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

Human 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: Immunoprecipitation, Western Blotting

Background: ERC1, an acronym named for previous protein names ELKS (1), RAB6IP2 (2) and CAST (3), is a RIM-binding protein that plays a role in neurotransmitter release and general membrane trafficking in other cell types (2-5). Interaction with the GTP-binding protein Rab6 suggests that it contributes to membrane traffic at the Golgi (2). In addition to its association with membrane trafficking, ERC1 has also been found as an essential part of the IκB kinase (IKK) complex required for the activation of NF-κB, perhaps by recruiting IκBα to the IKK complex (6). Alternative splicing of ERC1 generates 2 proteins with a divergent carboxy terminus, a long and a short form termed ERC1α and ERC1β, respectively. ERC1α is widely expressed, whereas ERC1β and a related family member ERC2 are expressed in the brain (4). Papillary thyroid carcinomas have been identified with the translocation t(10;12)(p11;p13) resulting in a fusion between ERC1 and the receptor tyrosine kinase Ret (1).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Catenin δ-1 (p120 catenin) has an amino-terminal coiled-coil domain followed by a regulatory domain containing multiple phosphorylation sites and a central Armadillo repeat domain of ten linked 42-amino acid repeats. The carboxy-terminal tail has no known function (1). Catenin δ-1 fulfills critical roles in the regulation of cell-cell adhesion as it regulates E-cadherin turnover at the cell surface to determine the level of E-cadherin available for cell-cell adhesion (2). Catenin δ-1 has both positive and negative effects on cadherin-mediated adhesion (3). Actin dynamics are also regulated by catenin δ-1, which modulates RhoA, Rac, and cdc42 proteins (1). Analogous to β-catenin, catenin δ-1 translocates to the nucleus, although its role at this location is unclear. Many studies show that catenin δ-1 is expressed irregularly or is absent in various types of tumor cells, suggesting that catenin δ-1 may function as a tumor suppressor (4).

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

Application Methods: Western Blotting

Background: Translation is the process where amino acid residues are assembled into polypeptides on ribosomes. This process is generally divided into three stages: initiation, elongation and termination. During elongation, mRNA and tRNA pair at the two active sites (A and P sites) on the ribosome. A number of eukaryotic elongation factors (eEFs) are involved in this process in mammalian cells (1). eEF1A, also called elongation factor Tu (EF-Tu), binds GTP and interacts with amino acyl-tRNAs to promote recruitment of amino acyl-tRNAs to the A-site of the ribosome (1). After GTP hydrolysis, GDP-eEF1A leaves the ribosome and is later converted back to the GTP-eEF1A by eEF1B (1). Studies have shown that eEF1A is phosphorylated under certain conditions, indicating that its activity is regulated at the post-translational level (2,3).

$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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Oct-1 (POU2F1) is a ubiquitously expressed, octamer-binding transcription factor containing a POU domain with a homeobox subdomain (1). Oct-1 has been shown to interact with several transcription factors in mediating specific gene expression, including SNAPc (2), OBF-1 (a B-cell transcriptional coactivator protein) (3), TFIIB (4), and TBP (TATA-box-binding protein) (5). Its POU DNA-binding domain allows Oct-1 the flexibility to facilitate the binding and recruitment of several tissue-specific cofactors to either positively or negatively regulate a variety of genes, exerting an important role in development (6).

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

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

Background: Ubiquitinating enzymes (UBEs) catalyze protein ubiquitination, a reversible process countered by deubiquitinating enzyme (DUB) action (1,2). Five DUB subfamilies are recognized, including the USP, UCH, OTU, MJD and JAMM enzymes. Herpesvirus-associated ubiquitin-specific protease (HAUSP, USP7) is an important deubiquitinase belonging to USP subfamily. A key HAUSP function is to bind and deubiquitinate the p53 transcription factor and an associated regulator protein Mdm2, thereby stabilizing both proteins (3,4). In addition to regulating essential components of the p53 pathway, HAUSP also modifies other ubiquitinylated proteins such as members of the FoxO family of forkhead transcription factors and the mitotic stress checkpoint protein CHFR (5,6).

