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Monoclonal Antibody Chromatin IP Positive Regulation of Transcription

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: The Jak-Stat signaling pathway is utilized by a large number of cytokines, growth factors, and hormones (1). Receptor-mediated tyrosine phosphorylation of Jak family members triggers phosphorylation of Stat proteins, resulting in their nuclear translocation, binding to specific DNA elements, and subsequent activation of transcription. The remarkable range and specificity of responses regulated by the Stats is determined, in part, by the tissue-specific expression of different cytokine receptors, Jaks, and Stats, as well as by the combinatorial coupling of various Stat members to different receptors (2). Stat4 is predominantly expressed in the spleen, thymus, and testis and has been most extensively investigated as the mediator of IL-12 responses (3-8). Activation of Stat4 is associated with phosphorylation at Tyr693 (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Mastermind-like (MAML) family of proteins are homologs of Drosophila Mastermind. The family is composed of three members in mammals: MAML1, MAML2, and MAML3 (1,2). MAML proteins form complexes with the intracellular domain of Notch (ICN) and the transcription factor CSL (RBP-Jκ) to regulate Notch target gene expression (3-5). MAML1 also interacts with myocyte enhancer factor 2C (MEF2C) to regulate myogenesis (6). MAML2 is frequently found to be fused with Mucoepidermoid carcinoma translocated gene 1 (MECT1, also know as WAMTP1 or TORC1) in patients with mucoepidermoid carcinomas and Warthin's tumors (7).

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

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

Background: Helios (Ikaros family zinc finger 2, IZKF2) is an Ikaros family transcription factor composed of several zinc fingers that mediate DNA binding and homodimerization or heterodimerization with other Ikaros family proteins (1,2). In the hematopoietic system, Helios expression is restricted to T cells and early hematopoietic progenitors (1,2). In regulatory T cells, expression of Helios contributes to an anergic phenotype by binding to the IL-2 promoter and suppressing IL-2 transcription (3). In addition, alteration of the corresponding Helios gene IZKF2 is one hallmark of low-hypodiploid acute lymphoblastic leukemia (4).

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

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

Background: Mastermind-like (MAML) family of proteins are homologs of Drosophila Mastermind. The family is composed of three members in mammals: MAML1, MAML2, and MAML3 (1,2). MAML proteins form complexes with the intracellular domain of Notch (ICN) and the transcription factor CSL (RBP-Jκ) to regulate Notch target gene expression (3-5). MAML1 also interacts with myocyte enhancer factor 2C (MEF2C) to regulate myogenesis (6). MAML2 is frequently found to be fused with Mucoepidermoid carcinoma translocated gene 1 (MECT1, also know as WAMTP1 or TORC1) in patients with mucoepidermoid carcinomas and Warthin's tumors (7).

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

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

Background: The Fos family of nuclear oncogenes includes c-Fos, FosB, Fos-related antigen 1 (FRA1), and Fos-related antigen 2 (FRA2) (1). While most Fos proteins exist as a single isoform, the FosB protein exists as two isoforms: full-length FosB and a shorter form, FosB2 (Delta FosB), which lacks the carboxy-terminal 101 amino acids (1-3). The expression of Fos proteins is rapidly and transiently induced by a variety of extracellular stimuli including growth factors, cytokines, neurotransmitters, polypeptide hormones, and stress. Fos proteins dimerize with Jun proteins (c-Jun, JunB, and JunD) to form Activator Protein-1 (AP-1), a transcription factor that binds to TRE/AP-1 elements and activates transcription. Fos and Jun proteins contain the leucine-zipper motif that mediates dimerization and an adjacent basic domain that binds to DNA. The various Fos/Jun heterodimers differ in their ability to transactivate AP-1 dependent genes. In addition to increased expression, phosphorylation of Fos proteins by Erk kinases in response to extracellular stimuli may further increase transcriptional activity (4-6). Phosphorylation of c-Fos at Ser32 and Thr232 by Erk5 increases protein stability and nuclear localization (5). Phosphorylation of FRA1 at Ser252 and Ser265 by Erk1/2 increases protein stability and leads to overexpression of FRA1 in cancer cells (6). Following growth factor stimulation, expression of FosB and c-Fos in quiescent fibroblasts is immediate, but very short-lived, with protein levels dissipating after several hours (7). FRA1 and FRA2 expression persists longer, and appreciable levels can be detected in asynchronously growing cells (8). Deregulated expression of c-Fos, FosB, or FRA2 can result in neoplastic cellular transformation; however, Delta FosB lacks the ability to transform cells (2,3).

