20% off purchase of 3 or more products* | Learn More >>

Monoclonal Antibody Immunofluorescence Immunocytochemistry Chromatin Binding

$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).

$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: Heterochromatin protein 1 (HP1) is a family of heterochromatic adaptor molecules involved in both gene silencing and higher order chromatin structure (1). All three HP1 family members (α, β, and γ) are primarily associated with centromeric heterochromatin; however, HP1β and γ also localize to euchromatic sites in the genome (2,3). HP1 proteins are approximately 25 kDa in size and contain a conserved amino-terminal chromodomain, followed by a variable hinge region and a conserved carboxy-terminal chromoshadow domain. The chromodomain facilitates binding to histone H3 tri-methylated at Lys9, a histone "mark" closely associated with centromeric heterochromatin (4,5). The variable hinge region binds both RNA and DNA in a sequence-independent manner (6). The chromoshadow domain mediates the dimerization of HP1 proteins, in addition to binding multiple proteins implicated in gene silencing and heterochromatin formation, including the SUV39H histone methyltransferase, the DNMT1 and DNMT3a DNA methyltransferases, and the p150 subunit of chromatin-assembly factor-1 (CAF1) (7-9). In addition to contributing to heterochromatin formation and propagation, HP1 and SUV39H are also found complexed with retinoblastoma (Rb) and E2F6 proteins, both of which function to repress euchromatic gene transcription in quiescent cells (10,11). HP1 proteins are subject to multiple types of post-translational modifications, including phosphorylation, acetylation, methylation, ubiquitination, and sumoylation, suggesting multiple means of regulation (12-14).

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

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

Background: The polycomb group (PcG) proteins contribute to the maintenance of cell identity, stem cell self-renewal, cell cycle regulation and oncogenesis by maintaining the silenced state of genes that promote cell lineage specification, cell death and cell-cycle arrest (1-4). PcG proteins exist in two complexes that cooperate to maintain long-term gene silencing through epigenetic chromatin modifications. The first complex, EED-EZH2, is recruited to genes by DNA-binding transcription factors and methylates histone H3 on Lys27. Methylation of Lys27 facilitates the recruitment of the second complex, PRC1, which ubiquitinylates histone H2A on Lys119 (5). Embryonic ectoderm development protein (EED) is a component of the PRC2 complex, which together with Ezh2 and SUZ12 is absolutely required for histone methyl-transferase activity (6). EED, SUZ12 and EZH2 are overexpressed in various types of cancer, including tumors of the colon, breast, prostate and ovary (7-9).

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

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

Background: The cohesin complex consists of a heterodimer between SMC1 (SMC1A or B) and SMC3, bound by additional RAD21 and STAG proteins (STAG1, 2, or 3) (1,2). These proteins form a ring-like structure that mediates the cohesion of two sister chromatids after DNA replication in S phase (1,2). RAD21 and STAG2 are phosphorylated by Polo-like kinase (PLK) during prophase, which leads to the dissociation of cohesin complexes from the chromosome arms; however, cohesin remains bound to centromeres until anaphase (3,4). RAD21 is cleaved by separin/ESPL1 in anaphase, which leads to dissociation of the remaining cohesin from centromeres, enabling sister chromatids to segregate during mitosis (5). RAD21 is also cleaved by caspase-3 and caspase-7 during apoptosis, resulting in a 64 kDa carboxy-terminal cleavage product that translocates to the cytoplasm and may help to trigger apoptosis (6,7). In addition to mediating cohesion of sister chromatids, the cohesin complex plays important roles in gene regulation and DNA repair, as SMC1 and SMC3 are both phosphorylated by ATM and ATR kinases upon DNA damage (1,2).

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

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

Background: ATP-dependent chromatin remodeling complexes play an essential role in the regulation of various nuclear processes, such as gene expression, DNA replication, and repair (1,2). The SWI/SNF chromatin remodeling complex consists of more than 10 subunits with a single molecule of the ATPase catalytic subunit BRM or BRG1, but not both. The activities of these two subunits drive the disruption of histone-DNA contacts that lead to changes in accessibility of crucial regulatory elements within chromatin (2-5). The BRM/BRG1 containing SWI/SNF complexes are recruited to target promoters by transcription factors, such as nuclear receptors, p53, RB, and BRCA1 to regulate gene activation, cell growth, the cell cycle, and differentiation processes (1,6-9). BRM and BRG1 are also considered to be tumor suppressors and their expression levels are severely reduced in several cancer cell lines (10-13).

