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Monoclonal Antibody Chromatin IP Ligand-Dependent Nuclear Receptor Activity

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Chromatin IP-seq, Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Human progesterone receptor (PR) is expressed as two forms: the full length PR-B and the short form PR-A. PR-A lacks the first 164 amino acid residues of PR-B (1,2). Both PR-A and PR-B are ligand activated, but differ in their relative ability to activate target gene transcription (3,4). The activity of PR is regulated by phosphorylation; at least seven serine residues are phosphorylated in its amino-terminal domain. Three sites (Ser81, Ser102, and Ser162) are unique to full length PR-B, while other sites (Ser190, Ser294, Ser345, and Ser400) are shared by both isoforms (5). Phosphorylation of PR-B at Ser190 (equivalent to Ser26 of PR-A) is catalyzed by CDK2 (6). Mutation of Ser190 results in decreased activity of PR (7), suggesting that the phosphorylation at Ser190 may be critical to its biological function.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Chromatin IP, Chromatin IP-seq, Western Blotting

Background: The estrogen-related receptor (ERR) subfamily of orphan nuclear receptors include three protein receptors, ERRα/NR3B1, ERRβ/NR3B2, and ERRγ/NR3B3, that have yet to be associated with natural ligands. PGC-1 coactivators regulate ERR transcription activation ability and receptor-induced transcription of genes involved in lipid metabolism, glucose metabolism, and mitochondrial biogenesis (1).

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Chromatin IP, Chromatin IP-seq, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: The orphan nuclear receptor, steroidogenic factor 1 (STF-1, also called Ad4BP), is encoded by the NR5A1 gene and plays an instrumental role in directing the transcriptional control of steroidogenesis (1). Initially identified as a tissue-specific transcriptional regulator of cytochrome P450 steroid hydroxylases, research studies of both global (2) and tissue-specific knockout mice (3-6) have demonstrated that STF-1 is required for the development of adrenal glands, gonads, ventromedial hypothalamus, and for the proper functioning of pituitary gonadotropes. Indeed, humans with mutations that render STF-1 transcriptionally inactive can present with testicular failure, ovarian failure, and adrenal insufficiency (7,8). Furthermore, dysregulation of STF-1 has been linked to diseases such as endometriosis (9) and adrenocortical carcinoma (10).Like other nuclear hormone receptors, STF-1 has a modular domain structure composed of an amino-terminal zinc finger DNA-binding domain, a ligand-binding domain, a carboxy-terminal AF-2 activation domain, and a hinge region with AF-1-like activation activity. STF-1 also contains a fushi tarazu factor 1 box, which functions as an accessory DNA binding domain (11). STF-1 is primarily phosphorylated at Ser203, which is thought to enhance its transcriptional activity by promoting complex formation with transcriptional cofactors (12). In addition to phosphorylation at Ser203, STF-1 is subject to SUMO conjugation and acetylation at ε-amino groups of target lysine residues. Whereas SUMOylation represses STF-1 function (13,14), acetylation enhances its transcriptional activity (15).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Chromatin IP, Chromatin IP-seq, Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: The Stat3 transcription factor is an important signaling molecule for many cytokines and growth factor receptors (1) and is required for murine fetal development (2). Research studies have shown that Stat3 is constitutively activated in a number of human tumors (3,4) and possesses oncogenic potential (5) and anti-apoptotic activities (3). Stat3 is activated by phosphorylation at Tyr705, which induces dimerization, nuclear translocation, and DNA binding (6,7). Transcriptional activation seems to be regulated by phosphorylation at Ser727 through the MAPK or mTOR pathways (8,9). Stat3 isoform expression appears to reflect biological function as the relative expression levels of Stat3α (86 kDa) and Stat3β (79 kDa) depend on cell type, ligand exposure, or cell maturation stage (10). It is notable that Stat3β lacks the serine phosphorylation site within the carboxy-terminal transcriptional activation domain (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Reverse orientation c-erbA gene α (Rev-erbα, EAR-1, or NR1D1) is a widely expressed member of the orphan nuclear receptor family of proteins (1). Rev-erbα is highly expressed in adipose tissue, skeletal muscle, brain and liver, and regulates cellular proliferation and differentiation. Expression increases during differentiation in adipocytes and ectopic expression of Rev-erbα potentiates the adipocyte differentiation of 3T3-L1 cells (2). In addition, expression oscillates with circadian rhythm in liver cells and Rev-erbα regulates expression of BMAL1, ApoA-I and ApoC-III, all key regulators of circadian rhythm (3-7). Phosphorylation of Rev-erbα Ser55 and Ser59 by GSK-3β appears to stabilize Rev-erbα protein levels and is important for synchronizing and maintaining the circadian clock (8). Rev-erbα also regulates inflammation by targeting the NF-κB responsive genes IL-6 and COX-2 (9). Rev-erbα lacks the activation function 2 domain required for ligand-dependent activation of transcription by other members of the nuclear receptor family; thus it behaves as a constitutive repressor protein, recruiting the nuclear receptor co-repressor (N-CoR)/HDAC3 complex to target genes to repress transcription (10).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Androgen receptor (AR), a zinc finger transcription factor belonging to the nuclear receptor superfamily, is activated by phosphorylation and dimerization upon ligand binding (1). This promotes nuclear localization and binding of AR to androgen response elements in androgen target genes. Research studies have shown that AR plays a crucial role in several stages of male development and the progression of prostate cancer (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: The aryl hydrocarbon receptor (AhR) is a ligand activated transcription factor involved in xenobiotic metabolism, cell cycle regulation, and development in response to both endogenous and environmental signals (1,2). AhR was initially identified as a receptor for dioxins, which are environmental pollutants generated by waste incineration and other industrial processes (3,4). AhR ligands include polycyclic aromatic hydrocarbons, including the carcinogen benzo(a)pyrene and other components of cigarette smoke (3,4). Naturally occurring AhR ligands include flavonoids, which are aromatic plant secondary compounds commonly found in vegetables and fruits (3). Cytoplasmic aryl hydrocarbon receptors are found in protein complexes with heat shock proteins. Upon ligand binding, AhR dissociates from heat shock proteins and translocate to the nucleus where it dimerizes with AhR nuclear translocator (ARNT, HIF-1β). The AhR/ARNT heterodimer binds to nuclear xenobiotic response elements to control the expression of genes associated with xenobiotic metabolism, including several cytochrome P450 genes (5,6). AhR is ubiquitously expressed and is thought to play a role in regulation of cell proliferation and differentiation, cytokine expression, and xenobiotic metabolism (2). Research studies link AhR activity with the control of regulatory T-cell and T-helper 17 cell differentiation, regulation of the inflammatory response, and the onset of lung cancer (1,2,7,8).

