Microsize antibodies for $99 | Learn More >>

Product listing: PRDM14 (E1D5S) XP® Rabbit mAb, UniProt ID Q9GZV8 #83527 to SET8 (C18B7) Rabbit mAb, UniProt ID Q9NQR1 #2996

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: PR domain zinc finger protein 14 (PRDM14) is a likely protein lysine methyltransferase that is primarily expressed in primordial germ cells and pluripotent embryonic stem cells. It is essential for the establishment and maintenance of primordial germ cells and critical for the maintenance of pluripotency in embryonic stem cells (1-3). PRDM14 represses genes involved in the differentiation of stem cells into various cell lineages, likely via a combination of interactions with TET proteins, the polycomb repressive complex 2 (PRC2), and CBFA2T2 (3-8). In addition, overexpression of PRDM14 in combination with Jarid2 promotes induced pluripotent stem cell (iPSC) formation (9). PRDM14 protein levels are overexpressed in certain cancers, including breast, leukemia (T-ALL), and non-small cell lung cancer (NSCLC) (10-13), and PRDM14 overexpression may serve as a novel prognostic marker in NSCLC (14). Targeting PRDM14 overexpression with a siRNA-based therapy was shown to decrease liver metastasis in a murine pancreatic cancer model, suggesting potential as a therapeutic option for cancers where this protein is abnormally expressed (15).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: PR domain zinc finger protein 14 (PRDM14) is a likely protein lysine methyltransferase that is primarily expressed in primordial germ cells and pluripotent embryonic stem cells. It is essential for the establishment and maintenance of primordial germ cells and critical for the maintenance of pluripotency in embryonic stem cells (1-3). PRDM14 represses genes involved in the differentiation of stem cells into various cell lineages, likely via a combination of interactions with TET proteins, the polycomb repressive complex 2 (PRC2), and CBFA2T2 (3-8). In addition, overexpression of PRDM14 in combination with Jarid2 promotes induced pluripotent stem cell (iPSC) formation (9). PRDM14 protein levels are overexpressed in certain cancers, including breast, leukemia (T-ALL), and non-small cell lung cancer (NSCLC) (10-13), and PRDM14 overexpression may serve as a novel prognostic marker in NSCLC (14). Targeting PRDM14 overexpression with a siRNA-based therapy was shown to decrease liver metastasis in a murine pancreatic cancer model, suggesting potential as a therapeutic option for cancers where this protein is abnormally expressed (15).

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

Application Methods: Western Blotting

Background: Protein arginine N-methyltransferase 1 (PRMT1) is a member of the protein arginine N-methyltransferase (PRMT) family of proteins that catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine (1). Though all PRMT proteins catalyze the formation of mono-methyl arginine, Type I PRMTs (PRMT1, 3, 4, and 6) add an additional methyl group to produce an asymmetric di-methyl arginine while Type II PRMTs (PRMT 5 and 7) produce symmetric di-methyl arginine (1). Mono-methyl arginine, but not di-methyl arginine, can be converted to citrulline through deimination catalyzed by enzymes such as PADI4 (2). Most PRMTs, including PRMT1, methylate arginine residues found within glycine-arginine rich (GAR) protein domains, such as RGG, RG, and RXR repeats (1). However, PRMT4/CARM1 and PRMT5 methylate arginine residues within PGM (proline-, glycine-, methionine-rich) motifs (3). PRMT1 methylates Arg3 of histone H4 and cooperates synergistically with p300/CBP to enhance transcriptional activation by nuclear receptor proteins (4-6). In addition, PRMT1 methylates many non-histone proteins, including the orphan nuclear receptor HNF4 (6), components of the heterogeneous nuclear ribonucleoprotein (hnRNP) particle (7), the RNA binding protein Sam68 (8), interleukin enhancer-binding factor 3 (ILF3) (9) and interferon-α and β receptors (10). These interactions suggest additional functions in transcriptional regulation, mRNA processing and signal transduction. Alternative mRNA splicing produces three enzymatically active PRMT1 isoforms that differ in their amino-terminal regions (11). PRMT1 is localized to the nucleus or cytoplasm, depending on cell type (12,13), and appears in many distinct protein complexes. ILF3, TIS21 and the leukemia-associated BTG1 proteins bind PRMT1 to regulate its methyltransferase activity (9,14).

