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Polyclonal Antibody Transcription Cofactor Activity

Also showing Polyclonal Antibody Western Blotting Transcription Cofactor Activity

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The mediator complex consists of about 25-30 proteins and is thought to facilitate transcription activation by acting as a molecular bridge between the RNA polymerase II (RNAPII) machinery and transcription factors (1). Mediator is recruited to target genes by transcription factors and plays an essential role in the recruitment and stabilization of the RNAPII transcription complex at promoters, as well as the activation of transcription post RNAPII recruitment (1-5). The mediator complex also plays an important role in creating ‘chromatin loops’ that occur as a result of interactions between the transcription factor bound at distal enhancers and RNAPII bound at the proximal promoter, and works to sustain proper chromatin architecture during active transcription (6-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state complexed with the inhibitory IκB proteins (1-3). Activation occurs via phosphorylation of IκBα at Ser32 and Ser36 followed by proteasome-mediated degradation that results in the release and nuclear translocation of active NF-κB (3-7). IκBα phosphorylation and resulting Rel-dependent transcription are activated by a highly diverse group of extracellular signals including inflammatory cytokines, growth factors, and chemokines. Kinases that phosphorylate IκB at these activating sites have been identified (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state complexed with the inhibitory IκB proteins (1-3). Activation occurs via phosphorylation of IκBα at Ser32 and Ser36 followed by proteasome-mediated degradation that results in the release and nuclear translocation of active NF-κB (3-7). IκBα phosphorylation and resulting Rel-dependent transcription are activated by a highly diverse group of extracellular signals including inflammatory cytokines, growth factors, and chemokines. Kinases that phosphorylate IκB at these activating sites have been identified (8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The mediator complex consists of about 25-30 proteins and is thought to facilitate transcription activation by acting as a molecular bridge between the RNA polymerase II (RNAPII) machinery and transcription factors (1). Mediator is recruited to target genes by transcription factors and plays an essential role in the recruitment and stabilization of the RNAPII transcription complex at promoters, as well as the activation of transcription post RNAPII recruitment (1-5). The mediator complex also plays an important role in creating ‘chromatin loops’ that occur as a result of interactions between the transcription factor bound at distal enhancers and RNAPII bound at the proximal promoter, and works to sustain proper chromatin architecture during active transcription (6-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Zinc finger MYND domain-containing protein 8 (ZMYND8), also referred to as receptor for activated C-kinase 7 (Rack7) and protein kinase C-binding protein 1 (PRKCBP1), is a DNA damage response protein and a transcriptional regulator that is a close homolog of ZMYND11 (BS69) (1). ZMYND8 binds to H3K36me2 and H4K16ac, two histone marks associated with active transcription (2). This protein is targeted to sites of DNA damage within actively transcribed genes, and recruits the H3K4me3-specific histone demethylase KDM5A/JARID1A and nucleosome remodeling and histone deacetylation (NuRD) complex (1-3). Together, these protein complexes mediate transcriptional repression and allow for subsequent double-strand break repair via homologous recombination. ZMYND8 contains a bromodomain and a PWWP domain near its N-terminus, and a MYND domain towards the C-terminus, the latter of which mediates interaction with the NuRD complex (1). ZMYND8 also functions to recruit the H3K4me3-specific histone demethylase KDM5C/JARID1C to enhancer and super-enhancer regions, and functions as a negative regulator of gene expression (4). ZMYND8 and JARID1C are both putative tumor suppressor proteins, and knockdown of either of these proteins leads to derepression of S100 oncogenes (1). ZMYND8 expression is altered in breast and cervical cancer (4, 5), and has been found to be translocated with RELA in at least one patient with acute erythroid leukemia (6). Knock-down of ZMYND8 expression in breast cancer cell lines increases anchorage-independent cell growth, cell migration and invasion, and tumor growth in mouse xenograft models (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: B-cell Oct binding factor-1 (BOB-1/OBF-1) is a B-cell restricted transcriptional coactivator. BOB-1 facilitates transactivation of immunoglobulins and other B-cell specific genes through the binding and activation of the transcription factors Oct-1 and Oct-2 (1-4). Research studies have demonstrated that BOB-1 expression is required for antigen-dependent B-cell maturation (5-7). In pathological conditions such as classical Hodgkin’s disease, loss of BOB-1 expression is thought, in part, to contribute to the defect in immunoglobulin gene expression by Hodgkin and Reed Sternberg cells (8,9). In the context of multiple myeloma, overexpression of BOB-1 has been shown to contribute to malignant plasma cell cell growth, in part, through enhanced transactivation of TNFRSF17/BCMA (10).

