GnRH membrane preparations were obtained from Millipore ChemiScreen (HTS027M). The GnRH receptor binding affinities (IC50 values) of FP-d -Lys6-GnRH, d -Lys6-GnRH, and NOTA-P-d -Lys6-GnRH were determined by in vitro competitive binding assay according to the manufacturer's protocol. In brief, 5 μL of Millipore ChemiScreen human GnRH membrane preparations was incubated at room temperature for 1.5 h with approximately 20,000 counts per minute (cpm) of [131I](His5, d -Tyr6)GnRH in the presence of 10−11 to 10−5 M of each peptide in 95 μL of binding buffer (50 mM HEPES, 5 mM MgCl2, 1 mM CaCl2, 0.2% BSA, buffer to pH 7.4 using 1 M NaOH). After the incubation, 600 μL of ice-cold washing buffer (50 mM HEPES, 500 mM NaCl, 0.1% BSA, buffer to pH 7.4 using 1 M NaOH) was added to each mixture. Each resulting mixture was filtered through a GF/C filter (Whatman, Clifton, NJ) presoaked in 0.33% polyethylenimine. Each filter was rinsed with 1 mL of ice-cold wash buffer six times. The activities on the filters were measured in a gamma counter (γ-counter).
Chemiscreen
Manufactured by Merck Group
Chemiscreen is a high-performance laboratory equipment designed for chemical screening and analysis. It provides precise and reliable data for a variety of applications in the pharmaceutical, chemical, and research industries.
Automatically generated - may contain errors
Lab products found in correlation
7 protocols using chemiscreen
1
GnRH Receptor Binding Assay
2
Characterization of Anti-CGRP Antibodies
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Example 6
To characterize recombinantly expressed antibodies for their ability to inhibit CGRP binding to its cellular receptor, a radioligand-binding assay was performed as previously described [Elshourbagy et al, Endocrinology 139:1678 (1998); Zimmerman et al, Peptides, 16:421 (1995)]. Membrane preparations of recombinant human CGRP receptors, calcitonin receptor-like receptor and RAMP (Chemiscreen, Millipore) were used. Antibody dilutions were preincubated with 125I radiolabeled human CGRPα (0.03 nM) for 30 minutes at room temperature. Non-specific binding was estimated in the presence of 0.1 M human CGRPα. Membranes were filtered and washed. The filters were then counted to determine 125I radiolabeled human CGRPα specifically bound.
Results:
3
Inhibition of CGRP Receptor Binding
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Example 6
To characterize recombinantly expressed antibodies for their ability to inhibit CGRP binding to its cellular receptor, a radioligand-binding assay was performed as previously described [Elshourbagy et al, Endocrinology 139:1678 (1998); Zimmerman et al, Peptides, 16:421 (1995)]. Membrane preparations of recombinant human CGRP receptors, calcitonin receptor-like receptor and RAMP1 (Chemiscreen, Millipore) were used. Antibody dilutions were preincubated with 125I radiolabeled human CGRPα (0.03 nM) for 30 minutes at room temperature. Non-specific binding was estimated in the presence of 0.1 μM human CGRPα. Membranes were filtered and washed. The filters were then counted to determine 125I radiolabeled human CGRPα specifically bound.
Results:
4
Characterizing Anti-CGRP Antibody Inhibition
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Example 6
To characterize recombinantly expressed antibodies for their ability to inhibit CGRP binding to its cellular receptor, a radioligand-binding assay was performed as previously described [Elshourbagy et al, Endocrinology 139:1678 (1998); Zimmerman et al, Peptides, 16:421 (1995)]. Membrane preparations of recombinant human CGRP receptors, calcitonin receptor-like receptor and RAMP1 (Chemiscreen, Millipore) were used. Antibody dilutions were preincubated with 125I radiolabeled human CGRPα (0.03 nM) for 30 minutes at room temperature. Non-specific binding was estimated in the presence of 0.1 μM human CGRPα. Membranes were filtered and washed. The filters were then counted to determine 125I radiolabeled human CGRPα specifically bound.
Results:
5
Inhibition of CGRP Receptor Binding
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Example 6
To characterize recombinantly expressed antibodies for their ability to inhibit CGRP binding to its cellular receptor, a radioligand-binding assay was performed as previously described [Elshourbagy et al, Endocrinology 139:1678 (1998); Zimmerman et al, Peptides, 16:421 (1995)]. Membrane preparations of recombinant human CGRP receptors, calcitonin receptor-like receptor and RAMP1 (Chemiscreen, Millipore) were used. Antibody dilutions were preincubated with 125I radiolabeled human CGRPα (0.03 nM) for 30 minutes at room temperature. Non-specific binding was estimated in the presence of 0.1 μM human CGRPα. Membranes were filtered and washed. The filters were then counted to determine 125I radiolabeled human CGRPα specifically bound.
Results:
6
Characterizing Anti-CGRP Antibody Inhibition
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Example 6
To characterize recombinantly expressed antibodies for their ability to inhibit CGRP binding to its cellular receptor, a radioligand-binding assay was performed as previously described [Elshourbagy et al, Endocrinology 139:1678 (1998); Zimmerman et al, Peptides, 16:421 (1995)]. Membrane preparations of recombinant human CGRP receptors, calcitonin receptor-like receptor and RAMP1 (Chemiscreen, Millipore) were used. Antibody dilutions were preincubated with 125I radiolabeled human CGRPα (0.03 nM) for 30 minutes at room temperature. Non-specific binding was estimated in the presence of 0.1 μM human CGRPα. Membranes were filtered and washed. The filters were then counted to determine 125I radiolabeled human CGRPα specifically bound.
Results:
7
Antibody Inhibition of CGRP Receptor Binding
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Example 6
To characterize recombinantly expressed antibodies for their ability to inhibit CGRP binding to its cellular receptor, a radioligand-binding assay was performed as previously described [Elshourbagy et al, Endocrinology 139:1678 (1998); Zimmerman et al, Peptides, 16:421 (1995)]. Membrane preparations of recombinant human CGRP receptors, calcitonin receptor-like receptor and RAMP1 (Chemiscreen, Millipore) were used. Antibody dilutions were preincubated with 125I radiolabeld human CGRPα (0.03 nM) for 30 minutes at room temperature. Non-specific binding was estimated in the presence of 0.1 μM human CGRPα. Membranes were filtered and washed. The filters were then counted to determine 125I radiolabeld human CGRPα specifically bound.
Results:
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