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Monkey N-Methyltransferase Activity

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

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

Background: The Erg-associated protein with SET domain (ESET), also known as SET-domain, bifurcated 1 (SETDB1) protein, 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). ESET also contains tudor and methyl-CpG-binding domains, which may coordinate binding to methylated histones and methylated DNA, respectively (1). ESET methylates histone H3 Lys9, creating a transcriptionally repressive mark that facilitates gene silencing (1-3). However, unlike SUV39H histone H3 Lys9 methyltransferases, which function mainly in heterochromatin regions such as pericentric heterochromatin, ESET functions mainly in euchromatic regions to repress gene promoters (3). ESET interacts with a variety of proteins, including transcription factors (ERG), histone deacetylases (HDAC1/2), DNA methyltransferases (DNMT3A/B) and transcriptional co-repressors (mSin3A/B, MBD1, KAP-1, the ATFa-associated modulator mAM) (1-6). mAM forms a complex with ESET, stimulating its methyltransferase activity, specifically the conversion of di-methyl to tri-methyl histone H3 Lys9 (2). MBD1 recruits ESET to the CAF-1 complex to facilitate methylation of histone H3 Lys9 during replication-coupled chromatin assembly in S phase (5). DNMT3A recruits ESET to silenced promoters in cancer cells (7). ESET may play a role in the pathogenesis of Huntington's disease, since levels of ESET protein and tri-methyl histone H3 Lys9 are both increased in diseased brains (8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: The Erg-associated protein with SET domain (ESET), also known as SET-domain, bifurcated 1 (SETDB1) protein, 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). ESET also contains tudor and methyl-CpG-binding domains, which may coordinate binding to methylated histones and methylated DNA, respectively (1). ESET methylates histone H3 Lys9, creating a transcriptionally repressive mark that facilitates gene silencing (1-3). However, unlike SUV39H histone H3 Lys9 methyltransferases, which function mainly in heterochromatin regions such as pericentric heterochromatin, ESET functions mainly in euchromatic regions to repress gene promoters (3). ESET interacts with a variety of proteins, including transcription factors (ERG), histone deacetylases (HDAC1/2), DNA methyltransferases (DNMT3A/B) and transcriptional co-repressors (mSin3A/B, MBD1, KAP-1, the ATFa-associated modulator mAM) (1-6). mAM forms a complex with ESET, stimulating its methyltransferase activity, specifically the conversion of di-methyl to tri-methyl histone H3 Lys9 (2). MBD1 recruits ESET to the CAF-1 complex to facilitate methylation of histone H3 Lys9 during replication-coupled chromatin assembly in S phase (5). DNMT3A recruits ESET to silenced promoters in cancer cells (7). ESET may play a role in the pathogenesis of Huntington's disease, since levels of ESET protein and tri-methyl histone H3 Lys9 are both increased in diseased brains (8).

$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: 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).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Human histone methyltransferase SUV39H1 is the homolog of the dominant Drosophila PEV modifier Su(var)3-9 and is composed of 412 amino acid residues (1). It combines two of the most evolutionarily conserved domains of the "chromatin regulators": the chromo and SET domains (2,3). The 60 amino acid chromo domain represents an ancient histone-like fold that directs heterochromatic localizations. It has been demonstrated that the 130 amino acid SET domain contains the methyltransferase catalytic motif, which cooperates with the adjacent cysteine-rich regions to confer histone methyltransferase activity (1). This enzyme selectively methylates histone H3 on Lys9, which generates a binding site for HP1 proteins, a family of heterochromatic adaptor molecules involved in both gene silencing and supra-nucleosomal chromatin structure (4,5). SUV39H1 histone methyltransferase plays an important role in modification of histone amino termini and regulation of gene expression.

$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: 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, Monkey

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

Background: MGMT (O-6-methylguanine-DNA methyltransferase) is a DNA repair enzyme that participates in a suicide reaction that specifically removes methyl or alkyl groups from the O(6) position of guanine, restoring guanine to its normal form without causing DNA breaks (1). MGMT protects cells from alkylating toxins, and is an important factor in drug resistance to alkylating therapeutic agents (2,3). It is ubiquitously expressed in normal human tissues (4) and is overexpressed in many types of human tumors, but epigenetically silenced in other tumors. MGMT silencing is a marker associated with poor prognosis, but is a good predictive marker for response to alkylating agent chemotherapy (5).