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

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

Background: Protein arginine N-methyltransferase 1 (PRMT1) is a member of the protein arginine N-methyltransferase (PRMT) family of proteins that catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine (1). Though all PRMT proteins catalyze the formation of mono-methyl arginine, Type I PRMTs (PRMT1, 3, 4, and 6) add an additional methyl group to produce an asymmetric di-methyl arginine while Type II PRMTs (PRMT 5 and 7) produce symmetric di-methyl arginine (1). Mono-methyl arginine, but not di-methyl arginine, can be converted to citrulline through deimination catalyzed by enzymes such as PADI4 (2). Most PRMTs, including PRMT1, methylate arginine residues found within glycine-arginine rich (GAR) protein domains, such as RGG, RG, and RXR repeats (1). However, PRMT4/CARM1 and PRMT5 methylate arginine residues within PGM (proline-, glycine-, methionine-rich) motifs (3). PRMT1 methylates Arg3 of histone H4 and cooperates synergistically with p300/CBP to enhance transcriptional activation by nuclear receptor proteins (4-6). In addition, PRMT1 methylates many non-histone proteins, including the orphan nuclear receptor HNF4 (6), components of the heterogeneous nuclear ribonucleoprotein (hnRNP) particle (7), the RNA binding protein Sam68 (8), interleukin enhancer-binding factor 3 (ILF3) (9) and interferon-α and β receptors (10). These interactions suggest additional functions in transcriptional regulation, mRNA processing and signal transduction. Alternative mRNA splicing produces three enzymatically active PRMT1 isoforms that differ in their amino-terminal regions (11). PRMT1 is localized to the nucleus or cytoplasm, depending on cell type (12,13), and appears in many distinct protein complexes. ILF3, TIS21 and the leukemia-associated BTG1 proteins bind PRMT1 to regulate its methyltransferase activity (9,14).

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

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

Background: Protein arginine N-methyltransferase 1 (PRMT1) is a member of the protein arginine N-methyltransferase (PRMT) family of proteins that catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine (1). Though all PRMT proteins catalyze the formation of mono-methyl arginine, Type I PRMTs (PRMT1, 3, 4, and 6) add an additional methyl group to produce an asymmetric di-methyl arginine while Type II PRMTs (PRMT 5 and 7) produce symmetric di-methyl arginine (1). Mono-methyl arginine, but not di-methyl arginine, can be converted to citrulline through deimination catalyzed by enzymes such as PADI4 (2). Most PRMTs, including PRMT1, methylate arginine residues found within glycine-arginine rich (GAR) protein domains, such as RGG, RG, and RXR repeats (1). However, PRMT4/CARM1 and PRMT5 methylate arginine residues within PGM (proline-, glycine-, methionine-rich) motifs (3). PRMT1 methylates Arg3 of histone H4 and cooperates synergistically with p300/CBP to enhance transcriptional activation by nuclear receptor proteins (4-6). In addition, PRMT1 methylates many non-histone proteins, including the orphan nuclear receptor HNF4 (6), components of the heterogeneous nuclear ribonucleoprotein (hnRNP) particle (7), the RNA binding protein Sam68 (8), interleukin enhancer-binding factor 3 (ILF3) (9) and interferon-α and β receptors (10). These interactions suggest additional functions in transcriptional regulation, mRNA processing and signal transduction. Alternative mRNA splicing produces three enzymatically active PRMT1 isoforms that differ in their amino-terminal regions (11). PRMT1 is localized to the nucleus or cytoplasm, depending on cell type (12,13), and appears in many distinct protein complexes. ILF3, TIS21 and the leukemia-associated BTG1 proteins bind PRMT1 to regulate its methyltransferase activity (9,14).