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

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

Background: Lipin 1 was identified as a nuclear protein required for adipose tissue development (1). The expression of Lipin 1 is induced during adipocyte differentiation (1). The abnormal development of adipose tissues caused by mutations in the lipin 1 gene results in lipodystrophy, a condition associated with low body fat, fatty liver, hypertriglyceridemia, and insulin resistance (1). Lipin 1 plays a role in lipid metabolism in various tissues and cell types including liver, muscle, adipose tissues, and neuronal cell lines (2-4). It has dual functions at the molecular level: Lipin 1 serves as a transcriptional coactivator in liver, and a phosphatidate phosphatase in triglyceride and phospholipid biosynthesis pathways (5). Lipin 1 is regulated by mTOR, illustrating a connection between adipocyte development and nutrient-sensing pathways (6). It also mediates hepatic insulin signaling by TORC2/CRTC2 (7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, 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

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
Bovine, Hamster, Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: Pirin is a highly conserved nuclear protein and a member of the cupin superfamily of proteins, all of which contain two conserved β-barrel fold domains (1). Pirin functions as a co-factor for NFI/CTF1 and Bcl-3, implicating it in DNA replication, transcriptional activation and apoptosis (2,3). Both human and bacterial pirins catalyze the di-oxygenation of quercetin, one of a class of widespread naturally occurring flavenoid compounds that have anti-inflammatory and anti-cancer activities (4). Flavenoids exert these beneficial activities by functioning as antioxidants that stabilize cellular free radical molecules and by directly modulating cell signaling pathways involving PI 3-kinase, Akt/PKB, PKC and MAP kinases (5). Quercetin has also been directly implicated in the regulation of NF-κB activity; thus, Pirin may exert its apoptotic functions both by directly regulating Bcl-3/NF-κB activity and by modulating quercetin levels in the cell (6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: DnaJ/Hsp40 proteins are a conserved family of J-domain-containing chaperone proteins that assist in protein folding and stability through their interactions with Hsp70 chaperone proteins (reviewed in 1). DNAJC2, also known as MPP11 (M-phase phosphoprotein 11 protein) or ZRF1, is a component of the ribosome-associated complex (RAC). The RAC is localized to the cytoplasm, where it assists in maintaining appropriate folding of nascent polypeptides by stimulating the ATPase activity of Hsp70 chaperone proteins (2,3). In the nucleus, MPP11 is involved in the activation of transcription through mediation of the switch from polycomb-repressed to active chromatin (4). Previous studies have shown MPP11 is overexpressed in leukemia and head and neck cancer, leading researchers to suggest MPP11 may be a potential therapeutic target (5-7). MPP11 is phosphorylated at serine 47 by S6 kinase, which regulates senescence in fibroblast cells (8).

$327
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. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-Stat4 (Tyr693) (D2E4) Rabbit mAb #4134.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

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, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: KHSRP, also known as KSRP, is a KH domain-containing AU-rich element (ARE) binding protein (1). It recruits degradation machinery and activates mRNA turnover (2). This protein was previously shown to function as a regulator for splicing (3). KHSRP associates with both the Drosha and Dicer multiprotein complexes (4), and controls the biogenesis of some microRNAs by binding to the terminal loops of these microRNA precursors (3). KHSRP is found in neural and non-neural cell types in both the nucleus and the cytoplasm (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: LIM homeobox transcription factor 1 β (Lmx1B) is a member of an evolutionarily conserved family of transcription factors that regulate developmental pattern formation in both vertebrates and invertebrates (1). Numerous developmental studies show that Lmx1B is required for vertebrate dorsoventral limb patterning, as well as normal glomerular basement membrane development and typical differentiation of central serotonergic neurons (2,3).Mutations in the corresponding Lmx1B gene have been associated with nail-patella syndrome (NPS), an autosomal dominant disorder characterized by dysplasia of fingernails, skeletal anomalies and, frequently, renal disease (2). Abnormal developmental disorders such as developmental glaucoma and idiopathic Parkinson’s disease have also been associated with Lmx1B function (4,5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: 5'-3' exoribonuclease 2 (XRN2) is a nuclear exonuclease that degrades RNA containing a 5’-monophosphate to component mononucleotides. XRN2 also plays an important role in the termination of transcription at the 3’-end of genes by displacing RNA polymerase II (RNAPII) from the DNA strand (1,2). According to the ‘torpedo’ model of transcription termination, XRN2 gains access to the 5’ phosphate of the nascent RNA during co-transcriptional polyadenylation site cleavage. XRN2 degrades RNA at a faster rate than RNAPII-mediated RNA synthesis, resulting in the eviction of RNAPII from the template (3-5). In addition, XRN2 is essential for maturation of 5.8S and 28S ribosomal RNA and small nucleolar RNA molecules (2). Several research studies suggest that XRN2 plays a role in the quality control check of RNA molecules. XRN2 co-transcriptionally degrades aberrant nuclear mRNA transcripts that result from defective 5’mRNA capping, splicing, or 3’end formation (6). XRN2 exonuclease rapidly degrades hypomodified tRNA and excess miRNA molecules, indicating that XRN2 likely regulates tRNA and miRNA quality control as well (7-9).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The flightless-I (fliI) gene was first identified in Drosophila mutant screens for genes involved in flight behavior. Homozygous mutant alleles at the fliI locus are embryonic lethal, whereas heterozygous mutations yield a "flightless" phenotype resulting from defects in flight muscle fiber development (1). The encoded protein (flightless-I, FLII) is a highly conserved member of the gelsolin superfamily, defined by the presence of C-terminal gelsolin motifs that function as actin-binding domains (2). Genetic knock-out studies in mice and worms confirmed that Flightless-I plays a critical and highly conserved role in embryonic development, likely through its effects on actin remodeling of the cytoskeleton (3,4). Postnatally, Flightless-I is recognized to play an important role in wound repair (5). Flightless-I protein levels are increased in many wound types, and depletion of Flightless-I protein levels has been shown to accelerate wound repair by promoting fibroblast proliferation and epithelial migration (6-8). Studies in animal models suggest that Flightless-I may inhibit the wound repair process by modulating TGF-β signaling dynamics in the wound environment (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunoprecipitation