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

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

Background: The Silent Information Regulator (Sir2) family of genes is a highly conserved group of genes that encode nicotinamide adenine dinucleotide (NAD)-dependent protein deacetylases, also known as class III histone deacetylases. The first discovered and best characterized of this family is Saccharomyces cerevisiae Sir2, which is involved in silencing of mating type loci, telomere maintenance, DNA damage response, and cell aging (1). SirT6, a mammalian homolog of Sir2, is a nuclear, chromatin-associated protein that promotes the normal maintenance of genome integrity mediated by the base excision repair (BER) pathway (2-4). The BER pathway repairs single-stranded DNA lesions that arise spontaneously from endogenous alkylation, oxidation, and deamination events. SirT6 deficient mice show increased sensitivity to DNA-damaging agents, including the alkylating agents MMS and H2O2 (2). In addition, these mice show genome instability with increased frequency of fragmented chromosomes, detached centromeres, and gaps (2). SirT6 may regulate the BER pathway by deacetylating DNA Polβ or other core components of the pathway (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

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

Background: Ring1A plays a role in polycomb group (PcG) protein function. PcG proteins are critically involved in transcriptional repression of Hox genes during development (1,2). PcG proteins form two distinct complexes: EED-EZH2 and the PRC complex, which is composed of at least Bmi1 and Ring1A/Ring1B. The EZH2-containing complex is responsible for the methylation of H3K27, and the PRC complex ubiquitylates H2A. EZH2 methylation is required prior to PRC ubiquitylation, and both are essential for Hox gene repression (3). It has recently been shown that PcG proteins silence a group of developmentally important regulator genes, referred to as bivalent genes (4). This regulation may be responsible for the ability of stem cells to self renew or switch to differentiate into multipotent progenitors. Aberrant epigenetic silencing by PcG proteins is also thought to be important in tumorigenesis (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

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

Background: ASF1 was first identified in S. cerevisiae based on its ability to de-repress transcriptional silencing when overexpressed (1). While only one gene exists in yeast and Drosophila, mammalian cells contain the two highly homologous ASF1A and ASF1B genes (2). ASF1A and ASF1B function as histone chaperones, delivering histone H3/H4 dimers to CAF-1 or HIRA histone deposition complexes to facilitate replication-coupled and replication-independent nucleosome assembly on DNA (2-5). Both ASF1A and ASF1B bind to CAF-1, but only ASF1A binds to HIRA (5). In addition to playing a role in DNA replication and gene silencing, ASF1 functions in DNA damage repair, genome stability and cellular senescence. Deletion of ASF1 in yeast and Drosophila confers sensitivity to various DNA damaging agents and inhibitors of DNA replication, increases genomic instability and sister chromatid exchange, and activates the DNA damage checkpoint (6-8). Depletion of both ASF1A and ASF1B in mammalian cells results in the accumulation of cells in S phase, increased phosphorylation of H2A.X, centrosome amplification and apoptosis (9,10). ASF1A is required for the formation of senescence-associated heterochromatin foci (SAHF), with overexpression of ASF1A inducing senescence in primary cells (4). Both ASF1A and ASF1B are phosphorylated in S phase by the Tousled-like kinases TLK1 and TLK2, and are dephosphorylated when TLK1 and TLK2 are inactivated by Chk1 kinase in response to replicative stress (11,12). The function of ASF1 phosphorylation is not yet understood.

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

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

Background: The polycomb group (PcG) proteins are involved in maintaining the silenced state of several developmentally regulated genes and contribute to the maintenance of cell identity, cell cycle regulation, and oncogenesis (1,2). Enhancer of zeste homolog 2 (Ezh2), a member of this large protein family, contains four conserved regions including domain I, domain II, and a cysteine-rich amino acid stretch that precedes the carboxy-terminal SET domain (3). The SET domain has been linked with histone methyltransferase (HMTase) activity. Moreover, mammalian Ezh2 is a member of a histone deacetylase complex that functions in gene silencing, acting at the level of chromatin structure (4). Ezh2 complexes methylate histone H3 at Lys9 and 27 in vitro, which is thought to be involved in targeting transcriptional regulators to specific loci (5). Ezh2 is deregulated in various tumor types, and its role, both as a primary effector and as a mediator of tumorigenesis, has become a subject of increased interest (6).