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

Application Methods: Chromatin IP, Western Blotting

Background: Core-binding factor subunit β (CBFβ) is a non-DNA binding transcription factor subunit that associates with and regulates the DNA binding activity of RUNX1, RUNX2, and RUNX3 (1). CBFβ is ubiquitously expressed and has been implicated in a variety of developmental processes including hematapoiesis, T cell development, chondrogenesis, and bone formation (2-7). In addition, investigators have identified CBFβ as one of the most frequently translocated genes in leukemia (8) and research studies have found it to be required for HIV immune evasion (9,10). CBFβ interacts with the viral protein VIF and triggers assembly of a ubiquitin ligase complex that targets the retroviral inhibitor APOBEC3G for degradation (9,10).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The Jak-Stat signaling pathway is utilized by a large number of cytokines, growth factors, and hormones (1). Receptor-mediated tyrosine phosphorylation of Jak family members triggers phosphorylation of Stat proteins, resulting in their nuclear translocation, binding to specific DNA elements, and subsequent activation of transcription. The remarkable range and specificity of responses regulated by the Stats is determined, in part, by the tissue-specific expression of different cytokine receptors, Jaks, and Stats, as well as by the combinatorial coupling of various Stat members to different receptors (2). Stat4 is predominantly expressed in the spleen, thymus, and testis and has been most extensively investigated as the mediator of IL-12 responses (3-8). Activation of Stat4 is associated with phosphorylation at Tyr693 (9).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

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

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

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

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

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

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

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

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The T-box gene family consists of transcription factors characterized by a related DNA-binding domain (T-box) of approximately 200 amino acids (1,2). The T-box genes exhibit diverse temporal and spatial patterns in the developing embryo. Studies have demonstrated members of this family play crucial roles during embryogenesis in a wide range of organisms by regulating cell fate decisions to establish the early body plan and to regulate later processes underlying organogenesis (3-5). Mutations in T-box genes are associated with many developmental defects (6). Recent studies also indicate potential roles in cancer by members of T-box family (7-9).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: Methylation of DNA at cytosine residues is a heritable, epigenetic modification that is critical for proper regulation of gene expression, genomic imprinting, and mammalian development (1,2). 5-methylcytosine is a repressive epigenetic mark established de novo by two enzymes, DNMT3a and DNMT3b, and is maintained by DNMT1 (3, 4). 5-methylcytosine was originally thought to be passively depleted during DNA replication. However, subsequent studies have shown that Ten-Eleven Translocation (TET) proteins TET1, TET2, and TET3 can catalyze the oxidation of methylated cytosine to 5-hydroxymethylcytosine (5-hmC) (5). Additionally, TET proteins can further oxidize 5-hmC to form 5-formylcytosine (5-fC) and 5-carboxylcytosine (5-caC), both of which are excised by thymine-DNA glycosylase (TDG), effectively linking cytosine oxidation to the base excision repair pathway and supporting active cytosine demethylation (6,7). TET2 is the most frequently mutated gene in myeloid dysplastic syndrome (MDS), a dysplasia of myeloid, megakaryocytic, and/or erythroid cell lineages, of which 30% progress to acute myeloid leukemia (AML) (8, 9). It is also mutated in diffuse large B-cell lymphoma (10). TET2 protein expression is often reduced in solid tumors such as prostate cancer, melanoma, and oral squamous cell carcinoma (11-13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

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

Background: Microphthalmia-associated transcription factor (MITF) is a basic helix-loop-helix leucine zipper transcription factor that is most widely known for its roles in melanocyte, ophthalmic, and osteoclast development (1-3). In humans, MITF can function as a melanoma oncogene (4) and mutations in the corresponding MITF gene are associated with Waardenburg syndrome type 2, an auditory-pigmentary syndrome characterized by developmental defects in cells derived from neural crest (5). At least 12 isoforms of MITF have been identified, which exhibit differential patterns of expression among cell and tissue types (6).

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

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

Background: PHD finger protein 8 (PHF8) is a histone lysine demethylase that functions as a transcriptional activator by specifically demethylating a number of repressive histone methylation marks: mono- and di-methyl-histone H3 Lys9 (H3K9me1 and H3K9me2), di-methyl-histone H3 Lys27 (H3K27me2) and mono-methyl-histone H4 Lys20 (H4K20me1). PHF8 contains an N-terminal zinc finger-like PHD domain that binds tri-methylated histone H3 Lys4 (H3K4Me3) and a C-terminal jumonji domain that is responsible for the demethylase activity (1). Deletion and point mutations (F279S) in the jumonji domain of PHF8 are associated with the onset of X-linked mental retardation (XLMR). In addition, PHF8 is highly expressed in prostate cancer, laryngeal squamous cell carcinoma, and human non-small-cell lung cancer (NSCLC). Its expression is predictive of poor survival (2-4). Overexpression of PHF8 increases cell proliferation and cell motility, while silencing of PHF8 reduces cell proliferation, migration, and invasion (4).

