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Mouse Hormone Metabolic Process

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: SHP-2 (PTPN11) is a ubiquitously expressed, nonreceptor protein tyrosine phosphatase (PTP). It participates in signaling events downstream of receptors for growth factors, cytokines, hormones, antigens, and extracellular matrices in the control of cell growth, differentiation, migration, and death (1). Activation of SHP-2 and its association with Gab1 is critical for sustained Erk activation downstream of several growth factor receptors and cytokines (2). In addition to its role in Gab1-mediated Erk activation, SHP-2 attenuates EGF-dependent PI3 kinase activation by dephosphorylating Gab1 at p85 binding sites (3). SHP-2 becomes phosphorylated at Tyr542 and Tyr580 in its carboxy-terminus in response to growth factor receptor activation (4). These phosphorylation events are thought to relieve basal inhibition and stimulate SHP-2 tyrosine phosphatase activity (5). Mutations in the corresponding gene result in a pair of clinically similar disorders (Noonan syndrome and LEOPARD syndrome) that may result from abnormal MAPK regulation (6).

$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 mouse cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-SHP-2 (Tyr580) (D66F10) Rabbit mAb #5431.
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Flow Cytometry

Background: SHP-2 (PTPN11) is a ubiquitously expressed, nonreceptor protein tyrosine phosphatase (PTP). It participates in signaling events downstream of receptors for growth factors, cytokines, hormones, antigens, and extracellular matrices in the control of cell growth, differentiation, migration, and death (1). Activation of SHP-2 and its association with Gab1 is critical for sustained Erk activation downstream of several growth factor receptors and cytokines (2). In addition to its role in Gab1-mediated Erk activation, SHP-2 attenuates EGF-dependent PI3 kinase activation by dephosphorylating Gab1 at p85 binding sites (3). SHP-2 becomes phosphorylated at Tyr542 and Tyr580 in its carboxy-terminus in response to growth factor receptor activation (4). These phosphorylation events are thought to relieve basal inhibition and stimulate SHP-2 tyrosine phosphatase activity (5). Mutations in the corresponding gene result in a pair of clinically similar disorders (Noonan syndrome and LEOPARD syndrome) that may result from abnormal MAPK regulation (6).

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

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

Background: SHP-2 (PTPN11) is a ubiquitously expressed, nonreceptor protein tyrosine phosphatase (PTP). It participates in signaling events downstream of receptors for growth factors, cytokines, hormones, antigens, and extracellular matrices in the control of cell growth, differentiation, migration, and death (1). Activation of SHP-2 and its association with Gab1 is critical for sustained Erk activation downstream of several growth factor receptors and cytokines (2). In addition to its role in Gab1-mediated Erk activation, SHP-2 attenuates EGF-dependent PI3 kinase activation by dephosphorylating Gab1 at p85 binding sites (3). SHP-2 becomes phosphorylated at Tyr542 and Tyr580 in its carboxy-terminus in response to growth factor receptor activation (4). These phosphorylation events are thought to relieve basal inhibition and stimulate SHP-2 tyrosine phosphatase activity (5). Mutations in the corresponding gene result in a pair of clinically similar disorders (Noonan syndrome and LEOPARD syndrome) that may result from abnormal MAPK regulation (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: SHP-2 (PTPN11) is a ubiquitously expressed, nonreceptor protein tyrosine phosphatase (PTP). It participates in signaling events downstream of receptors for growth factors, cytokines, hormones, antigens, and extracellular matrices in the control of cell growth, differentiation, migration, and death (1). Activation of SHP-2 and its association with Gab1 is critical for sustained Erk activation downstream of several growth factor receptors and cytokines (2). In addition to its role in Gab1-mediated Erk activation, SHP-2 attenuates EGF-dependent PI3 kinase activation by dephosphorylating Gab1 at p85 binding sites (3). SHP-2 becomes phosphorylated at Tyr542 and Tyr580 in its carboxy-terminus in response to growth factor receptor activation (4). These phosphorylation events are thought to relieve basal inhibition and stimulate SHP-2 tyrosine phosphatase activity (5). Mutations in the corresponding gene result in a pair of clinically similar disorders (Noonan syndrome and LEOPARD syndrome) that may result from abnormal MAPK regulation (6).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: SHP-2 (PTPN11) is a ubiquitously expressed, nonreceptor protein tyrosine phosphatase (PTP). It participates in signaling events downstream of receptors for growth factors, cytokines, hormones, antigens, and extracellular matrices in the control of cell growth, differentiation, migration, and death (1). Activation of SHP-2 and its association with Gab1 is critical for sustained Erk activation downstream of several growth factor receptors and cytokines (2). In addition to its role in Gab1-mediated Erk activation, SHP-2 attenuates EGF-dependent PI3 kinase activation by dephosphorylating Gab1 at p85 binding sites (3). SHP-2 becomes phosphorylated at Tyr542 and Tyr580 in its carboxy-terminus in response to growth factor receptor activation (4). These phosphorylation events are thought to relieve basal inhibition and stimulate SHP-2 tyrosine phosphatase activity (5). Mutations in the corresponding gene result in a pair of clinically similar disorders (Noonan syndrome and LEOPARD syndrome) that may result from abnormal MAPK regulation (6).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: SHP-2 (PTPN11) is a ubiquitously expressed, nonreceptor protein tyrosine phosphatase (PTP). It participates in signaling events downstream of receptors for growth factors, cytokines, hormones, antigens, and extracellular matrices in the control of cell growth, differentiation, migration, and death (1). Activation of SHP-2 and its association with Gab1 is critical for sustained Erk activation downstream of several growth factor receptors and cytokines (2). In addition to its role in Gab1-mediated Erk activation, SHP-2 attenuates EGF-dependent PI3 kinase activation by dephosphorylating Gab1 at p85 binding sites (3). SHP-2 becomes phosphorylated at Tyr542 and Tyr580 in its carboxy-terminus in response to growth factor receptor activation (4). These phosphorylation events are thought to relieve basal inhibition and stimulate SHP-2 tyrosine phosphatase activity (5). Mutations in the corresponding gene result in a pair of clinically similar disorders (Noonan syndrome and LEOPARD syndrome) that may result from abnormal MAPK regulation (6).