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: MGMT (O-6-methylguanine-DNA methyltransferase) is a DNA repair enzyme that participates in a suicide reaction that specifically removes methyl or alkyl groups from the O(6) position of guanine, restoring guanine to its normal form without causing DNA breaks (1). MGMT protects cells from alkylating toxins, and is an important factor in drug resistance to alkylating therapeutic agents (2,3). It is ubiquitously expressed in normal human tissues (4) and is overexpressed in many types of human tumors, but epigenetically silenced in other tumors. MGMT silencing is a marker associated with poor prognosis, but is a good predictive marker for response to alkylating agent chemotherapy (5).

$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: Immunoprecipitation, Western Blotting

Background: Protein arginine N-methyltransferase 4 (PRMT4), also known as coactivator-associated arginine methyltransferase 1 (CARM1), is a member of the protein arginine N-methyltransferase (PRMT) family of proteins, which catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine (1). There are two types of PRMT proteins. While both types catalyze the formation of mono-methyl arginine, type I PRMTs (PRMT1, 3, 4 and 6) add an additional methyl group to produce asymmetric di-methyl arginine and 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 performed by enzymes such as PADI4 (2). Most of the PRMTs methylate arginine residues found within glycine-arginine rich (GAR) domains of proteins, such as RGG, RG and RXR repeats (1). However, PRMT4/CARM1 and PRMT5 instead methylate arginine residues within PGM (proline-, glycine-, methionine-rich) motifs (3). PRMT4 methylates Arg2, 17 and 26 of histone H3 and cooperates synergistically with p300/CBP and p160 coactivators to enhance transcriptional activation by nuclear receptor proteins (4). In addition, PRMT4 methylates many non-histone proteins, including transcriptional coactivators (p300/CBP, SRC-3) (5,6,7,8), splicing factors (SmB, CA150, SAP49, UIC) (3), RNA binding proteins (PABP1, Sam68, HuD, HuR) (9,10,11), and thymocyte cyclic AMP-regulated phosphoprotein (TARPP) (12), suggesting additional functions in transcriptional regulation, mRNA processing and thymocyte maturation. Methylation of the splicing factor CA150 by PRMT4 facilitates an interaction with the Tudor domain of SMN, suggesting a role for PRMT4 in spinal muscular atrophy (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Wolf-Hirschhorn syndrome candidate protein 1 (WHSC1), also known as Nuclear SET domain-containing protein 2 (NSD2) and Multiple myeloma SET domain-containing protein (MMSET), is a histone methyltransferase protein that catalyzes the di-methylation of histone H3 Lys36, a mark that is associated with transcriptionally active regions of the genome (1,2). WHSC1 haploinsufficiency is implicated in the developmental disorder known as Wolf-Hirshchorn syndrome (WHS), which is characterized by growth and mental retardation, and congenital heart defects (3). In addition, WHSC1 is overexpressed and associated with poor prognosis in a large variety of human cancers, including neuroblastoma, and ovarian, hepatocellular, endometrial, and colorectal carcinoma (4-8). In multiple myeloma, 15-20% of all patients show overexpression of WHSC1 due to a t(4;14)(p16.3;q32) chromosomal translocation that places the WHSC1 gene upstream of a strong enhancer (2). The WHSC1 gene encodes for three major protein isoforms. Isoform II is the full-length protein containing 1365 amino acids. Isoform I, which is generated by alternative splicing, is identical to the N-terminal 647 amino acids of isoform II. A third isoform, known as REIIBP, is generated from a transcript initiating in intron 9 of the WHSC1 locus and is identical to the C-terminal 584 amino acids of isoform II.