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

Application Methods: Chromatin IP, Western Blotting

Background: Modulation of chromatin structure plays a critical role in the regulation of transcription in eukaryotes. The nucleosome, made up of four core histone proteins (H2A, H2B, H3 and H4), is the primary building block of chromatin. In addition to the growing number of post-translational histone modifications regulating chromatin structure, cells can also exchange canonical histones with variant histones that can directly or indirectly modulate chromatin structure (1). There are five major variants of histone H2A: canonical H2A (most abundant), H2A.X, MacroH2A, H2ABbd and H2A.Z (2). Histone H2A.Z, the most conserved variant across species, functions as both a positive and negative regulator of transcription and is important for chromosome stability (2). Several homologous protein complexes, such as SWR-C (S. cerevisiae), TIP60 (D. melanogaster) and SRCAP (mammals), have been shown to catalyze the ATP-dependent exchange of H2A.Z for H2A in the nucleosome (3,4,5). This exchange of histone H2A variants changes histone-histone interactions in the nucleosome core and alters an acidic patch on the surface of the nucleosome, resulting in changes in nucleosome stability and binding of non-histone proteins such as HP1α (6,7).

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

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

Background: p300/CBP-associated factor (PCAF), also known as lysine acetyl-transferase 2B (KAT2B), is a transcriptional adaptor protein and histone acetyl-transferase (HAT) that functions as the catalytic subunit of the PCAF transcriptional co-activator complex (1). PCAF is 73% homologous to GCN5L2, another HAT protein found in similar complexes (1,2). Like GCN5L2, PCAF acetylates histone H3 on Lys14 and histone H4 on Lys8, both of which contribute to gene activation by modulating chromatin structure and recruiting additional co-activator proteins that contain acetyl-lysine binding bromo-domains (3). PCAF also acetylates non-histone proteins including transcriptional activators (p53, E2F1, MyoD), general transcription factors (TFIIEβ and TFIIF) and architectural DNA binding proteins (HMGA1 and HMG17) (4-10). Acetylation of these proteins regulates their nuclear localization, protein stability, DNA binding, and co-activator association.

$293
100 µl
REACTIVITY
Human

Background: Nanog is a homeodomain-containing transcription factor that is essential for the maintenance of pluripotency and self renewal in embryonic stem cells (1). Nanog expression is controlled by a network of factors including Sox2 and the key pluripotency regulator Oct-4 (1). Recent advances in somatic cell reprogramming have utilized viral expression of combinations of transcription factors including nanog, Oct-4, Sox2, KLF4, c-Myc, and LIN28 (2,3).

$260
100 µl
REACTIVITY
Human, Mouse

Background: Oct-4 (POU5F1) is a transcription factor highly expressed in undifferentiated embryonic stem cells and embryonic germ cells (1). A network of key factors that includes Oct-4, Nanog, and Sox2 is necessary for the maintenance of pluripotent potential, and downregulation of Oct-4 has been shown to trigger cell differentiation (2,3). Research studies have demonstrated that Oct-4 is a useful germ cell tumor marker (4). Oct-4 exists as two splice variants, Oct-4A and Oct-4B (5). Recent studies have suggested that the Oct-4A isoform has the ability to confer and sustain pluripotency, while Oct-4B may exist in some somatic, non-pluripotent cells (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Specificity protein 1 (SP1) is a ubiquitously expressed transcription factor belonging to the family of C2H2-type zinc finger containing DNA-binding proteins. SP1 binds GC-rich motifs with high affinity and regulates the expression of numerous mammalian genes (1,2). It interacts with many other transcription factors, such as c-Myc, EGR1, and Stat1, and with basal transcription machinery components. SP1 interacts with chromatin-modifying factors, such as histone deacetylases (HDACs) and p300 in chromatin remodeling. Transcriptional activity and stability of SP1 are regulated by post-translational modification, including phosphorylation, acetylation, ubiquitination, and glycosylation (3). Glycosylation of SP1 following insulin treatment leads to increased nuclear localization, while glucagon treatment increases cytoplasmic SP1 levels (4-6). Investigators have found high levels of SP1 in patients with Alzheimer's disease (7).

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

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

Background: Glucocorticoid hormones control cellular proliferation, inflammation, and metabolism through their association with the glucocorticoid receptor (GR)/NR3C1, a member of the nuclear hormone receptor superfamily of transcription factors (1). GR is composed of several conserved structural elements, including a carboxy-terminal ligand-binding domain (which also contains residues critical for receptor dimerization and hormone-dependent gene transactivation), a neighboring hinge region containing nuclear localization signals, a central zinc-finger-containing DNA-binding domain, and an amino-terminal variable region that participates in ligand-independent gene transcription. In the absence of hormone, a significant population of GR is localized to the cytoplasm in an inactive form via its association with regulatory chaperone proteins, such as HSP90, HSP70, and FKBP52. On hormone binding, GR is released from the chaperone complex and translocates to the nucleus as a dimer to associate with specific DNA sequences termed glucocorticoid response elements (GREs), thereby enhancing or repressing transcription of specific target genes (2). It was demonstrated that GR-mediated transcriptional activation is modulated by phosphorylation (3-5). Although GR can be basally phosphorylated in the absence of hormone, it becomes hyperphosphorylated upon binding receptor agonists. It has been suggested that hormone-dependent phosphorylation of GR may determine target promoter specificity, cofactor interaction, strength and duration of receptor signaling, receptor stability, and receptor subcellular localization (3).