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Human sin3 Complex

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: SIN3 was originally identified as a negative regulator of transcription in budding yeast (1,2). Since then, three isoforms of the SIN3 proteins have been identified in mammalian cells, as products of two different genes, SIN3A and SIN3B (3,4). Both SIN3A and SIN3B are nuclear proteins that function as scaffolding subunits for the multi-subunit SIN3 transcriptional repressor complex, containing SIN3A or SIN3B, HDAC1, HDAC2, SDS3, RBBP4/RBAP48, RBBP7/RBAP46, SAP30, and SAP18 (3,4). SIN3 proteins contain four paired amphipathic alpha-helix (PAH) motifs that function in the recruitment of the SIN3 complex to target genes by binding a multitude of DNA-binding transcriptional repressor proteins, including Mad1, p53, E2F4, HCF-1, AML1, Elk-1, NRSF, CTCF, ERα, and MeCP2 (3,4). In addition, SIN3 proteins contain an HDAC interaction domain (HID), which mediates binding of HDAC1 and HDAC2 via the SDS3 bridging protein, and a highly conserved region (HCR) at the carboxy terminus, which contributes to repressor protein binding (3,4). RBBP4 and RBBP7 proteins also bind to SDS3 and contribute to nucleosome binding of the complex. The SIN3 complex functions to repress transcription, in part, by deacetylating histones at target gene promoters (3,4). In addition, recent studies have shown that SIN3 is recruited to the coding regions of repressed and active genes, where it deacetylates histones and suppresses spurious transcription by RNA polymerase II (3,5). In addition to histone deacetylase activity, the SIN3 complex associates with histone methyltransferase (ESET), histone demethylase (JARID1A/RBP2), ATP-dependent chromatin remodeling (SWI/SNF), methylcytosine dioxygenase (TET1), and O-GlcNAc transferase (OGT) activities, all of which appear to contribute to the regulation of target genes (5-9). The SIN3 complex is critical for proper regulation of embryonic development, cell growth and proliferation, apoptosis, DNA replication, DNA repair, and DNA methylation (imprinting and X-chromosome inactivation) (3,4).

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

Application Methods: Chromatin IP, Western Blotting

Background: SIN3 was originally identified as a negative regulator of transcription in budding yeast (1,2). Since then, three isoforms of the SIN3 proteins have been identified in mammalian cells, as products of two different genes, SIN3A and SIN3B (3,4). Both SIN3A and SIN3B are nuclear proteins that function as scaffolding subunits for the multi-subunit SIN3 transcriptional repressor complex, containing SIN3A or SIN3B, HDAC1, HDAC2, SDS3, RBBP4/RBAP48, RBBP7/RBAP46, SAP30, and SAP18 (3,4). SIN3 proteins contain four paired amphipathic alpha-helix (PAH) motifs that function in the recruitment of the SIN3 complex to target genes by binding a multitude of DNA-binding transcriptional repressor proteins, including Mad1, p53, E2F4, HCF-1, AML1, Elk-1, NRSF, CTCF, ERα, and MeCP2 (3,4). In addition, SIN3 proteins contain an HDAC interaction domain (HID), which mediates binding of HDAC1 and HDAC2 via the SDS3 bridging protein, and a highly conserved region (HCR) at the carboxy terminus, which contributes to repressor protein binding (3,4). RBBP4 and RBBP7 proteins also bind to SDS3 and contribute to nucleosome binding of the complex. The SIN3 complex functions to repress transcription, in part, by deacetylating histones at target gene promoters (3,4). In addition, recent studies have shown that SIN3 is recruited to the coding regions of repressed and active genes, where it deacetylates histones and suppresses spurious transcription by RNA polymerase II (3,5). In addition to histone deacetylase activity, the SIN3 complex associates with histone methyltransferase (ESET), histone demethylase (JARID1A/RBP2), ATP-dependent chromatin remodeling (SWI/SNF), methylcytosine dioxygenase (TET1), and O-GlcNAc transferase (OGT) activities, all of which appear to contribute to the regulation of target genes (5-9). The SIN3 complex is critical for proper regulation of embryonic development, cell growth and proliferation, apoptosis, DNA replication, DNA repair, and DNA methylation (imprinting and X-chromosome inactivation) (3,4).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).

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

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

Background: Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).

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

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

Background: Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).

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

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

Background: Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).

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

Application Methods: Western Blotting

Background: Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).