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

Application Methods: Western Blotting

Background: Transformation/transcription domain-associated protein (TRRAP) is a highly conserved 434 kDa protein found in various multiprotein complexes, such as SAGA, PCAF, NuA4 and TIP60, which contain histone acetyltransferase (HAT) activity (1-4). TRRAP functions as an adaptor protein by binding directly to the transactivation domains of transcriptional activator proteins and facilitating the recruitment of HAT complexes to acetylate histone proteins and activate transcription (1-5). TRRAP is required for the transcriptional activation and cell transformation activities of c-Myc, E2F1, E2F4, p53 and the adenovirus E1A proteins (1,6,7). TRRAP is also essential in early development and is required at the mitotic checkpoint and for normal cell cycle progression (8,9). In addition, TRRAP has been shown to function in DNA repair. As part of the TIP60 complex, TRRAP is required for the acetylation of histone H4 at double-stranded DNA breaks and subsequent DNA repair by homologous recombination (10). In addition, TRRAP associates with the MRN (MRE11, RAD50, NBS1) complex, which lacks intrinsic HAT activity yet functions in the sensing and subsequent repair of double-stranded breaks by non-homologous DNA end-joining (11). TRRAP shows significant homology to the PI-3 kinase domain of the ATM family of kinases; however, amino acids that map to the catalytic site of the kinase domain are not conserved in TRRAP (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: Transformation/transcription domain-associated protein (TRRAP) is a highly conserved 434 kDa protein found in various multiprotein complexes, such as SAGA, PCAF, NuA4 and TIP60, which contain histone acetyltransferase (HAT) activity (1-4). TRRAP functions as an adaptor protein by binding directly to the transactivation domains of transcriptional activator proteins and facilitating the recruitment of HAT complexes to acetylate histone proteins and activate transcription (1-5). TRRAP is required for the transcriptional activation and cell transformation activities of c-Myc, E2F1, E2F4, p53 and the adenovirus E1A proteins (1,6,7). TRRAP is also essential in early development and is required at the mitotic checkpoint and for normal cell cycle progression (8,9). In addition, TRRAP has been shown to function in DNA repair. As part of the TIP60 complex, TRRAP is required for the acetylation of histone H4 at double-stranded DNA breaks and subsequent DNA repair by homologous recombination (10). In addition, TRRAP associates with the MRN (MRE11, RAD50, NBS1) complex, which lacks intrinsic HAT activity yet functions in the sensing and subsequent repair of double-stranded breaks by non-homologous DNA end-joining (11). TRRAP shows significant homology to the PI-3 kinase domain of the ATM family of kinases; however, amino acids that map to the catalytic site of the kinase domain are not conserved in TRRAP (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Members of the Myc/Max/Mad network function as transcriptional regulators with roles in various aspects of cell behavior including proliferation, differentiation and apoptosis (1). These proteins share a common basic-helix-loop-helix leucine zipper (bHLH-ZIP) motif required for dimerization and DNA-binding. Max was originally discovered based on its ability to associate with c-Myc and found to be required for the ability of Myc to bind DNA and activate transcription (2). Subsequently, Max has been viewed as a central component of the transcriptional network, forming homodimers as well as heterodimers with other members of the Myc and Mad families (1). The association between Max and either Myc or Mad can have opposing effects on transcriptional regulation and cell behavior (1). The Mad family consists of four related proteins; Mad1, Mad2 (Mxi1), Mad3 and Mad4, and the more distantly related members of the bHLH-ZIP family, Mnt and Mga. Like Myc, the Mad proteins are tightly regulated with short half-lives. In general, Mad family members interfere with Myc-mediated processes such as proliferation, transformation and prevention of apoptosis by inhibiting transcription (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Hox, Pbx, and Meis are families of transcription factors that bind DNA via their homeodomains. Members from each family form heterodimers to give rise to complexes with unique DNA binding specificities. Homeodomain containing proteins are frequently involved in normal developmental processes, but can also be associated with tumorigenic states (1). MEIS proteins belong to the TALE (Three Amino Acid Loop Extension) homeobox containing transcription factor family. MEIS1 has been associated with leukemogenesis and neuroblastoma (2,3) while MEIS2 is known to play an important role in the transcriptional program that is induced in normal pancreatic development (4) and cardiogenesis (5).