$260
100 µl
REACTIVITY
Human

Background: Androgen receptor (AR), a zinc finger transcription factor belonging to the nuclear receptor superfamily, is activated by phosphorylation and dimerization upon ligand binding (1). This promotes nuclear localization and binding of AR to androgen response elements in androgen target genes. Research studies have shown that AR plays a crucial role in several stages of male development and the progression of prostate cancer (2,3).

$134
20 µl
$336
100 µl
$792
300 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Chromatin IP, Chromatin IP-seq, Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Frozen), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: The Stat3 transcription factor is an important signaling molecule for many cytokines and growth factor receptors (1) and is required for murine fetal development (2). Research studies have shown that Stat3 is constitutively activated in a number of human tumors (3,4) and possesses oncogenic potential (5) and anti-apoptotic activities (3). Stat3 is activated by phosphorylation at Tyr705, which induces dimerization, nuclear translocation, and DNA binding (6,7). Transcriptional activation seems to be regulated by phosphorylation at Ser727 through the MAPK or mTOR pathways (8,9). Stat3 isoform expression appears to reflect biological function as the relative expression levels of Stat3α (86 kDa) and Stat3β (79 kDa) depend on cell type, ligand exposure, or cell maturation stage (10). It is notable that Stat3β lacks the serine phosphorylation site within the carboxy-terminal transcriptional activation domain (8).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Chromatin IP, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Western Blotting