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

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

Background: Protein arginine N-methyltransferase 5 (PRMT5) is a member of the protein arginine N-methyltransferase (PRMT) family of proteins that catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine (1). Though all PRMT proteins catalyze the formation of mono-methyl arginine, Type I PRMTs (PRMT1, 3, 4, and 6) add an additional methyl group to produce an asymmetric di-methyl arginine, while Type II PRMTs (PRMT 5 and 7) produce symmetric di-methyl arginine (1). Mono-methyl arginine, but not di-methyl arginine, can be converted to citrulline through deimination catalyzed by enzymes such as PADI4 (2). Most PRMTs methylate arginine residues found within glycine-arginine rich (GAR) protein domains, such as RGG, RG, and RXR repeats (1). However, PRMT5 and PRMT4/CARM1 methylate arginine residues within PGM (proline-, glycine-, methionine-rich) motifs (3).PRMT5 is the predominant Type II PRMT and was first identified through interaction with Jak2 (4). It can catalyze the symmetric di-methylation of histone H2A and H4 on arginine 3 and histone H3 on arginine 2 and 8 (5-6). Methylation of H2A and H4 is thought to be inactivating through the recruitment of DNA methyltransferases, while methylation of H3 recruits WDR5 and MLL, thus promoting the maintenance of euchromatin (5,7). Other putative roles for PRMT5 have been shown in development, mRNA splicing, and chromatin remodeling (8-10). PRMT5 has been shown to be overexpressed in many different types of cancers (11-14).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Protein arginine N-methyltransferase 6 (PRMT6) is a member of the protein arginine N-methyltransferase (PRMT) family of proteins that catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine (1). The three types of PRMTs share the ability to mono-methylate arginine residues, but vary in their ability to generate differential methylation states (1-3). Mono-methylated arginine residues are further methylated by type I PRMTs to generate an asymmetric di-methyl arginine or by type II PRMTs to form a symmetric-dimethyl arginine. Type III methyltransferases are only able to mono-methylate arginine residues (1-3). PRMT6 is a type I PRMT that acts as both a transcriptional coactivator and a corepressor and catalyzes the asymmetric di-methylation of histone H3 (Arg 2, Arg42), histone H4 (Arg3), and histone H2A at Arg29 (2,4). PRMT6 acts as a coactivator for transcription factors, including estrogen receptor and NFκB, while asymmetric di-methylation of histone H3 (Arg2) by PRMT6 prevents MLL methylation of histone H3 at Lys4 and inhibits transcription activation (5-8). In addition to its role in regulating transcription, PRMT6 methylates DNA polymerase β, leading to enhanced DNA binding and processivity during base excision repair of damaged DNA (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: Protein arginine N-methyltransferase 7 (PRMT7) is a member of the protein arginine N-methyltransferase (PRMT) family of proteins that catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine (1). The three types of PRMTs share the ability to mono-methylate arginine residues, but vary in their ability to generate differential methylation states (1-3). Mono-methylated arginine residues are further methylated by type I PRMTs to generate an asymmetric di-methyl arginine or by type II PRMTs to form a symmetric-dimethyl arginine. Type III methyltransferases are only able to mono-methylate arginine residues (1-3). Research studies indicate that PRMT7 is a type III PRMT that displays substrate specificity for an arginine-X-arginine (RXR) motif surrounded by several basic residues (4,5). PRMT7 interacts with a wide array of protein substrates and likely plays a role in many biological processes including pluripotency, neuronal differentiation, genomic instability, snRNP biogenesis, and breast cancer metastasis (6-11).

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

Application Methods: 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).

$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).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: The Set1 histone methyltransferase protein was first identified in yeast as part of the Set1/COMPASS histone methyltransferase complex, which methylates histone H3 at Lys4 and functions as a transcriptional co-activator (1). While yeast contain only one known Set1 protein, six Set1-related proteins exist in mammals: SET1A, SET1B, MLL1, MLL2, MLL3, and MLL4, all of which assemble into COMPASS-like complexes and methylate histone H3 at Lys4 (2,3). These Set1-related proteins are each found in distinct protein complexes, all of which share the common subunits WDR5, RBBP5, ASH2L, CXXC1 and DPY30. These subunits are required for proper complex assembly and modulation of histone methyltransferase activity (2-6). MLL1 and MLL2 complexes contain the additional protein subunit, menin (6). Like yeast Set1, all six Set1-related mammalian proteins methylate histone H3 at Lys4 (2-6). MLL translocations are found in a large number of hematological malignancies, suggesting that Set1/COMPASS histone methyltransferase complexes play a critical role in leukemogenesis (6).