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: The orphan nuclear receptor, steroidogenic factor 1 (STF-1, also called Ad4BP), is encoded by the NR5A1 gene and plays an instrumental role in directing the transcriptional control of steroidogenesis (1). Initially identified as a tissue-specific transcriptional regulator of cytochrome P450 steroid hydroxylases, research studies of both global (2) and tissue-specific knockout mice (3-6) have demonstrated that STF-1 is required for the development of adrenal glands, gonads, ventromedial hypothalamus, and for the proper functioning of pituitary gonadotropes. Indeed, humans with mutations that render STF-1 transcriptionally inactive can present with testicular failure, ovarian failure, and adrenal insufficiency (7,8). Furthermore, dysregulation of STF-1 has been linked to diseases such as endometriosis (9) and adrenocortical carcinoma (10).Like other nuclear hormone receptors, STF-1 has a modular domain structure composed of an amino-terminal zinc finger DNA-binding domain, a ligand-binding domain, a carboxy-terminal AF-2 activation domain, and a hinge region with AF-1-like activation activity. STF-1 also contains a fushi tarazu factor 1 box, which functions as an accessory DNA binding domain (11). STF-1 is primarily phosphorylated at Ser203, which is thought to enhance its transcriptional activity by promoting complex formation with transcriptional cofactors (12). In addition to phosphorylation at Ser203, STF-1 is subject to SUMO conjugation and acetylation at ε-amino groups of target lysine residues. Whereas SUMOylation represses STF-1 function (13,14), acetylation enhances its transcriptional activity (15).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Huntington's Disease (HD) is a fatal neurodegenerative disorder characterized by psychiatric, cognitive, and motor dysfunction. Neuropathology of HD involves specific neuronal subpopulations: GABA-ergic neurons of the striatum and neurons within the cerebral cortex selectively degenerate (1,2). The genetic analysis of HD has been the flagship study of inherited neurological diseases from initial chromosomal localization to identification of the gene.Huntingtin is a large (340-350 kD) cytosolic protein that may be involved in a number of cellular functions such as transcription, gastrulation, neurogenesis, neurotransmission, axonal transport, neural positioning, and apoptosis (2,3). The HD gene from unaffected individuals contains between 6 and 34 CAG trinucleotide repeats, with expansion beyond this range causing the onset of disease symptoms. A strong inverse correlation exists between the age of onset in patients and the number of huntingtin gene CAG repeats encoding a stretch of polyglutamine peptides (1,2). The huntingtin protein undergoes numerous post-translational modifications including phosphorylation, ubiquitination, sumoylation, palmitoylation, and cleavage (2). Phosphorylation of Ser421 by Akt can partially counteract the toxicity that results from the expanded polyglutamine tract. Varying Akt expression in the brain correlates with regional differences in huntingtin protein phosphorylation; this pattern inversely correlates with the regions that are most affected by degeneration in diseased brain (2). A key step in the disease is the proteolytic cleavage of huntingtin protein into amino-terminal fragments that contain expanded glutamine repeats and translocate into the nucleus. Caspase mediated cleavage of huntingtin at Asp513 is associated with increased polyglutamine aggregate formation and toxicity. Phosphorylation of Ser434 by CDK5 protects against cleavage (2,3).