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

Application Methods: Western Blotting

Background: CK2 (formerly called Casein Kinase II) is a highly conserved protein kinase with more than 300 substrates regulating cell growth, cell death, and cell survival. CK2 has been implicated in the response to UV irradiation-induced DNA damage, targeting XRCC1 (1) and BRCA1 (2) as well as regulating p53 tumor suppressor protein functions (3). Furthermore, CK2 plays a key role in NF-κB activation (4). UV irradiation stimulates CK2-mediated phosphorylation of several carboxy-terminal residues within IκBα, resulting in IκBα proteasomal degradation and the release and nuclear translocation of active NF-κB. CK2 is also dysregulated in many cancers (5) and neurodegenerative diseases such as Alzheimer's and Parkinson's diseases (6). Structurally, CK2 is a multimeric protein complex consisting of two catalytic subunits (α or α') and two regulatory β subunits (7). CK2 is distributed ubiquitously and is apparently constitutively active (7). While cell cycle-dependent Ser-Pro phosphorylation sites have been identified on CK2α and CK2β, Tyr255 phosphorylation by the Src-related kinase c-Fgr seems to have the greatest effect on CK2α activity (8,9).

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

Application Methods: Western Blotting

Background: Retinoblastoma-associated proteins 46 and 48 (RBAP46 and RBAP48; also known as RBBP7 and RBBP4) were first characterized in human cells as proteins that bind to the retinoblastoma (Rb) tumor suppressor protein (1). Since then, these proteins have been shown to be components of many protein complexes involved in chromatin regulation, including the chromatin assembly factor 1 (CAF-1) complex and type B histone acetyltransferase complex HAT1, both of which function in chromatin assembly during DNA replication (2,3). RBAP46 and RBAP48 are also found in the nucleosome remodeling factor complex NURF, the nucleosome remodeling and histone de-acetylation complex NuRD, and the Sin3/HDAC histone de-acetylation complex (4-7). More recently, RBAP46 and RBAP48 were identified as components of the polycomb repressor complex PRC2, which also contains EED and Ezh2 (8). RBAP46 and RBAP48 bind to the histone fold region of histone H4 and are believed to target these chromatin remodeling, histone acetylation, and histone de-acetylation complexes to their histone substrates (3).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).

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

Application Methods: Western Blotting

Background: The most well characterized nuclear receptor corepressors are SMRT (silencing mediator for retinoic acid and thyroid hormone receptors) and its close paralog NCoR1 (nuclear receptor corepressor) (1,2). NCoR1 functions to transcriptionally silence various unliganded, DNA bound non-steroidal nuclear receptors by serving as a large molecular scaffold that bridges the receptors with multiple chromatin remodeling factors that repress nuclear receptor-mediated gene transcription, in part, through deacetylation of core histones surrounding target promoters. Indeed, the N-terminal portion of NCoR1 possesses multiple distinct transcriptional repression domains (RDs) reponsible for the recruitment of additional components of the corepressor complex such as HDACs, mSin3, GPS2, and TBL1/TBLR1. In between the RDs lies a pair of potent repressor motifs known as SANT motifs (SWI3, ADA2, N-CoR, and TFIIIB), which recruit HDAC3 and histones to the repressor complex in order to enhance HDAC3 activity (3). The C-terminal portion of NCoR1 contains multiple nuclear receptor interaction domains (NDs), each of which contains a conserved CoRNR box (or L/I-X-X-I/V-I) motif that allow for binding to various unliganded nuclear hormone receptors such as thyroid hormone (THR) and retinoic acid (RAR) receptors (4,5).Recent genetic studies in mice have not only corroborated the wealth of biochemical studies involving NCoR1 but have also provided significant insight regarding the function of NCoR1 in mammalian development and physiology. Although it has been observed that loss of Ncor1 does not affect early embyonic development, likely due to compensation by Smrt, embryonic lethality ultimately results during mid-gestation, largely due to defects in erythropoesis and thymopoesis (6). Another study demonstrated that the NDs of NCoR1 are critical for its ability to function in a physiological setting as a transcriptional repressor of hepatic THR and Liver X Receptor (LXR) (7).