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

Application Methods: Western Blotting

Background: The Set1 histone methyltransferase protein was first identified in yeast as part of the Set1/COMPASS histone methyltransferase complex, which methylates histone H3 at Lys4 and functions as a transcriptional co-activator (1). While yeast contain only one known Set1 protein, six Set1-related proteins exist in mammals: SET1A, SET1B, MLL1, MLL2, MLL3, and MLL4, all of which assemble into COMPASS-like complexes and methylate histone H3 at Lys4 (2,3). These Set1-related proteins are each found in distinct protein complexes, all of which share the common subunits WDR5, RBBP5, ASH2L, CXXC1 and DPY30. These subunits are required for proper complex assembly and modulation of histone methyltransferase activity (2-6). MLL1 and MLL2 complexes contain the additional protein subunit, menin (6). Like yeast Set1, all six Set1-related mammalian proteins methylate histone H3 at Lys4 (2-6). MLL translocations are found in a large number of hematological malignancies, suggesting that Set1/COMPASS histone methyltransferase complexes play a critical role in leukemogenesis (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: The retinoblastoma (Rb) tumor suppressor family includes the retinoblastoma protein Rb (p105), retinoblastoma-like protein 1 (RBL1, p107), and retinoblastoma-like protein 2 (RBL2, p130). These Rb family proteins are referred to as "pocket proteins" because they contain a conserved binding pocket region that interacts with critical regulatory proteins, including E2F family transcription factors, c-Abl tyrosine kinase, and proteins containing a conserved LXCXE motif (1,2). In quiescent G0 phase cells, active Rb proteins hypophosphorylate and bind to E2F transcription factors to repress transcription and inhibit cell cycle progression (1,2). Upon growth factor induction of quiescent cells, Rb proteins become hyperphosphorylated and inactivated by G1-phase cyclinD-cdk4/6, G1/S-phase cyclin E-cdk2, and G1/S-phase cyclin A-cdk2 complexes (1,2). Hyperphosphorylation of Rb proteins results in a loss of E2F binding and allows for transcriptional activation and cell cycle progression (1,2). In addition to regulating the cell cycle, Rb proteins regulate chromosome stability, induction, and maintenance of senescence, apoptosis, cellular differentiation, and angiogenesis (3).Retinoblastoma-like protein 1 (RBL1, p107) interacts with E2F4 and E2F5 to recruit the DP, RB-like, E2F, and MuvB protein (DREAM) complex to E2F target genes to repress transcription of multiple genes required for progression into S phase and mitosis (4-6). Hypophosphorylation of RBL1 during cellular senescence is required for maintenance of senescent cells (7,8).

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

Application Methods: Western Blotting

Background: Reptin/RuvBL2 and Pontin/RuvBL1 are closely related members of the AAA+ (ATPase associated with diverse cellular activities) superfamily of proteins, and are putatively homologous to bacterial RuvB proteins that drive branch migration of Holliday junctions (1). Reptin and Pontin function together as essential components of chromatin remodeling and modification complexes, such as INO80, TIP60, SRCAP, and Uri1, which play key roles in regulating gene transcription (1,2). In their capacity as essential transcriptional co-regulators, Reptin and Pontin have both been implicated in oncogenic transformations, including those driven by c-Myc, β-catenin, and E1A (2-7).

$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).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated RING1B (D22F2) XP® Rabbit mAb #5694.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

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).

