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Fluorescein-SMRT ID2 Corepressor Peptide, 100 µM

LanthaScreen® fluorescent nuclear receptor coregulator peptides contain known interaction motifs and are labeled with fluorescein. These peptides are matched and validated to complement the LanthaScreen® TR-FRET Nuclear Receptor Coregulator Assays. Assays developed using these reagents enable primary or secondary screening of nuclear receptor agonists and/or antagonists.

How they work
Ligand binding to nuclear receptors causes conformational changes in the receptor, resulting in a cascade of events, including dissociation of repressor proteins, association of coactivator proteins, and assembly of pol II and other transcriptional factors for activation of target genes. TR-FRET based assays can be developed using the LanthaScreen® panel of fluorescein-labeled coregulator peptides to investigate conformational changes of nuclear receptors upon ligand binding, either by determining the affinity of ligand-bound receptor for different coregulator peptides, or by identifying additional agonists or antagonists via displacement or recruitment of a specific coregulator peptide. In the LanthaScreen® TR-FRET RXR beta Coactivator Assay, a terbium (Tb)-labeled anti-GST antibody is used to indirectly label GSTtagged RXR beta protein. An agonist (9-cis Retinoic Acid) added to the receptor which, upon ligand binding, causes a conformational change resulting in recruitment of the Fl-D22 coactivator peptide (Figure 1). The binding of the fluorescent coregulator peptide to RXR beta causes an increase in the TR-FRET emission ratio (Figure 2).

Contents and Storage:

LanthaScreen® fluorescent nuclear receptor coregulator peptides are supplied as 100 µM solutions in peptide-appropriate buffers. Store peptides at -20°C.

FL - EAB1 Peptide, 100µM

LanthaScreen® fluorescent nuclear receptor coregulator peptides contain known interaction motifs and are labeled with fluorescein. These peptides are matched and validated to complement the LanthaScreen® TR-FRET Nuclear Receptor Coregulator Assays. Assays developed using these reagents enable primary or secondary screening of nuclear receptor agonists and/or antagonists.

How they work
Ligand binding to nuclear receptors causes conformational changes in the receptor, resulting in a cascade of events, including dissociation of repressor proteins, association of coactivator proteins, and assembly of pol II and other transcriptional factors for activation of target genes. TR-FRET based assays can be developed using the LanthaScreen® panel of fluorescein-labeled coregulator peptides to investigate conformational changes of nuclear receptors upon ligand binding, either by determining the affinity of ligand-bound receptor for different coregulator peptides, or by identifying additional agonists or antagonists via displacement or recruitment of a specific coregulator peptide. In the LanthaScreen® TR-FRET RXR beta Coactivator Assay, a terbium (Tb)-labeled anti-GST antibody is used to indirectly label GSTtagged RXR beta protein. An agonist (9-cis Retinoic Acid) added to the receptor which, upon ligand binding, causes a conformational change resulting in recruitment of the Fl-D22 coactivator peptide (Figure 1). The binding of the fluorescent coregulator peptide to RXR beta causes an increase in the TR-FRET emission ratio (Figure 2).

Contents and Storage:

LanthaScreen® fluorescent nuclear receptor coregulator peptides are supplied as 100 µM solutions in peptide-appropriate buffers. Store peptides at -20°C.

FL - SRC 3-2 Peptide, 100µM

LanthaScreen® fluorescent nuclear receptor coregulator peptides contain known interaction motifs and are labeled with fluorescein. These peptides are matched and validated to complement the LanthaScreen® TR-FRET Nuclear Receptor Coregulator Assays. Assays developed using these reagents enable primary or secondary screening of nuclear receptor agonists and/or antagonists.

How they work
Ligand binding to nuclear receptors causes conformational changes in the receptor, resulting in a cascade of events, including dissociation of repressor proteins, association of coactivator proteins, and assembly of pol II and other transcriptional factors for activation of target genes. TR-FRET based assays can be developed using the LanthaScreen® panel of fluorescein-labeled coregulator peptides to investigate conformational changes of nuclear receptors upon ligand binding, either by determining the affinity of ligand-bound receptor for different coregulator peptides, or by identifying additional agonists or antagonists via displacement or recruitment of a specific coregulator peptide. In the LanthaScreen® TR-FRET RXR beta Coactivator Assay, a terbium (Tb)-labeled anti-GST antibody is used to indirectly label GSTtagged RXR beta protein. An agonist (9-cis Retinoic Acid) added to the receptor which, upon ligand binding, causes a conformational change resulting in recruitment of the Fl-D22 coactivator peptide (Figure 1). The binding of the fluorescent coregulator peptide to RXR beta causes an increase in the TR-FRET emission ratio (Figure 2).

