylated detection mAbs were used at 2 µg/ml. Error bars represent standard error of duplicates; data for other capture mAbs can be found in Figure . (B) Western blot showing detection with mAbs 2D5 and 4C7 (2 µg/ml) of purified clusterin (80 ng/lane) and clusterin in serum <t>(NHS;</t> 1 µl/lane) run under NR (single band at 70 kDa) and R (double band at 40 kDa) conditions. Secondary only and other mAb blots are shown in Figure . (C–D) Representative SPR sensorgrams showing mAbs 2D5 and 4C7 (100–6.25 nM) binding clusterin immobilized on the surface. Gray and colored lines represent raw and fitted data, respectively. (E) Binding kinetics were calculated from three independent experiments; KD, k a , and k d are the equilibrium dissociation constant, association rate constant, and dissociation rate constant, respectively. mAb, monoclonal antibody; ELISA, enzyme‐linked immunosorbent assay; NHS, <t>N‐hydroxysuccinimide;</t> NR, non‐reducing; R, reducing; SPR, surface plasmon resonance.
Metal Affinity Chromatography, supplied by Cytiva Europe, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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TaKaRa cobalt based affinity resin
Characterization of novel anti‐clusterin mAbs. (A) Representative sandwich ELISA testing compatibility of mAb 2D5 as capture with all eight clusterin mAbs as detection. Purified clusterin was used as standard (1–0.0625 µg/ml), 2D5 and biotinylated detection mAbs were used at 2 µg/ml. Error bars represent standard error of duplicates; data for other capture mAbs can be found in Figure . (B) Western blot showing detection with mAbs 2D5 and 4C7 (2 µg/ml) of purified clusterin (80 ng/lane) and clusterin in serum <t>(NHS;</t> 1 µl/lane) run under NR (single band at 70 kDa) and R (double band at 40 kDa) conditions. Secondary only and other mAb blots are shown in Figure . (C–D) Representative SPR sensorgrams showing mAbs 2D5 and 4C7 (100–6.25 nM) binding clusterin immobilized on the surface. Gray and colored lines represent raw and fitted data, respectively. (E) Binding kinetics were calculated from three independent experiments; KD, k a , and k d are the equilibrium dissociation constant, association rate constant, and dissociation rate constant, respectively. mAb, monoclonal antibody; ELISA, enzyme‐linked immunosorbent assay; NHS, <t>N‐hydroxysuccinimide;</t> NR, non‐reducing; R, reducing; SPR, surface plasmon resonance.
Cobalt Based Affinity Resin, supplied by TaKaRa, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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TaKaRa ni nta agarose beads
Characterization of novel anti‐clusterin mAbs. (A) Representative sandwich ELISA testing compatibility of mAb 2D5 as capture with all eight clusterin mAbs as detection. Purified clusterin was used as standard (1–0.0625 µg/ml), 2D5 and biotinylated detection mAbs were used at 2 µg/ml. Error bars represent standard error of duplicates; data for other capture mAbs can be found in Figure . (B) Western blot showing detection with mAbs 2D5 and 4C7 (2 µg/ml) of purified clusterin (80 ng/lane) and clusterin in serum <t>(NHS;</t> 1 µl/lane) run under NR (single band at 70 kDa) and R (double band at 40 kDa) conditions. Secondary only and other mAb blots are shown in Figure . (C–D) Representative SPR sensorgrams showing mAbs 2D5 and 4C7 (100–6.25 nM) binding clusterin immobilized on the surface. Gray and colored lines represent raw and fitted data, respectively. (E) Binding kinetics were calculated from three independent experiments; KD, k a , and k d are the equilibrium dissociation constant, association rate constant, and dissociation rate constant, respectively. mAb, monoclonal antibody; ELISA, enzyme‐linked immunosorbent assay; NHS, <t>N‐hydroxysuccinimide;</t> NR, non‐reducing; R, reducing; SPR, surface plasmon resonance.
Ni Nta Agarose Beads, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Cytiva Europe affinity chromatography
Characterization of novel anti‐clusterin mAbs. (A) Representative sandwich ELISA testing compatibility of mAb 2D5 as capture with all eight clusterin mAbs as detection. Purified clusterin was used as standard (1–0.0625 µg/ml), 2D5 and biotinylated detection mAbs were used at 2 µg/ml. Error bars represent standard error of duplicates; data for other capture mAbs can be found in Figure . (B) Western blot showing detection with mAbs 2D5 and 4C7 (2 µg/ml) of purified clusterin (80 ng/lane) and clusterin in serum <t>(NHS;</t> 1 µl/lane) run under NR (single band at 70 kDa) and R (double band at 40 kDa) conditions. Secondary only and other mAb blots are shown in Figure . (C–D) Representative SPR sensorgrams showing mAbs 2D5 and 4C7 (100–6.25 nM) binding clusterin immobilized on the surface. Gray and colored lines represent raw and fitted data, respectively. (E) Binding kinetics were calculated from three independent experiments; KD, k a , and k d are the equilibrium dissociation constant, association rate constant, and dissociation rate constant, respectively. mAb, monoclonal antibody; ELISA, enzyme‐linked immunosorbent assay; NHS, <t>N‐hydroxysuccinimide;</t> NR, non‐reducing; R, reducing; SPR, surface plasmon resonance.
Affinity Chromatography, supplied by Cytiva Europe, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Sino Biological resource source identifier antibodies rabbit anti tbx5 sino biological
Characterization of novel anti‐clusterin mAbs. (A) Representative sandwich ELISA testing compatibility of mAb 2D5 as capture with all eight clusterin mAbs as detection. Purified clusterin was used as standard (1–0.0625 µg/ml), 2D5 and biotinylated detection mAbs were used at 2 µg/ml. Error bars represent standard error of duplicates; data for other capture mAbs can be found in Figure . (B) Western blot showing detection with mAbs 2D5 and 4C7 (2 µg/ml) of purified clusterin (80 ng/lane) and clusterin in serum <t>(NHS;</t> 1 µl/lane) run under NR (single band at 70 kDa) and R (double band at 40 kDa) conditions. Secondary only and other mAb blots are shown in Figure . (C–D) Representative SPR sensorgrams showing mAbs 2D5 and 4C7 (100–6.25 nM) binding clusterin immobilized on the surface. Gray and colored lines represent raw and fitted data, respectively. (E) Binding kinetics were calculated from three independent experiments; KD, k a , and k d are the equilibrium dissociation constant, association rate constant, and dissociation rate constant, respectively. mAb, monoclonal antibody; ELISA, enzyme‐linked immunosorbent assay; NHS, <t>N‐hydroxysuccinimide;</t> NR, non‐reducing; R, reducing; SPR, surface plasmon resonance.
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R&D Systems somatropin affinity purified goat polyclonal antibody
Characterization of novel anti‐clusterin mAbs. (A) Representative sandwich ELISA testing compatibility of mAb 2D5 as capture with all eight clusterin mAbs as detection. Purified clusterin was used as standard (1–0.0625 µg/ml), 2D5 and biotinylated detection mAbs were used at 2 µg/ml. Error bars represent standard error of duplicates; data for other capture mAbs can be found in Figure . (B) Western blot showing detection with mAbs 2D5 and 4C7 (2 µg/ml) of purified clusterin (80 ng/lane) and clusterin in serum <t>(NHS;</t> 1 µl/lane) run under NR (single band at 70 kDa) and R (double band at 40 kDa) conditions. Secondary only and other mAb blots are shown in Figure . (C–D) Representative SPR sensorgrams showing mAbs 2D5 and 4C7 (100–6.25 nM) binding clusterin immobilized on the surface. Gray and colored lines represent raw and fitted data, respectively. (E) Binding kinetics were calculated from three independent experiments; KD, k a , and k d are the equilibrium dissociation constant, association rate constant, and dissociation rate constant, respectively. mAb, monoclonal antibody; ELISA, enzyme‐linked immunosorbent assay; NHS, <t>N‐hydroxysuccinimide;</t> NR, non‐reducing; R, reducing; SPR, surface plasmon resonance.
Somatropin Affinity Purified Goat Polyclonal Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Characterization of novel anti‐clusterin mAbs. (A) Representative sandwich ELISA testing compatibility of mAb 2D5 as capture with all eight clusterin mAbs as detection. Purified clusterin was used as standard (1–0.0625 µg/ml), 2D5 and biotinylated detection mAbs were used at 2 µg/ml. Error bars represent standard error of duplicates; data for other capture mAbs can be found in Figure . (B) Western blot showing detection with mAbs 2D5 and 4C7 (2 µg/ml) of purified clusterin (80 ng/lane) and clusterin in serum (NHS; 1 µl/lane) run under NR (single band at 70 kDa) and R (double band at 40 kDa) conditions. Secondary only and other mAb blots are shown in Figure . (C–D) Representative SPR sensorgrams showing mAbs 2D5 and 4C7 (100–6.25 nM) binding clusterin immobilized on the surface. Gray and colored lines represent raw and fitted data, respectively. (E) Binding kinetics were calculated from three independent experiments; KD, k a , and k d are the equilibrium dissociation constant, association rate constant, and dissociation rate constant, respectively. mAb, monoclonal antibody; ELISA, enzyme‐linked immunosorbent assay; NHS, N‐hydroxysuccinimide; NR, non‐reducing; R, reducing; SPR, surface plasmon resonance.