$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).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: In mammalian cells, the significance of histone H2B ubiquitination in chromatin epigenetics came from the identification of the budding yeast protein Bre1 (1,2). Together with the ubiquitin-conjugating enzyme Rad6, Bre1 serves as the E3 ligase in the monoubiquitination of the yeast histone H2B within transcribed regions of chromatin (1-3). Subsequently, the mammalian orthologs of yeast Bre1, RNF20 and RNF40, were identified (4,5). These two proteins form a tight heterodimer that acts as the major E3 ligase responsible for histone H2B monoubiquitination at Lys120 in mammalian cells, a modification linked to RNA Pol II-dependent transcription elongation in undamaged cells. Researchers have shown that DNA double-strand breaks (DSBs) are also capable of inducing monoubiquitination of H2B. This process depends upon the recruitment to DSB sites, as well as ATM-dependent phosphorylation of the RNF20-RNF40 heterodimer, thus highlighting a role for this E3 ligase in DSB repair pathways (6). Indeed, investigators have shown that loss of RNF20-RNF40 function promotes replication stress and chromosomal instability, which may constitute an early step in malignant transformation that precedes cell invasion (7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: In mammalian cells, the significance of histone H2B ubiquitination in chromatin epigenetics came from the identification of the budding yeast protein Bre1 (1,2). Together with the ubiquitin-conjugating enzyme Rad6, Bre1 serves as the E3 ligase in the monoubiquitination of the yeast histone H2B within transcribed regions of chromatin (1-3). Subsequently, the mammalian orthologs of yeast Bre1, RNF20 and RNF40, were identified (4,5). These two proteins form a tight heterodimer that acts as the major E3 ligase responsible for histone H2B monoubiquitination at Lys120 in mammalian cells, a modification linked to RNA Pol II-dependent transcription elongation in undamaged cells. Researchers have shown that DNA double-strand breaks (DSBs) are also capable of inducing monoubiquitination of H2B. This process depends upon the recruitment to DSB sites, as well as ATM-dependent phosphorylation of the RNF20-RNF40 heterodimer, thus highlighting a role for this E3 ligase in DSB repair pathways (6). Indeed, investigators have shown that loss of RNF20-RNF40 function promotes replication stress and chromosomal instability, which may constitute an early step in malignant transformation that precedes cell invasion (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: In mammalian cells, the significance of histone H2B ubiquitination in chromatin epigenetics came from the identification of the budding yeast protein Bre1 (1,2). Together with the ubiquitin-conjugating enzyme Rad6, Bre1 serves as the E3 ligase in the monoubiquitination of the yeast histone H2B within transcribed regions of chromatin (1-3). Subsequently, the mammalian orthologs of yeast Bre1, RNF20 and RNF40, were identified (4,5). These two proteins form a tight heterodimer that acts as the major E3 ligase responsible for histone H2B monoubiquitination at Lys120 in mammalian cells, a modification linked to RNA Pol II-dependent transcription elongation in undamaged cells. Researchers have shown that DNA double-strand breaks (DSBs) are also capable of inducing monoubiquitination of H2B. This process depends upon the recruitment to DSB sites, as well as ATM-dependent phosphorylation of the RNF20-RNF40 heterodimer, thus highlighting a role for this E3 ligase in DSB repair pathways (6). Indeed, investigators have shown that loss of RNF20-RNF40 function promotes replication stress and chromosomal instability, which may constitute an early step in malignant transformation that precedes cell invasion (7).