$262
3 nmol
300 µl
SignalSilence® CK2α siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit CK2α expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products from CST are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Human

Background: CK2 (formerly called Casein Kinase II) is a highly conserved protein kinase with more than 300 substrates regulating cell growth, cell death, and cell survival. CK2 has been implicated in the response to UV irradiation-induced DNA damage, targeting XRCC1 (1) and BRCA1 (2) as well as regulating p53 tumor suppressor protein functions (3). Furthermore, CK2 plays a key role in NF-κB activation (4). UV irradiation stimulates CK2-mediated phosphorylation of several carboxy-terminal residues within IκBα, resulting in IκBα proteasomal degradation and the release and nuclear translocation of active NF-κB. CK2 is also dysregulated in many cancers (5) and neurodegenerative diseases such as Alzheimer's and Parkinson's diseases (6). Structurally, CK2 is a multimeric protein complex consisting of two catalytic subunits (α or α') and two regulatory β subunits (7). CK2 is distributed ubiquitously and is apparently constitutively active (7). While cell cycle-dependent Ser-Pro phosphorylation sites have been identified on CK2α and CK2β, Tyr255 phosphorylation by the Src-related kinase c-Fgr seems to have the greatest effect on CK2α activity (8,9).

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

Application Methods: Western Blotting

Background: Retinoblastoma-associated proteins 46 and 48 (RBAP46 and RBAP48; also known as RBBP7 and RBBP4) were first characterized in human cells as proteins that bind to the retinoblastoma (Rb) tumor suppressor protein (1). Since then, these proteins have been shown to be components of many protein complexes involved in chromatin regulation, including the chromatin assembly factor 1 (CAF-1) complex and type B histone acetyltransferase complex HAT1, both of which function in chromatin assembly during DNA replication (2,3). RBAP46 and RBAP48 are also found in the nucleosome remodeling factor complex NURF, the nucleosome remodeling and histone de-acetylation complex NuRD, and the Sin3/HDAC histone de-acetylation complex (4-7). More recently, RBAP46 and RBAP48 were identified as components of the polycomb repressor complex PRC2, which also contains EED and Ezh2 (8). RBAP46 and RBAP48 bind to the histone fold region of histone H4 and are believed to target these chromatin remodeling, histone acetylation, and histone de-acetylation complexes to their histone substrates (3).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated HDAC1 (10E2) Mouse mAb #5356.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The most well characterized nuclear receptor corepressors are SMRT (silencing mediator for retinoic acid and thyroid hormone receptors) and its close paralog NCoR1 (nuclear receptor corepressor) (1,2). NCoR1 functions to transcriptionally silence various unliganded, DNA bound non-steroidal nuclear receptors by serving as a large molecular scaffold that bridges the receptors with multiple chromatin remodeling factors that repress nuclear receptor-mediated gene transcription, in part, through deacetylation of core histones surrounding target promoters. Indeed, the N-terminal portion of NCoR1 possesses multiple distinct transcriptional repression domains (RDs) reponsible for the recruitment of additional components of the corepressor complex such as HDACs, mSin3, GPS2, and TBL1/TBLR1. In between the RDs lies a pair of potent repressor motifs known as SANT motifs (SWI3, ADA2, N-CoR, and TFIIIB), which recruit HDAC3 and histones to the repressor complex in order to enhance HDAC3 activity (3). The C-terminal portion of NCoR1 contains multiple nuclear receptor interaction domains (NDs), each of which contains a conserved CoRNR box (or L/I-X-X-I/V-I) motif that allow for binding to various unliganded nuclear hormone receptors such as thyroid hormone (THR) and retinoic acid (RAR) receptors (4,5).Recent genetic studies in mice have not only corroborated the wealth of biochemical studies involving NCoR1 but have also provided significant insight regarding the function of NCoR1 in mammalian development and physiology. Although it has been observed that loss of Ncor1 does not affect early embyonic development, likely due to compensation by Smrt, embryonic lethality ultimately results during mid-gestation, largely due to defects in erythropoesis and thymopoesis (6). Another study demonstrated that the NDs of NCoR1 are critical for its ability to function in a physiological setting as a transcriptional repressor of hepatic THR and Liver X Receptor (LXR) (7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Mortality factor 4-like protein 1 (MORF4L1/MRG15) is a chromo domain-containing protein that is part of several histone modifying complexes, including the Tip60 histone acetyltransferase (HAT) complex, histone deacetylase (HDAC) complexes, and the JARID1A and JARID1B histone demethylase complexes (1-6). MORF4L1/MRG15 recognizes di- or trimethylated Lys36 of histone H3 through its chromo domain. This interaction recruits and anchors MORF4L1/MRG15-associated chromatin modifying complexes to target genes for transcriptional regulation (7,8). MORF4L1/MRG15 plays a role in DNA repair as part of the Tip60 HAT complex (9,10). MORF4L1/MRG15 regulates alternative splicing during co-transcriptional splicing of mRNA as a part of the JARID1A complex (11). MORF4L1/MRG15 recruitment of the JARID1B complex to embryonic stem cell renewal-associated genes is important for repression of cryptic transcription and maintenance of proper transcriptional elongation (6).