Journal: Alzheimer's & Dementia

Article Title: Clusterin is enriched in plaque‐associated astrocytes and localizes to synapses in Alzheimer's disease

doi: 10.1002/alz.71885

Figure Lengend Snippet: Characterization of novel anti‐clusterin mAbs. (A) Representative sandwich ELISA testing compatibility of mAb 2D5 as capture with all eight clusterin mAbs as detection. Purified clusterin was used as standard (1–0.0625 µg/ml), 2D5 and biotinylated detection mAbs were used at 2 µg/ml. Error bars represent standard error of duplicates; data for other capture mAbs can be found in Figure . (B) Western blot showing detection with mAbs 2D5 and 4C7 (2 µg/ml) of purified clusterin (80 ng/lane) and clusterin in serum (NHS; 1 µl/lane) run under NR (single band at 70 kDa) and R (double band at 40 kDa) conditions. Secondary only and other mAb blots are shown in Figure . (C–D) Representative SPR sensorgrams showing mAbs 2D5 and 4C7 (100–6.25 nM) binding clusterin immobilized on the surface. Gray and colored lines represent raw and fitted data, respectively. (E) Binding kinetics were calculated from three independent experiments; KD, k a , and k d are the equilibrium dissociation constant, association rate constant, and dissociation rate constant, respectively. mAb, monoclonal antibody; ELISA, enzyme‐linked immunosorbent assay; NHS, N‐hydroxysuccinimide; NR, non‐reducing; R, reducing; SPR, surface plasmon resonance.

Article Snippet: Anti‐clusterin mAb 2D5 (7 mg) was coupled to a HiTrap N‐hydroxysuccinimide (NHS) ‐activated high performance (HP) affinity column (Cytiva, #17071601).

Techniques: Sandwich ELISA, Purification, Western Blot, Binding Assay, Affinity Constant, Association Rate Constant, Dissociation Rate Constant, Enzyme-linked Immunosorbent Assay, SPR Assay