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

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

Background: RNA polymerase II (RNAPII) is a large multi-protein complex that functions as a DNA-dependent RNA polymerase, catalyzing the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (1). The largest subunit, RNAPII subunit B1 (Rpb1), also known as RNAPII subunit A (POLR2A), contains a unique heptapeptide sequence (Tyr1,Ser2,Pro3,Thr4,Ser5,Pro6,Ser7), which is repeated up to 52 times in the carboxy-terminal domain (CTD) of the protein (1). This CTD heptapeptide repeat is subject to multiple post-translational modifications, which dictate the functional state of the polymerase complex. Phosphorylation of the CTD during the active transcription cycle integrates transcription with chromatin remodeling and nascent RNA processing by regulating the recruitment of chromatin modifying enzymes and RNA processing proteins to the transcribed gene (1). During transcription initiation, RNAPII contains a hypophosphorylated CTD and is recruited to gene promoters through interactions with DNA-bound transcription factors and the Mediator complex (1). The escape of RNAPII from gene promoters requires phosphorylation at Ser5 by CDK7, the catalytic subunit of transcription factor IIH (TFIIH) (2). Phosphorylation at Ser5 mediates the recruitment of RNA capping enzymes, in addition to histone H3 Lys4 methyltransferases, which function to regulate transcription initiation and chromatin structure (3,4). After promoter escape, RNAPII proceeds down the gene to an intrinsic pause site, where it is halted by the negative elongation factors NELF and DSIF (5). At this point, RNAPII is unstable and frequently aborts transcription and dissociates from the gene. Productive transcription elongation requires phosphorylation at Ser2 by CDK9, the catalytic subunit of the positive transcription elongation factor P-TEFb (6). Phosphorylation at Ser2 creates a stable transcription elongation complex and facilitates recruitment of RNA splicing and polyadenylation factors, in addition to histone H3 Lys36 methyltransferases, which function to promote elongation-compatible chromatin (7,8). Ser2/Ser5-phosphorylated RNAPII then transcribes the entire length of the gene to the 3' end, where transcription is terminated. RNAPII dissociates from the DNA and is recycled to the hypophosphorylated form by various CTD phosphatases (1).In addition to Ser2/Ser5 phosphorylation, Ser7 of the CTD heptapeptide repeat is also phosphorylated during the active transcription cycle. Phosphorylation at Ser7 is required for efficient transcription of small nuclear (sn) RNA genes (9,10). snRNA genes, which are neither spliced nor poly-adenylated, are structurally different from protein-coding genes. Instead of a poly(A) signal found in protein-coding RNAs, snRNAs contain a conserved 3'-box RNA processing element, which is recognized by the Integrator snRNA 3' end processing complex (11,12). Phosphorylation at Ser7 by CDK7 during the early stages of transcription facilitates recruitment of RPAP2, which dephosphorylates Ser5, creating a dual Ser2/Ser7 phosphorylation mark that facilitates recruitment of the Integrator complex and efficient processing of nascent snRNA transcripts (13-15).