Background: Peroxisome proliferator-activated receptor γ (PPARγ) is a member of the ligand-activated nuclear receptor superfamily and functions as a transcriptional activator (1). PPARγ is preferentially expressed in adipocytes as well as in vascular smooth muscle cells and macrophage (2). Besides its role in mediating adipogenesis and lipid metabolism (2), PPARγ also modulates insulin sensitivity, cell proliferation and inflammation (3). PPARγ transcriptional activity is inhibited by MAP kinase phosphorylation of PPARγ at Ser84 (4,5).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Chromatin IP, Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: The Stat3 transcription factor is an important signaling molecule for many cytokines and growth factor receptors (1) and is required for murine fetal development (2). Research studies have shown that Stat3 is constitutively activated in a number of human tumors (3,4) and possesses oncogenic potential (5) and anti-apoptotic activities (3). Stat3 is activated by phosphorylation at Tyr705, which induces dimerization, nuclear translocation, and DNA binding (6,7). Transcriptional activation seems to be regulated by phosphorylation at Ser727 through the MAPK or mTOR pathways (8,9). Stat3 isoform expression appears to reflect biological function as the relative expression levels of Stat3α (86 kDa) and Stat3β (79 kDa) depend on cell type, ligand exposure, or cell maturation stage (10). It is notable that Stat3β lacks the serine phosphorylation site within the carboxy-terminal transcriptional activation domain (8).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: The Stat3 transcription factor is an important signaling molecule for many cytokines and growth factor receptors (1) and is required for murine fetal development (2). Research studies have shown that Stat3 is constitutively activated in a number of human tumors (3,4) and possesses oncogenic potential (5) and anti-apoptotic activities (3). Stat3 is activated by phosphorylation at Tyr705, which induces dimerization, nuclear translocation, and DNA binding (6,7). Transcriptional activation seems to be regulated by phosphorylation at Ser727 through the MAPK or mTOR pathways (8,9). Stat3 isoform expression appears to reflect biological function as the relative expression levels of Stat3α (86 kDa) and Stat3β (79 kDa) depend on cell type, ligand exposure, or cell maturation stage (10). It is notable that Stat3β lacks the serine phosphorylation site within the carboxy-terminal transcriptional activation domain (8).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Application Methods: Chromatin IP, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: The Stat3 transcription factor is an important signaling molecule for many cytokines and growth factor receptors (1) and is required for murine fetal development (2). Research studies have shown that Stat3 is constitutively activated in a number of human tumors (3,4) and possesses oncogenic potential (5) and anti-apoptotic activities (3). Stat3 is activated by phosphorylation at Tyr705, which induces dimerization, nuclear translocation, and DNA binding (6,7). Transcriptional activation seems to be regulated by phosphorylation at Ser727 through the MAPK or mTOR pathways (8,9). Stat3 isoform expression appears to reflect biological function as the relative expression levels of Stat3α (86 kDa) and Stat3β (79 kDa) depend on cell type, ligand exposure, or cell maturation stage (10). It is notable that Stat3β lacks the serine phosphorylation site within the carboxy-terminal transcriptional activation domain (8).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunoprecipitation

Background: The Stat3 transcription factor is an important signaling molecule for many cytokines and growth factor receptors (1) and is required for murine fetal development (2). Research studies have shown that Stat3 is constitutively activated in a number of human tumors (3,4) and possesses oncogenic potential (5) and anti-apoptotic activities (3). Stat3 is activated by phosphorylation at Tyr705, which induces dimerization, nuclear translocation, and DNA binding (6,7). Transcriptional activation seems to be regulated by phosphorylation at Ser727 through the MAPK or mTOR pathways (8,9). Stat3 isoform expression appears to reflect biological function as the relative expression levels of Stat3α (86 kDa) and Stat3β (79 kDa) depend on cell type, ligand exposure, or cell maturation stage (10). It is notable that Stat3β lacks the serine phosphorylation site within the carboxy-terminal transcriptional activation domain (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Chromatin IP, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Peroxisome proliferator-activated receptor γ (PPARγ) is a member of the ligand-activated nuclear receptor superfamily and functions as a transcriptional activator (1). PPARγ is preferentially expressed in adipocytes as well as in vascular smooth muscle cells and macrophage (2). Besides its role in mediating adipogenesis and lipid metabolism (2), PPARγ also modulates insulin sensitivity, cell proliferation and inflammation (3). PPARγ transcriptional activity is inhibited by MAP kinase phosphorylation of PPARγ at Ser84 (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: The human retinoid X receptors (RXRs) are encoded by three distinct genes (RXRα, RXRβ, and RXRγ) and bind selectively and with high affinity to the vitamin A derivative, 9-cis-retinoic acid. RXRs are type-II nuclear hormone receptors that are largely localized to the nuclear compartment independent of ligand binding. Nuclear RXRs form heterodimers with nuclear hormone receptor subfamily 1 proteins, including thyroid hormone receptor, retinoic acid receptors, vitamin D receptor, peroxisome proliferator-activated receptors, liver X receptors, and farnesoid X receptor (1). Since RXRs heterodimerize with multiple nuclear hormone receptors, they play a central role in transcriptional control of numerous hormonal signaling pathways by binding to cis-acting response elements in the promoter/enhancer region of target genes (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Chromatin IP, Chromatin IP-seq, Immunoprecipitation, Western Blotting