Contents and Storage:

LanthaScreen® fluorescent nuclear receptor coregulator peptides are supplied as 100 µM solutions in peptide-appropriate buffers. Store peptides at -20°C.

FL - eA2 Peptide, 100µM

LanthaScreen® fluorescent nuclear receptor coregulator peptides contain known interaction motifs and are labeled with fluorescein. These peptides are matched and validated to complement the LanthaScreen® TR-FRET Nuclear Receptor Coregulator Assays. Assays developed using these reagents enable primary or secondary screening of nuclear receptor agonists and/or antagonists.

How they work
Ligand binding to nuclear receptors causes conformational changes in the receptor, resulting in a cascade of events, including dissociation of repressor proteins, association of coactivator proteins, and assembly of pol II and other transcriptional factors for activation of target genes. TR-FRET based assays can be developed using the LanthaScreen® panel of fluorescein-labeled coregulator peptides to investigate conformational changes of nuclear receptors upon ligand binding, either by determining the affinity of ligand-bound receptor for different coregulator peptides, or by identifying additional agonists or antagonists via displacement or recruitment of a specific coregulator peptide. In the LanthaScreen® TR-FRET RXR beta Coactivator Assay, a terbium (Tb)-labeled anti-GST antibody is used to indirectly label GSTtagged RXR beta protein. An agonist (9-cis Retinoic Acid) added to the receptor which, upon ligand binding, causes a conformational change resulting in recruitment of the Fl-D22 coactivator peptide (Figure 1). The binding of the fluorescent coregulator peptide to RXR beta causes an increase in the TR-FRET emission ratio (Figure 2).

Contents and Storage:

LanthaScreen® fluorescent nuclear receptor coregulator peptides are supplied as 100 µM solutions in peptide-appropriate buffers. Store peptides at -20°C.

FL - SRC 3-3 Peptide, 100µM

LanthaScreen® fluorescent nuclear receptor coregulator peptides contain known interaction motifs and are labeled with fluorescein. These peptides are matched and validated to complement the LanthaScreen® TR-FRET Nuclear Receptor Coregulator Assays. Assays developed using these reagents enable primary or secondary screening of nuclear receptor agonists and/or antagonists.

How they work
Ligand binding to nuclear receptors causes conformational changes in the receptor, resulting in a cascade of events, including dissociation of repressor proteins, association of coactivator proteins, and assembly of pol II and other transcriptional factors for activation of target genes. TR-FRET based assays can be developed using the LanthaScreen® panel of fluorescein-labeled coregulator peptides to investigate conformational changes of nuclear receptors upon ligand binding, either by determining the affinity of ligand-bound receptor for different coregulator peptides, or by identifying additional agonists or antagonists via displacement or recruitment of a specific coregulator peptide. In the LanthaScreen® TR-FRET RXR beta Coactivator Assay, a terbium (Tb)-labeled anti-GST antibody is used to indirectly label GSTtagged RXR beta protein. An agonist (9-cis Retinoic Acid) added to the receptor which, upon ligand binding, causes a conformational change resulting in recruitment of the Fl-D22 coactivator peptide (Figure 1). The binding of the fluorescent coregulator peptide to RXR beta causes an increase in the TR-FRET emission ratio (Figure 2).

Contents and Storage:

LanthaScreen® fluorescent nuclear receptor coregulator peptides are supplied as 100 µM solutions in peptide-appropriate buffers. Store peptides at -20°C.

FL - TB3 Peptide, 100µM

LanthaScreen® fluorescent nuclear receptor coregulator peptides contain known interaction motifs and are labeled with fluorescein. These peptides are matched and validated to complement the LanthaScreen® TR-FRET Nuclear Receptor Coregulator Assays. Assays developed using these reagents enable primary or secondary screening of nuclear receptor agonists and/or antagonists.

How they work
Ligand binding to nuclear receptors causes conformational changes in the receptor, resulting in a cascade of events, including dissociation of repressor proteins, association of coactivator proteins, and assembly of pol II and other transcriptional factors for activation of target genes. TR-FRET based assays can be developed using the LanthaScreen® panel of fluorescein-labeled coregulator peptides to investigate conformational changes of nuclear receptors upon ligand binding, either by determining the affinity of ligand-bound receptor for different coregulator peptides, or by identifying additional agonists or antagonists via displacement or recruitment of a specific coregulator peptide. In the LanthaScreen® TR-FRET RXR beta Coactivator Assay, a terbium (Tb)-labeled anti-GST antibody is used to indirectly label GSTtagged RXR beta protein. An agonist (9-cis Retinoic Acid) added to the receptor which, upon ligand binding, causes a conformational change resulting in recruitment of the Fl-D22 coactivator peptide (Figure 1). The binding of the fluorescent coregulator peptide to RXR beta causes an increase in the TR-FRET emission ratio (Figure 2).