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

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

Background: SET domain-containing protein 2 (SETD2 or SET2), also known as lysine N-methyltransferase 3 A (KMT3A), huntingtin yeast partner B (HYBP), and huntingtin-interacting factor (HIF-1), is a ubiquitously expressed nuclear protein methyltransferase that is responsible for the majority of tri-methylation of histone H3 on lysine 36 (H3K36Me3) (1-3). SETD2-mediated H3K36Me3 is critical for proper regulation of transcription elongation, RNA splicing and DNA mismatch repair (1). SETD2 interacts with RNA polymerase II (RNAPII) that is hyper-phosphorylated on the C-terminal domain (CTD) of the largest subunit Rpb1 (2-4). Upon hyper-phosphorylation of the RNAPII CTD during activation of transcriptional elongation, SETD2 is recruited and facilitates tri-methylation of histone H3 lysine 36 in the body of transcriptionally active genes (2-4). H3K36Me3 then acts to recruit the transcription elongation factor FACT, which modulates nucleosome dynamics to facilitate transcription elongation and prevent cryptic transcriptional initiation (5). In addition, H3K36Me3 acts to recruit RNA-splicing proteins and regulate proper splicing of introns concurrent with transcriptional elongation (3, 6-9). In addition to regulating transcription, SETD2-dependent H3K36Me3 regulates DNA mismatch repair by recruiting MutSα (MSH2 and MSH6) to chromatin during G1 and early S phase (10). Loss of SETD2 results in an increase in microsatellite instability and elevated levels of spontaneous mutations (10). SETD2 is often mutated and/or inactivated in multiple types of cancer, including renal cell carcinoma, leukemia, melanoma and liver cancer (11-13).

$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: SET and MYND domain-containing protein 2 (SMYD2), also known as lysine methyltransferase protein 3C (KMT3C), is a member of the SMYD family of protein methyltransferases (1). All five members of this family (SMYD1, SMYD2, SMYD3, SMYD4, and SMYD5) contain a conserved catalytic SET domain, originally identified in Drosophila Su[var]3-9, Enhancer of zeste, and Trithorax proteins. This domain is split by the MYN domain/zinc finger motif believed to facilitate protein-protein interactions (1). SMYD2 localizes to both the cytoplasm and nucleus, and is highly expressed in the adult mouse heart, brain, liver, kidney, thymus, and ovary, as well as in the developing mouse embryo (1). SMYD2 functions to repress transcription by interacting with the Sin3A repressor complex and methylating Lys36 of histone H3 (1). SMYD2 also interacts with HSP90α and methylates Lys4 of histone H3, a mark associated with transcriptional activation (2). In addition to histones as methyl substrates, SMYD2 methylates p53 at Lys370 to repress p53-mediated transcriptional activation and apoptosis (3,4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: SET and MYND domain-containing protein 2 (SMYD2), also known as lysine methyltransferase protein 3C (KMT3C), is a member of the SMYD family of protein methyltransferases (1). All five members of this family (SMYD1, SMYD2, SMYD3, SMYD4, and SMYD5) contain a conserved catalytic SET domain, originally identified in Drosophila Su[var]3-9, Enhancer of zeste, and Trithorax proteins. This domain is split by the MYN domain/zinc finger motif believed to facilitate protein-protein interactions (1). SMYD2 localizes to both the cytoplasm and nucleus, and is highly expressed in the adult mouse heart, brain, liver, kidney, thymus, and ovary, as well as in the developing mouse embryo (1). SMYD2 functions to repress transcription by interacting with the Sin3A repressor complex and methylating Lys36 of histone H3 (1). SMYD2 also interacts with HSP90α and methylates Lys4 of histone H3, a mark associated with transcriptional activation (2). In addition to histones as methyl substrates, SMYD2 methylates p53 at Lys370 to repress p53-mediated transcriptional activation and apoptosis (3,4).

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

Application Methods: Western Blotting

Background: One-carbon metabolism includes enzymatic reactions involving the transfer of one-carbon groups mediated by folate cofactor. The activated one-carbon groups are used by various metabolic pathways, including purine synthesis, thymidine synthesis, and remethylation of homocysteine to methionine (1). One of the enzymes in one-carbon metabolism, methionine synthase, catalyzes the conversion of 5-methyltetrahydrofolate and homocysteine to tetrahydrofolate and methionine. Methionine is further converted to S-adenosylmethionine (SAM) (1, 2). S-adenosylmethionine (SAM) is a major reactive methyl carrier and plays a critical role in epigenetic regulation (2, 3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Chromatin IP, Flow Cytometry, 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).