Background: There are three members of the steroid receptor co-activator (SRC) family of proteins: SRC-1 (NCoA-1), SRC-2 (TIF2/GRIP1/NCoA-2), and SRC-3 (ACTR/pCIP/RAC3/TRAM-1/AIB1). All SRC family members share significant structural homology and function to stimulate transcription mediated by nuclear hormone receptors and other transcriptional activators such as Stat3, NF-κB, E2F1, and p53 (1-4). Two SRC proteins, SRC-1 and SRC-3, function as histone acetyltransferases (5,6). In addition, all three family members can recruit other histone acetyltransferases (CBP/p300, PCAF) and histone methyltransferases (PRMT1, CARM1) to target promoters and cooperate to enhance expression of many genes (5-8). The SRC proteins play important roles in multiple physiological processes including cell proliferation, cell survival, somatic cell growth, mammary gland development, female reproductive function, and vasoprotection (9). SRC-1 and SRC-3 are conduits for kinase-mediated growth factor signaling to the estrogen receptor and other transcriptional activators. Seven SRC-1 phosphorylation sites and six SRC-3 phosphorylation sites have been identified, which are induced by steroids, cytokines, and growth factors and involve multiple kinase signaling pathways (9-11). Research has shown that all three SRC family members are associated with increased activity of nuclear receptors in breast, prostate, and ovarian carcinomas. According to the literature, SRC-3 is frequently amplified or overexpressed in a number of cancers (12), and SRC-1/PAX3 and SRC-2/MYST3 translocations are found associated with rhabdomyosarcoma and acute myeloid leukemia, respectively (13,14).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Chromatin IP, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: There are three members of the steroid receptor co-activator (SRC) family of proteins: SRC-1 (NCoA-1), SRC-2 (TIF2/GRIP1/NCoA-2), and SRC-3 (ACTR/pCIP/RAC3/TRAM-1/AIB1). All SRC family members share significant structural homology and function to stimulate transcription mediated by nuclear hormone receptors and other transcriptional activators such as Stat3, NF-κB, E2F1, and p53 (1-4). Two SRC proteins, SRC-1 and SRC-3, function as histone acetyltransferases (5,6). In addition, all three family members can recruit other histone acetyltransferases (CBP/p300, PCAF) and histone methyltransferases (PRMT1, CARM1) to target promoters and cooperate to enhance expression of many genes (5-8). The SRC proteins play important roles in multiple physiological processes including cell proliferation, cell survival, somatic cell growth, mammary gland development, female reproductive function, and vasoprotection (9). SRC-1 and SRC-3 are conduits for kinase-mediated growth factor signaling to the estrogen receptor and other transcriptional activators. Seven SRC-1 phosphorylation sites and six SRC-3 phosphorylation sites have been identified, which are induced by steroids, cytokines, and growth factors and involve multiple kinase signaling pathways (9-11). Research has shown that all three SRC family members are associated with increased activity of nuclear receptors in breast, prostate, and ovarian carcinomas. According to the literature, SRC-3 is frequently amplified or overexpressed in a number of cancers (12), and SRC-1/PAX3 and SRC-2/MYST3 translocations are found associated with rhabdomyosarcoma and acute myeloid leukemia, respectively (13,14).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Chromatin IP, Western Blotting

Background: There are three members of the steroid receptor co-activator (SRC) family of proteins: SRC-1 (NCoA-1), SRC-2 (TIF2/GRIP1/NCoA-2), and SRC-3 (ACTR/pCIP/RAC3/TRAM-1/AIB1). All SRC family members share significant structural homology and function to stimulate transcription mediated by nuclear hormone receptors and other transcriptional activators such as Stat3, NF-κB, E2F1, and p53 (1-4). Two SRC proteins, SRC-1 and SRC-3, function as histone acetyltransferases (5,6). In addition, all three family members can recruit other histone acetyltransferases (CBP/p300, PCAF) and histone methyltransferases (PRMT1, CARM1) to target promoters and cooperate to enhance expression of many genes (5-8). The SRC proteins play important roles in multiple physiological processes including cell proliferation, cell survival, somatic cell growth, mammary gland development, female reproductive function, and vasoprotection (9). SRC-1 and SRC-3 are conduits for kinase-mediated growth factor signaling to the estrogen receptor and other transcriptional activators. Seven SRC-1 phosphorylation sites and six SRC-3 phosphorylation sites have been identified, which are induced by steroids, cytokines, and growth factors and involve multiple kinase signaling pathways (9-11). Research has shown that all three SRC family members are associated with increased activity of nuclear receptors in breast, prostate, and ovarian carcinomas. According to the literature, SRC-3 is frequently amplified or overexpressed in a number of cancers (12), and SRC-1/PAX3 and SRC-2/MYST3 translocations are found associated with rhabdomyosarcoma and acute myeloid leukemia, respectively (13,14).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Chromatin IP, Chromatin IP-seq, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: ATP-dependent chromatin remodeling complexes play an essential role in the regulation of nuclear processes such as transcription and DNA replication and repair (1,2). The SWI/SNF chromatin remodeling complex consists of more than 10 subunits and contains a single molecule of either BRM or BRG1 as the ATPase catalytic subunit. The activity of the ATPase subunit disrupts histone-DNA contacts and changes the accessibility of crucial regulatory elements to the chromatin. The additional core and accessory subunits play a scaffolding role to maintain stability and provide surfaces for interaction with various transcription factors and chromatin (2-5). The interactions between SWI/SNF subunits and transcription factors, such as nuclear receptors, p53, Rb, BRCA1, and MyoD, facilitate recruitment of the complex to target genes for regulation of gene activation, cell growth, cell cycle, and differentiation processes (1,6-9).