Contents and Storage:

LanthaScreen® fluorescent nuclear receptor coregulator peptides are supplied as 100 µM solutions in peptide-appropriate buffers. Store peptides at -20°C.

FL - CBP-1 Peptide, 100µM

LanthaScreen® fluorescent nuclear receptor coregulator peptides contain known interaction motifs and are labeled with fluorescein. These peptides are matched and validated to complement the LanthaScreen® TR-FRET Nuclear Receptor Coregulator Assays. Assays developed using these reagents enable primary or secondary screening of nuclear receptor agonists and/or antagonists.

How they work
Ligand binding to nuclear receptors causes conformational changes in the receptor, resulting in a cascade of events, including dissociation of repressor proteins, association of coactivator proteins, and assembly of pol II and other transcriptional factors for activation of target genes. TR-FRET based assays can be developed using the LanthaScreen® panel of fluorescein-labeled coregulator peptides to investigate conformational changes of nuclear receptors upon ligand binding, either by determining the affinity of ligand-bound receptor for different coregulator peptides, or by identifying additional agonists or antagonists via displacement or recruitment of a specific coregulator peptide. In the LanthaScreen® TR-FRET RXR beta Coactivator Assay, a terbium (Tb)-labeled anti-GST antibody is used to indirectly label GSTtagged RXR beta protein. An agonist (9-cis Retinoic Acid) added to the receptor which, upon ligand binding, causes a conformational change resulting in recruitment of the Fl-D22 coactivator peptide (Figure 1). The binding of the fluorescent coregulator peptide to RXR beta causes an increase in the TR-FRET emission ratio (Figure 2).

Contents and Storage:

LanthaScreen® fluorescent nuclear receptor coregulator peptides are supplied as 100 µM solutions in peptide-appropriate buffers. Store peptides at -20°C.

Fluorescein-D22 Coactivator Peptide, 100 µM

LanthaScreen® fluorescent nuclear receptor coregulator peptides contain known interaction motifs and are labeled with fluorescein. These peptides are matched and validated to complement the LanthaScreen® TR-FRET Nuclear Receptor Coregulator Assays. Assays developed using these reagents enable primary or secondary screening of nuclear receptor agonists and/or antagonists.

How they work
Ligand binding to nuclear receptors causes conformational changes in the receptor, resulting in a cascade of events, including dissociation of repressor proteins, association of coactivator proteins, and assembly of pol II and other transcriptional factors for activation of target genes. TR-FRET based assays can be developed using the LanthaScreen® panel of fluorescein-labeled coregulator peptides to investigate conformational changes of nuclear receptors upon ligand binding, either by determining the affinity of ligand-bound receptor for different coregulator peptides, or by identifying additional agonists or antagonists via displacement or recruitment of a specific coregulator peptide. In the LanthaScreen® TR-FRET RXR beta Coactivator Assay, a terbium (Tb)-labeled anti-GST antibody is used to indirectly label GST-tagged RXR beta protein. An agonist (9-cis Retinoic Acid) added to the receptor which, upon ligand binding, causes a conformational change resulting in recruitment of the Fl-D22 coactivator peptide (Figure 1). The binding of the fluorescent coregulator peptide to RXR beta causes an increase in the TR-FRET emission ratio (Figure 2).

Format:
LanthaScreen® fluorescent nuclear receptor coregulator peptides are supplied as 100 µM solutions in peptide-appropriate buffers.

FL-SMRT ID1 Peptide, 100µM

FL-SMRT ID1 PEPTIDE

FL - RIP140L6 Peptide, 100µM

LanthaScreen® fluorescent nuclear receptor coregulator peptides contain known interaction motifs and are labeled with fluorescein. These peptides are matched and validated to complement the LanthaScreen® TR-FRET Nuclear Receptor Coregulator Assays. Assays developed using these reagents enable primary or secondary screening of nuclear receptor agonists and/or antagonists.