$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: The polycomb group (PcG) proteins contribute to the maintenance of cell identity, stem cell self-renewal, cell-cycle regulation, and oncogenesis by maintaining the silenced state of genes that promote cell lineage specification, cell death, and cell-cycle arrest (1-4). PcG proteins exist in two complexes that cooperate to maintain long-term gene silencing through epigenetic chromatin modifications. The first complex, Eed-Ezh2, is recruited to genes by DNA-binding transcription factors and methylates histone H3 on Lys27. This histone methyltransferase activity requires the Ezh2, Eed, and Suz12 subunits of the complex (5). Methylation of Lys27 facilitates the recruitment of the second complex, PRC1, which ubiquitinates histone H2A on Lys119 (6). PRC1 is composed of Bmi1 and RING1A (also RING1 or RNF1), both of which act to enhance the E3 ubiquitin ligase activity of an additional catalytic subunit RING1B (also RING2 or RNF2) (7). PcG proteins play an important role in the regulation of cell proliferation and senescence through repression of the p16 INK4A and p19 ARF genes and are required for maintenance of adult hematopoietic and neural stem cells, as well as embryonic stem cells (3,4,8-10).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

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

Background: YAP (Yes-associated protein, YAP65) was identified based on its ability to associate with the SH3 domain of Yes. It also binds to other SH3 domain-containing proteins such as Nck, Crk, Src, and Abl (1). In addition to the SH3 binding motif, YAP contains a PDZ interaction motif, a coiled-coil domain, and WW domains (2-4). While initial studies of YAP all pointed towards a role in anchoring and targeting to specific subcellular compartments, subsequent studies showed that YAP is a transcriptional co-activator by virtue of its WW domain interacting with the PY motif (PPxY) of the transcription factor PEBP2 and other transcription factors (5). In its capacity as a transcriptional co-activator, YAP is now widely recognized as a central mediator of the Hippo Pathway, which plays a fundamental and widely conserved role in regulating tissue growth and organ size. Phosphorylation at multiple sites (e.g., Ser109, Ser127) by LATS kinases promotes YAP translocation from the nucleus to the cytoplasm, where it is sequestered through association with 14-3-3 proteins (6-8). These LATS-driven phosphorylation events serve to prime YAP for subsequent phosphorylation by CK1δ/ε in an adjacent phosphodegron, triggering proteosomal degradation of YAP (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: The LEDGF (lens epithelium-derived growth factor) gene encodes splice variants P75 and P52 (1). LEDGF (C57G11) Rabbit mAb detects the 75 kDA LEDGF splice form. Both LEDGF variants have transcriptional coactivator functions that may regulate gene transcription and mRNA splicing of a variety of proteins that are essential for cell growth and survival. (2,3). LEDGF has also been identified as a factor that can, in serum free media, stimulate the growth and survival of lens epithelial cells and other cell types such as retinal photoreceptor cells, COS7 cells, skin fibroblasts, and keratinocytes (2). In addition to its function as a transcriptional coactivator, LEDGF has been shown to be involved in the pathogenesis of atopic dermatitis (4) and in the activity of HIV1 integrase. LEDGF binds chromatin throughout the cell cycle, and may act as a chromatin docking factor for HIV integrase and other lentiviral pre-integration complexes. It protects HIV integrase from degradation, and influences the pattern of viral integration into the cell genome (5).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The polycomb group (PcG) proteins are involved in maintaining the silenced state of several developmentally regulated genes and contribute to the maintenance of cell identity, cell cycle regulation, and oncogenesis (1,2). Enhancer of zeste homolog 2 (Ezh2), a member of this large protein family, contains four conserved regions including domain I, domain II, and a cysteine-rich amino acid stretch that precedes the carboxy-terminal SET domain (3). The SET domain has been linked with histone methyltransferase (HMTase) activity. Moreover, mammalian Ezh2 is a member of a histone deacetylase complex that functions in gene silencing, acting at the level of chromatin structure (4). Ezh2 complexes methylate histone H3 at Lys9 and 27 in vitro, which is thought to be involved in targeting transcriptional regulators to specific loci (5). Ezh2 is deregulated in various tumor types, and its role, both as a primary effector and as a mediator of tumorigenesis, has become a subject of increased interest (6).