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

Application Methods: Western Blotting

Background: The PAF (RNA polymerase II (RNAPII) associated factor) complex was initially identified in yeast and is comprised of subunits PAF1, Leo1, Ctr9, Cdc73, RTF1 and Ski8 (1,2). The PAF complex plays an important role in transcription initiation and elongation by RNAPII by regulating the establishment of proper histone modifications such as histone H2B ubiquitination and the recruitment of the histone chaperone FACT (facilitates chromatin transcription) (3-5). The PAF complex also plays a role in mRNA processing and maturation by interacting with and recruiting the cleavage and polyadenylation specificity factor and cleavage stimulation factor complexes via the Cdc73 subunit (6,7). In addition, the Ski8 subunit of the PAF complex is part of the hSKi complex that regulates RNA surveillance, suggesting an important function of the complex in coordinating events associated with proper RNA maturation during transcription (1,5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Ring1 and YY1-binding protein (RYBP) is a widely expressed nuclear protein that functions as a modulator of Ring1A/Ring1B-dependent histone H2A monoubiquitylation (1-3). Ring1A and Ring1B proteins function as the catalytic core subunits of polyclomb repressor complex 1 (PRC1), which acts to repress gene expression in part through monoubiquitination of histone H2A on Lys119 (4). By binding to both the YY1 DNA-binding transcription factor and Ring1A/Ring1B, RYPB is able to recruit the PRC1 complex to target loci independent of prior tri-methylation of histone H3 Lys27 by the EZH2-dependent PRC2 complex (2,3). RYBP also binds monoubiquitinated H2A Lys119 and may act to stabilize or spread binding of PRC1 across large domains of repressed chromatin (5). In addition, RYBP directly stimulates the ubiquitination activity of Ring1A/Ring1B and is required for proper differentiation of stem cells along multiple cell lineages (2,3,6,7). RYBP has also been shown to bind MDM2 and block ubiquitination and degradation of p53, leading to cell cycle arrest and apoptosis in response to DNA damage (8). Many studies demonstrate that RYBP functions as a tumor suppressor protein. RYBP expression is decreased in multiple cancers, including non-small cell lung cancer, hepatocellular carcinoma, and glioblastoma with decreased expression correlating with metastasis and poor prognosis (8-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Special AT-rich binding protein 1 (SATB1) functions as both a global chromatin organizer and a gene-specific transcription factor (1). SATB1 cooperates with promyelocytic leukemia protein (PML) to regulate global chromatin architecture by organizing chromatin into distinct loops via periodic anchoring of matrix attachment regions (MARs) in DNA to the nuclear matrix (1-3). In addition, SATB1 recruits multiple chromatin-remodeling proteins that contribute to specific gene activation and repression, including the chromatin remodeling enzymes ACF and ISWI, the histone deacetylase HDAC1, and the histone acetyltransferases PCAF and p300/CBP (4-6). Phosphorylation of SATB1 on Ser185 by protein kinase C regulates its interaction with HDAC1 and PCAF. While unphosphorylated SATB1 binds to PCAF, phosphorylated SATB1 preferentially binds to HDAC1 (6). Acetylation of SATB1 on Lys136 by PCAF impairs its DNA binding activity, thereby removing SATB1 from gene promoters (6). SATB1 is expressed predominantly in thymocytes and is involved in gene regulation during T cell activation (1). SATB1 is also expressed in metastatic breast cancer cells and is a potential prognostic marker and therapeutic target for metastatic breast cancer (7). In a mouse model system, RNAi-mediated knockdown of SATB1 reversed tumorigenesis by inhibiting tumor growth and metastasis, while ectopic expression of SATB1 in non-metastatic breast cancer cells produced invasive tumors.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Special AT-rich binding protein 2 (SATB2) is a close homolog to SATB1 that functions as a transcription factor. It binds to nuclear matrix attachment regions (MARS); regulatory DNA sequences important for chromatin structure. SATB2 was initially identified when bound to the MARS of the immunoglobulin μ gene in pre-B cells, enhancing its expression (1). SATB2 plays a role in osteoblast differentiation by repressing the HoxA2 gene and enhancing the activity of Runx2 and ATF4 (2). SATB2 also plays a role in the developing cerebral cortex by changing chromatin structure surrounding the Ctip2 regulatory regions (3). In erythroid cells, SATB2 activates the γ-globin locus by recruiting PCAF and reordering the chromatin structure (4). Downregulation of SATB2 is linked to colorectal cancer and head and neck squamous carcinomas (5,6).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Special AT-rich binding protein 2 (SATB2) is a close homolog to SATB1 that functions as a transcription factor. It binds to nuclear matrix attachment regions (MARS); regulatory DNA sequences important for chromatin structure. SATB2 was initially identified when bound to the MARS of the immunoglobulin μ gene in pre-B cells, enhancing its expression (1). SATB2 plays a role in osteoblast differentiation by repressing the HoxA2 gene and enhancing the activity of Runx2 and ATF4 (2). SATB2 also plays a role in the developing cerebral cortex by changing chromatin structure surrounding the Ctip2 regulatory regions (3). In erythroid cells, SATB2 activates the γ-globin locus by recruiting PCAF and reordering the chromatin structure (4). Downregulation of SATB2 is linked to colorectal cancer and head and neck squamous carcinomas (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The Set1 histone methyltransferase protein was first identified in yeast as part of the Set1/COMPASS histone methyltransferase complex, which methylates histone H3 at Lys4 and functions as a transcriptional co-activator (1). While yeast contain only one known Set1 protein, six Set1-related proteins exist in mammals: SET1A, SET1B, MLL1, MLL2, MLL3, and MLL4, all of which assemble into COMPASS-like complexes and methylate histone H3 at Lys4 (2,3). These Set1-related proteins are each found in distinct protein complexes, all of which share the common subunits WDR5, RBBP5, ASH2L, CXXC1 and DPY30. These subunits are required for proper complex assembly and modulation of histone methyltransferase activity (2-6). MLL1 and MLL2 complexes contain the additional protein subunit, menin (6). Like yeast Set1, all six Set1-related mammalian proteins methylate histone H3 at Lys4 (2-6). MLL translocations are found in a large number of hematological malignancies, suggesting that Set1/COMPASS histone methyltransferase complexes play a critical role in leukemogenesis (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The Set1 histone methyltransferase protein was first identified in yeast as part of the Set1/COMPASS histone methyltransferase complex, which methylates histone H3 at Lys4 and functions as a transcriptional co-activator (1). While yeast contain only one known Set1 protein, six Set1-related proteins exist in mammals: SET1A, SET1B, MLL1, MLL2, MLL3, and MLL4, all of which assemble into COMPASS-like complexes and methylate histone H3 at Lys4 (2,3). These Set1-related proteins are each found in distinct protein complexes, all of which share the common subunits WDR5, RBBP5, ASH2L, CXXC1 and DPY30. These subunits are required for proper complex assembly and modulation of histone methyltransferase activity (2-6). MLL1 and MLL2 complexes contain the additional protein subunit, menin (6). Like yeast Set1, all six Set1-related mammalian proteins methylate histone H3 at Lys4 (2-6). MLL translocations are found in a large number of hematological malignancies, suggesting that Set1/COMPASS histone methyltransferase complexes play a critical role in leukemogenesis (6).