How they work
Ligand binding to nuclear receptors causes conformational changes in the receptor, resulting in a cascade of events, including dissociation of repressor proteins, association of coactivator proteins, and assembly of pol II and other transcriptional factors for activation of target genes. TR-FRET based assays can be developed using the LanthaScreen® panel of fluorescein-labeled coregulator peptides to investigate conformational changes of nuclear receptors upon ligand binding, either by determining the affinity of ligand-bound receptor for different coregulator peptides, or by identifying additional agonists or antagonists via displacement or recruitment of a specific coregulator peptide. In the LanthaScreen® TR-FRET RXR beta Coactivator Assay, a terbium (Tb)-labeled anti-GST antibody is used to indirectly label GSTtagged RXR beta protein. An agonist (9-cis Retinoic Acid) added to the receptor which, upon ligand binding, causes a conformational change resulting in recruitment of the Fl-D22 coactivator peptide (Figure 1). The binding of the fluorescent coregulator peptide to RXR beta causes an increase in the TR-FRET emission ratio (Figure 2).

Contents and Storage:

LanthaScreen® fluorescent nuclear receptor coregulator peptides are supplied as 100 µM solutions in peptide-appropriate buffers. Store peptides at -20°C.

Fl - SRC 2-2 peptide, 100µM

LanthaScreen® fluorescent nuclear receptor coregulator peptides contain known interaction motifs and are labeled with fluorescein. These peptides are matched and validated to complement the LanthaScreen® TR-FRET Nuclear Receptor Coregulator Assays. Assays developed using these reagents enable primary or secondary screening of nuclear receptor agonists and/or antagonists.

How they work
Ligand binding to nuclear receptors causes conformational changes in the receptor, resulting in a cascade of events, including dissociation of repressor proteins, association of coactivator proteins, and assembly of pol II and other transcriptional factors for activation of target genes. TR-FRET based assays can be developed using the LanthaScreen® panel of fluorescein-labeled coregulator peptides to investigate conformational changes of nuclear receptors upon ligand binding, either by determining the affinity of ligand-bound receptor for different coregulator peptides, or by identifying additional agonists or antagonists via displacement or recruitment of a specific coregulator peptide. In the LanthaScreen® TR-FRET RXR beta Coactivator Assay, a terbium (Tb)-labeled anti-GST antibody is used to indirectly label GSTtagged RXR beta protein. An agonist (9-cis Retinoic Acid) added to the receptor which, upon ligand binding, causes a conformational change resulting in recruitment of the Fl-D22 coactivator peptide (Figure 1). The binding of the fluorescent coregulator peptide to RXR beta causes an increase in the TR-FRET emission ratio (Figure 2).

Contents and Storage:

LanthaScreen® fluorescent nuclear receptor coregulator peptides are supplied as 100 µM solutions in peptide-appropriate buffers. Store peptides at -20°C.

Fluorescein-PGC1a Coactivator Peptide, 100 µM

LanthaScreen® fluorescent nuclear receptor coregulator peptides contain known interaction motifs and are labeled with fluorescein. These peptides are matched and validated to complement the LanthaScreen® TR-FRET Nuclear Receptor Coregulator Assays. Assays developed using these reagents enable primary or secondary screening of nuclear receptor agonists and/or antagonists.

How they work
Ligand binding to nuclear receptors causes conformational changes in the receptor, resulting in a cascade of events, including dissociation of repressor proteins, association of coactivator proteins, and assembly of pol II and other transcriptional factors for activation of target genes. TR-FRET based assays can be developed using the LanthaScreen® panel of fluorescein-labeled coregulator peptides to investigate conformational changes of nuclear receptors upon ligand binding, either by determining the affinity of ligand-bound receptor for different coregulator peptides, or by identifying additional agonists or antagonists via displacement or recruitment of a specific coregulator peptide. In the LanthaScreen® TR-FRET RXR beta Coactivator Assay, a terbium (Tb)-labeled anti-GST antibody is used to indirectly label GSTtagged RXR beta protein. An agonist (9-cis Retinoic Acid) added to the receptor which, upon ligand binding, causes a conformational change resulting in recruitment of the Fl-D22 coactivator peptide (Figure 1). The binding of the fluorescent coregulator peptide to RXR beta causes an increase in the TR-FRET emission ratio (Figure 2).

Contents and Storage:

LanthaScreen® fluorescent nuclear receptor coregulator peptides are supplied as 100 µM solutions in peptide-appropriate buffers. Store peptides at -20°C.

FL-AR N-TERM Peptide

LanthaScreen® fluorescent nuclear receptor coregulator peptides contain known interaction motifs and are labeled with fluorescein. These peptides are matched and validated to complement the LanthaScreen® TR-FRET Nuclear Receptor Coregulator Assays. Assays developed using these reagents enable primary or secondary screening of nuclear receptor agonists and/or antagonists.