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

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

Background: The polycomb group (PcG) proteins contribute to the maintenance of cell identity, stem cell self-renewal, cell cycle regulation and oncogenesis by maintaining the silenced state of genes that promote cell lineage specification, cell death and cell-cycle arrest (1-4). PcG proteins exist in two complexes that cooperate to maintain long-term gene silencing through epigenetic chromatin modifications. The first complex, EED-EZH2, is recruited to genes by DNA-binding transcription factors and methylates histone H3 on Lys27. Methylation of Lys27 facilitates the recruitment of the second complex, PRC1, which ubiquitinylates histone H2A on Lys119 (5). Suppressor of Zeste 12 (SUZ12) is a component of the PRC2 complex, which together with Ezh2 and Eed is absolutely required for histone methyl-transferase activity (6). SUZ12 contains a C2H2 zinc finger domain similar to the zinc finger domains found in sequence-specific DNA binding proteins and may mediate the interaction between EZH2 and nucleosomes (6). SUZ12 is overexpressed in several human tumors, including tumors of the colon, breast and liver (7,8).

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Chromatin assembly factor 1 (CAF-1) is a histone H3/H4 chaperone complex that functions in de novo assembly of nucleosomes during DNA replication and nucleotide excision repair (1). Nucleosome assembly is a two-step process, involving initial deposition of a histone H3/H4 tetramer onto DNA, followed by the deposition of a pair of histone H2A/H2B dimers (1). CAF-1 interacts with PCNA and localizes to DNA replication and DNA repair foci, where it functions to assemble newly synthesized histone H3/H4 tetramers onto replicating DNA (2-6). Assembly of histone H2A/H2B dimers requires additional assembly factors. The CAF-1 complex consists of three proteins: CHAF1A (p150), CHAF1B (p60) and RBAP48 (p48 or RBBP4). CHAF1A and CHAF1B proteins are specific for the CAF-1 complex, while RBAP48 is a component of multiple chromatin modifying complexes (1). CHAF1A and CHAF1B expression levels correlate with cellular proliferation and both proteins are significantly down-regulated in quiescent cells (7).