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

Application Methods: Western Blotting

Background: SET7/SET9 is a member of the SET domain-containing family, and can specifically methylate Lys4 on histone H3 (1). Like most other lysine-directed histone methyltransferases, it contains a conserved catalytic SET domain originally identified in the Drosophila Su(var)3-9, Enhancer of zeste and Trithorax proteins. Histone methylation is a major determinant for the formation of active and inactive regions of the genome and is crucial for the proper programming of the genome during development (2,3). Methylation of histone H3 Lys4 enhances transcriptional activation by coordinating the recruitment of BPTF, a component of the NURF chromatin remodeling complex, and WDR5, a component of multiple histone methyltransferase complexes (4,5). In addition, methylation of lysine 4 blocks transcriptional repression by inhibiting the binding of the NURD histone deacetylation complex to the amino-terminal tail of histone H3 and interfering with SUV39H1-mediated methylation of histone H3 Lys9 (1). SET7/SET9 is highly active on free histone H3, but only very weakly methylates H3 within nucleosomes (1). Besides histones, SET7/SET9 also methylates Lys189 of the TAF10, a member of the TFIID transcription factor complex, and Lys372 of the p53 tumor suppressor protein (6,7). Methylation of TAF10 stimulates transcription in a promoter-specific manner by increasing the affinity of TAF10 for RNA polymerase II, which may potentiate pre-initiation complex formation (6). Methylation of p53 at Lys372 increases protein stability and leads to upregulation of target genes such as p21. Thus the loss of SET7/SET9 may represent another mechanism for the inactivation of p53 in human cancers (7).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: SET domain-containing lysine methyltransferase 8 (SET8), also known as PR/SET domain-containing protein 7 (PR/SET7), is a member of a family of histone lysine methyltransferases, each of which contains a conserved catalytic SET domain originally identified in Drosophila Su[var]3-9, Enhancer of zeste, and Trithorax proteins (1-3). SET8 is a single-subunit enzyme that mono-methylates histone H4 on Lys20, preferably on nucleosomal substrates (1-3). SET8 protein levels and Histone H4 Lys20 methylation are cell cycle regulated, both increasing in S phase and peaking at G2/M phase (4,5). SET8 interacts with the PCNA protein, associates with sites of active DNA synthesis, and is required for DNA replication and genome stability during S phase (5-7). Inhibition of SET8 using shRNA or siRNA results in arrest of replication forks, induction of double-stranded DNA breaks, and a Chk1-mediated cell-cycle arrest in S and G2/M phases of the cell cycle (6,7). Furthermore, SET8 methylates p53 on Lys382, down regulating the pro-apoptotic and checkpoint activation functions of p53 (8). In response to DNA damage, SET8 expression levels decrease, allowing p53 to activate checkpoints and/or apoptosis (8). Both the methylation of histone H4 Lys20 and p53 appear to be important for the functions of SET8 in S phase.