Background: Spi-B belongs to the ETS family of transcription factors and activates transcription through direct binding to the PU box (1). Spi-B was identified based on its homology with PU.1/Spi-I (1). The function of Spi-B is most well studied in B cells and plasmacytoid dendritic cells (pDCs). B cells from mice deficient in Spi-B proliferate poorly and die in response to signaling through the B cell receptor (2). In addition, Spi-B(-/-) mice have a defect in germinal center formation (2). Spi-B plays a role in both the development and function of pDCs. It is highly expressed by pDCs and not by monocyte-derived DCs, and overexpression of Spi-B in hematopoietic progenitor cells inhibits development of other lymphoid lineages (3). pDCs from Spi-B(-/-) mice produce less interferon in response to TLR7 and TLR9 stimulation and have lower expression of pDC-specific surface markers (4). Finally, Spi-B is required for differentiation of intestinal microfold cells (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: Lipin 1 was identified as a nuclear protein required for adipose tissue development (1). The expression of Lipin 1 is induced during adipocyte differentiation (1). The abnormal development of adipose tissues caused by mutations in the lipin 1 gene results in lipodystrophy, a condition associated with low body fat, fatty liver, hypertriglyceridemia, and insulin resistance (1). Lipin 1 plays a role in lipid metabolism in various tissues and cell types including liver, muscle, adipose tissues, and neuronal cell lines (2-4). It has dual functions at the molecular level: Lipin 1 serves as a transcriptional coactivator in liver, and a phosphatidate phosphatase in triglyceride and phospholipid biosynthesis pathways (5). Lipin 1 is regulated by mTOR, illustrating a connection between adipocyte development and nutrient-sensing pathways (6). It also mediates hepatic insulin signaling by TORC2/CRTC2 (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Caveolae ("little caves") are 60-80 nm pits representing specialized plasma membrane domains in many cell types. The principal protein component of caveolae is caveolin, a small integral membrane protein composed of three family members, including the widely expressed caveolin-1 and -2, and the muscle-specific caveolin-3 (1). Caveolin proteins are required for caveolae formation and serve as scaffolding proteins for the recruitment of signaling proteins. Research studies in cavelolin-deficient mice implicate cavelolin proteins in several pathologies, including diabetes, cancer, cardiovascular diseases, atherosclerosis, pulmonary disease, and muscular dystrophies (2).The cavin proteins (cavin-1, -2, -3, and -4 in mammals) are a family of caveolae-associated integral membrane proteins involved in the biogenesis and stability of caveolae. Cavin proteins form homo- or hetero-oligomers whose composition is tissue-specific, which may confer distinct functions of caveolae in various tissues (3). Cavin-1 (PTRF), which is widely expressed, is required for caveolae formation and is thought to play roles in lipid metabolism, adipocyte differentiation, and IGF-1 receptor signaling (4-6). Research studies involving prostate cancer suggest that expression of cavin-1 is related to tumor progression and angiogenesis/lymphangiogenesis (7-8).