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

Application Methods: Western Blotting

Background: The 26S proteasome is a highly abundant proteolytic complex involved in the degradation of ubiquitinated substrate proteins. It consists largely of two sub-complexes, the 20S catalytic core particle (CP) and the 19S/PA700 regulatory particle (RP) that can cap either end of the CP. The CP consists of two stacked heteroheptameric β-rings (β1-7) that contain three catalytic β-subunits and are flanked on either side by two heteroheptameric α-rings (α1-7). The RP includes a base and a lid, each having multiple subunits. The base, in part, is composed of a heterohexameric ring of ATPase subunits belonging to the AAA (ATPases Associated with diverse cellular Activities) family. The ATPase subunits function to unfold the substrate and open the gate formed by the α-subunits, thus exposing the unfolded substrate to the catalytic β-subunits. The lid consists of ubiquitin receptors and DUBs that function in recruitment of ubiquitinated substrates and modification of ubiquitin chain topology (1,2). Other modulators of proteasome activity, such as PA28/11S REG, can also bind to the end of the 20S CP and activate it (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Members of the Myc/Max/Mad network function as transcriptional regulators with roles in various aspects of cell behavior including proliferation, differentiation and apoptosis (1). These proteins share a common basic-helix-loop-helix leucine zipper (bHLH-ZIP) motif required for dimerization and DNA-binding. Max was originally discovered based on its ability to associate with c-Myc and found to be required for the ability of Myc to bind DNA and activate transcription (2). Subsequently, Max has been viewed as a central component of the transcriptional network, forming homodimers as well as heterodimers with other members of the Myc and Mad families (1). The association between Max and either Myc or Mad can have opposing effects on transcriptional regulation and cell behavior (1). The Mad family consists of four related proteins; Mad1, Mad2 (Mxi1), Mad3 and Mad4, and the more distantly related members of the bHLH-ZIP family, Mnt and Mga. Like Myc, the Mad proteins are tightly regulated with short half-lives. In general, Mad family members interfere with Myc-mediated processes such as proliferation, transformation and prevention of apoptosis by inhibiting transcription (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Heregulin (HRG), also called neuregulin (NRG1), neu differentiation factor (NDF) or glial growth factor-2 (GGF-2), is a soluble growth factor synthesized as a transmembrane precursor molecule. Metalloproteinases and other proteases catalyze the cleavage of its extracellular domain which is then released and functions as a ligand for ErbB3 and ErbB4 receptor tyrosine kinase. The signaling pathways of HRG-ErbB3/ErbB4 are involved in regulation of cell proliferation, differentiation, invasion, and survival of both normal and malignant tissues (1,2). Abnormality of HRG-ErbB signaling leads to development of a variety of human diseases.HRG family has four isoforms including HRG-1, -2, -3 and -4, which are derived from alternative exon splicing. Moreover, they showed various tissue expression and biological activities (3).