How they work
Ligand binding to nuclear receptors causes conformational changes in the receptor, resulting in a cascade of events, including dissociation of repressor proteins, association of coactivator proteins, and assembly of pol II and other transcriptional factors for activation of target genes. TR-FRET based assays can be developed using the LanthaScreen® panel of fluorescein-labeled coregulator peptides to investigate conformational changes of nuclear receptors upon ligand binding, either by determining the affinity of ligand-bound receptor for different coregulator peptides, or by identifying additional agonists or antagonists via displacement or recruitment of a specific coregulator peptide. In the LanthaScreen® TR-FRET RXR beta Coactivator Assay, a terbium (Tb)-labeled anti-GST antibody is used to indirectly label GSTtagged RXR beta protein. An agonist (9-cis Retinoic Acid) added to the receptor which, upon ligand binding, causes a conformational change resulting in recruitment of the Fl-D22 coactivator peptide (Figure 1). The binding of the fluorescent coregulator peptide to RXR beta causes an increase in the TR-FRET emission ratio (Figure 2).

Contents and Storage:

LanthaScreen® fluorescent nuclear receptor coregulator peptides are supplied as 100 µM solutions in peptide-appropriate buffers. Store peptides at -20°C.

FL - TRAP220DRIP1 PEP, 100µM

LanthaScreen® fluorescent nuclear receptor coregulator peptides contain known interaction motifs and are labeled with fluorescein. These peptides are matched and validated to complement the LanthaScreen® TR-FRET Nuclear Receptor Coregulator Assays. Assays developed using these reagents enable primary or secondary screening of nuclear receptor agonists and/or antagonists.

How they work
Ligand binding to nuclear receptors causes conformational changes in the receptor, resulting in a cascade of events, including dissociation of repressor proteins, association of coactivator proteins, and assembly of pol II and other transcriptional factors for activation of target genes. TR-FRET based assays can be developed using the LanthaScreen® panel of fluorescein-labeled coregulator peptides to investigate conformational changes of nuclear receptors upon ligand binding, either by determining the affinity of ligand-bound receptor for different coregulator peptides, or by identifying additional agonists or antagonists via displacement or recruitment of a specific coregulator peptide. In the LanthaScreen® TR-FRET RXR beta Coactivator Assay, a terbium (Tb)-labeled anti-GST antibody is used to indirectly label GSTtagged RXR beta protein. An agonist (9-cis Retinoic Acid) added to the receptor which, upon ligand binding, causes a conformational change resulting in recruitment of the Fl-D22 coactivator peptide (Figure 1). The binding of the fluorescent coregulator peptide to RXR beta causes an increase in the TR-FRET emission ratio (Figure 2).

Contents and Storage:

LanthaScreen® fluorescent nuclear receptor coregulator peptides are supplied as 100 µM solutions in peptide-appropriate buffers. Store peptides at -20°C.

Fl - SRC 2-1 peptide, 100µM

LanthaScreen® fluorescent nuclear receptor coregulator peptides contain known interaction motifs and are labeled with fluorescein. These peptides are matched and validated to complement the LanthaScreen® TR-FRET Nuclear Receptor Coregulator Assays. Assays developed using these reagents enable primary or secondary screening of nuclear receptor agonists and/or antagonists.

How they work
Ligand binding to nuclear receptors causes conformational changes in the receptor, resulting in a cascade of events, including dissociation of repressor proteins, association of coactivator proteins, and assembly of pol II and other transcriptional factors for activation of target genes. TR-FRET based assays can be developed using the LanthaScreen® panel of fluorescein-labeled coregulator peptides to investigate conformational changes of nuclear receptors upon ligand binding, either by determining the affinity of ligand-bound receptor for different coregulator peptides, or by identifying additional agonists or antagonists via displacement or recruitment of a specific coregulator peptide. In the LanthaScreen® TR-FRET RXR beta Coactivator Assay, a terbium (Tb)-labeled anti-GST antibody is used to indirectly label GSTtagged RXR beta protein. An agonist (9-cis Retinoic Acid) added to the receptor which, upon ligand binding, causes a conformational change resulting in recruitment of the Fl-D22 coactivator peptide (Figure 1). The binding of the fluorescent coregulator peptide to RXR beta causes an increase in the TR-FRET emission ratio (Figure 2).

Contents and Storage:

LanthaScreen® fluorescent nuclear receptor coregulator peptides are supplied as 100 µM solutions in peptide-appropriate buffers. Store peptides at -20°C.