$269
100 µl
APPLICATIONS
REACTIVITY
Bovine, Dog, Human, Monkey, Mouse, Pig, Rat

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

Background: All organisms respond to increased temperatures and other environmental stresses by rapidly inducing the expression of highly conserved heat shock proteins (HSPs) that serve as molecular chaperones to refold denatured proteins and promote the degradation of damaged proteins. Heat shock gene transcription is regulated by a family of heat shock factors (HSFs), transcriptional activators that bind to heat shock response elements (HSEs) located upstream of all heat shock genes (1). HSEs are highly conserved among organisms and contain multiple adjacent and inverse iterations of the pentanucleotide motif 5'-nGAAn-3'. HSFs are less conserved and share only 40% sequence identity. Vertebrate cells contain four HSF proteins: HSF1, 2 and 4 are ubiquitous, while HSF3 has only been characterized in avian species. HSF1 induces heat shock gene transcription in response to heat, heavy metals, and oxidative agents, while HSF2 is involved in spermatogenesis and erythroid cell development. HSF3 and HSF4 show overlapping functions with HSF1 and HSF2. The inactive form of HSF1 exists as a monomer that localizes to both the cytoplasm and nucleus, but does not bind DNA (1,2). In response to stress, HSF1 becomes phosphorylated, forms homotrimers, binds DNA and activates heat shock gene transcription (1,2). HSF1 activity is positively regulated by phosphorylation of Ser419 by PLK1, which enhances nuclear translocation, and phosphorylation of Ser230 by CaMKII, which enhances transactivation (3,4). Alternatively, HSF1 activity is repressed by phosphorylation of serines at 303 and 307 by GSK3 and ERK1, respectively, which leads to binding of 14-3-3 protein and sequestration of HSF1 in the cytoplasm (5,6). In addition, during attenuation from the heat shock response, HSF1 is repressed by direct binding of Hsp70, HSP40/Hdj-1, and HSF binding protein 1 (HSBP1) (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: The homeodomain protein NKX6.1 is a transcription factor that regulates pancreatic β-cell development (1). Overexpressed NKX6.1 stimulates rat pancreatic β-cell proliferation and increases glucose-stimulated insulin secretion (GSIS) (2). The effect on GSIS was shown to be mediated by the up-regulation of prohormone VGF expression and the subsequent potentiation by TLQP-21, a peptide derived from VGF (3). Both nuclear receptors Nr4a1 and Nr4a3 are essential for pancreatic β-cell proliferation driven by overexpressed NKX6.1 (4). In addition, studies suggest that NKX6.1 is a suppressor for epithelial-to-mesenchymal transition (EMT), leading to inhibition of tumor metastasis (5).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Methylation of DNA at cytosine residues in mammalian cells is a heritable, epigenetic modification that is critical for proper regulation of gene expression, genomic imprinting and development (1,2). Three families of mammalian DNA methyltransferases have been identified: DNMT1, DNMT2 and DNMT3 (1,2). DNMT1 is constitutively expressed in proliferating cells and functions as a maintenance methyltransferase, transferring proper methylation patterns to newly synthesized DNA during replication. DNMT3A and DNMT3B are strongly expressed in embryonic stem cells with reduced expression in adult somatic tissues. DNMT3A and DNMT3B function as de novo methyltransferases that methylate previously unmethylated regions of DNA. DNMT2 is expressed at low levels in adult somatic tissues and its inactivation affects neither de novo nor maintenance DNA methylation. DNMT1, DNMT3A and DNMT3B together form a protein complex that interacts with histone deacetylases (HDAC1, HDAC2, Sin3A), transcriptional repressor proteins (RB, TAZ-1) and heterochromatin proteins (HP1, SUV39H1), to maintain proper levels of DNA methylation and facilitate gene silencing (3-8). Improper DNA methylation contributes to diseased states such as cancer (1,2). Hypermethylation of promoter CpG islands within tumor suppressor genes correlates with gene silencing and the development of cancer. In addition, hypomethylation of bulk genomic DNA correlates with and may contribute to the onset of cancer. DNMT1, DNMT3A and DNMT3B are over-expressed in many cancers, including acute and chronic myelogenous leukemias, in addition to colon, breast and stomach carcinomas (9-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Methylation of DNA at cytosine residues in mammalian cells is a heritable, epigenetic modification that is critical for proper regulation of gene expression, genomic imprinting and development (1,2). Three families of mammalian DNA methyltransferases have been identified: DNMT1, DNMT2 and DNMT3 (1,2). DNMT1 is constitutively expressed in proliferating cells and functions as a maintenance methyltransferase, transferring proper methylation patterns to newly synthesized DNA during replication. DNMT3A and DNMT3B are strongly expressed in embryonic stem cells with reduced expression in adult somatic tissues. DNMT3A and DNMT3B function as de novo methyltransferases that methylate previously unmethylated regions of DNA. DNMT2 is expressed at low levels in adult somatic tissues and its inactivation affects neither de novo nor maintenance DNA methylation. DNMT1, DNMT3A and DNMT3B together form a protein complex that interacts with histone deacetylases (HDAC1, HDAC2, Sin3A), transcriptional repressor proteins (RB, TAZ-1) and heterochromatin proteins (HP1, SUV39H1), to maintain proper levels of DNA methylation and facilitate gene silencing (3-8). Improper DNA methylation contributes to diseased states such as cancer (1,2). Hypermethylation of promoter CpG islands within tumor suppressor genes correlates with gene silencing and the development of cancer. In addition, hypomethylation of bulk genomic DNA correlates with and may contribute to the onset of cancer. DNMT1, DNMT3A and DNMT3B are over-expressed in many cancers, including acute and chronic myelogenous leukemias, in addition to colon, breast and stomach carcinomas (9-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: Methylation of DNA at cytosine residues in mammalian cells is a heritable, epigenetic modification that is critical for proper regulation of gene expression, genomic imprinting and development (1,2). Three families of mammalian DNA methyltransferases have been identified: DNMT1, DNMT2 and DNMT3 (1,2). DNMT1 is constitutively expressed in proliferating cells and functions as a maintenance methyltransferase, transferring proper methylation patterns to newly synthesized DNA during replication. DNMT3A and DNMT3B are strongly expressed in embryonic stem cells with reduced expression in adult somatic tissues. DNMT3A and DNMT3B function as de novo methyltransferases that methylate previously unmethylated regions of DNA. DNMT2 is expressed at low levels in adult somatic tissues and its inactivation affects neither de novo nor maintenance DNA methylation. DNMT1, DNMT3A and DNMT3B together form a protein complex that interacts with histone deacetylases (HDAC1, HDAC2, Sin3A), transcriptional repressor proteins (RB, TAZ-1) and heterochromatin proteins (HP1, SUV39H1), to maintain proper levels of DNA methylation and facilitate gene silencing (3-8). Improper DNA methylation contributes to diseased states such as cancer (1,2). Hypermethylation of promoter CpG islands within tumor suppressor genes correlates with gene silencing and the development of cancer. In addition, hypomethylation of bulk genomic DNA correlates with and may contribute to the onset of cancer. DNMT1, DNMT3A and DNMT3B are over-expressed in many cancers, including acute and chronic myelogenous leukemias, in addition to colon, breast and stomach carcinomas (9-12).