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Huntington's Disease (HD) is a fatal neurodegenerative disorder characterized by psychiatric, cognitive, and motor dysfunction. Neuropathology of HD involves specific neuronal subpopulations: GABA-ergic neurons of the striatum and neurons within the cerebral cortex selectively degenerate (1,2). The genetic analysis of HD has been the flagship study of inherited neurological diseases from initial chromosomal localization to identification of the gene.Huntingtin is a large (340-350 kD) cytosolic protein that may be involved in a number of cellular functions such as transcription, gastrulation, neurogenesis, neurotransmission, axonal transport, neural positioning, and apoptosis (2,3). The HD gene from unaffected individuals contains between 6 and 34 CAG trinucleotide repeats, with expansion beyond this range causing the onset of disease symptoms. A strong inverse correlation exists between the age of onset in patients and the number of huntingtin gene CAG repeats encoding a stretch of polyglutamine peptides (1,2). The huntingtin protein undergoes numerous post-translational modifications including phosphorylation, ubiquitination, sumoylation, palmitoylation, and cleavage (2). Phosphorylation of Ser421 by Akt can partially counteract the toxicity that results from the expanded polyglutamine tract. Varying Akt expression in the brain correlates with regional differences in huntingtin protein phosphorylation; this pattern inversely correlates with the regions that are most affected by degeneration in diseased brain (2). A key step in the disease is the proteolytic cleavage of huntingtin protein into amino-terminal fragments that contain expanded glutamine repeats and translocate into the nucleus. Caspase mediated cleavage of huntingtin at Asp513 is associated with increased polyglutamine aggregate formation and toxicity. Phosphorylation of Ser434 by CDK5 protects against cleavage (2,3).

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

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

Background: Forkhead box protein A1 (FoxA1, HNF3α) is a transcription factor required for the development of endoderm-derived organs, such as liver, lung, and prostate (1). FoxA1 functions as a pioneer factor that is recruited primarily to the distant enhancers to change chromatin structure for transcription in a cell type-specific manner (2,3). The FoxA1 transcription factor is implicated in various diseases, playing a role in hormone-dependent disorders such as breast and prostate cancers (4). The treatment of relapsing-remitting multiple sclerosis patients with IFN-β results in FoxA1-induced stimulation of a novel population of FoxA1(+) regulatory T-cells, suggesting a possible immunosuppressive role for FoxA1 (5).

$108
250 PCR reactions
500 µl
SimpleChIP® Mouse MYT-1 Promoter Primers contain a mix of forward and reverse PCR primers that are specific to a region of the mouse myelin transcription factor 1 (MYT-1) promoter. These primers can be used to amplify DNA that has been isolated using chromatin immunoprecipitation (ChIP). Primers have been optimized for use in SYBR® Green quantitative real-time PCR and have been tested in conjunction with SimpleChIP® Enzymatic Chromatin IP Kits #9002 and #9003 and ChIP-validated antibodies from Cell Signaling Technology®. The MYT-1 gene is repressed in most cell types and is bound by polycomb group proteins such as Ezh2, SUZ12, Rnf2 and Bmi-1. MYT-1 exon 1 is also enriched for histone H3 Lys27 tri-methylation and histone H2A Lys119 ubiquitylation.
REACTIVITY
Mouse

Background: The chromatin immunoprecipitation (ChIP) assay is a powerful and versatile technique used for probing protein-DNA interactions within the natural chromatin context of the cell (1,2). This assay can be used to either identify multiple proteins associated with a specific region of the genome or to identify the many regions of the genome bound by a particular protein (3-6). ChIP can be used to determine the specific order of recruitment of various proteins to a gene promoter or to "measure" the relative amount of a particular histone modification across an entire gene locus (3,4). In addition to histone proteins, the ChIP assay can be used to analyze binding of transcription factors and co-factors, DNA replication factors, and DNA repair proteins. When performing the ChIP assay, cells are first fixed with formaldehyde, a reversible protein-DNA cross-linking agent that "preserves" the protein-DNA interactions occurring in the cell (1,2). Cells are lysed and chromatin is harvested and fragmented using either sonication or enzymatic digestion. Fragmented chromatin is then immunoprecipitated with antibodies specific to a particular protein or histone modification. Any DNA sequences that are associated with the protein or histone modification of interest will co-precipitate as part of the cross-linked chromatin complex and the relative amount of that DNA sequence will be enriched by the immunoselection process. After immunoprecipitation, the protein-DNA cross-links are reversed and the DNA is purified. Standard PCR or quantitative real-time PCR are often used to measure the amount of enrichment of a particular DNA sequence by a protein-specific immunoprecipitation (1,2). Alternatively, the ChIP assay can be combined with genomic tiling micro-array (ChIP on chip) techniques, high throughput sequencing (ChIP-Seq), or cloning strategies, all of which allow for genome-wide analysis of protein-DNA interactions and histone modifications (5-8). SimpleChIP® primers have been optimized for amplification of ChIP-isolated DNA using real-time quantitative PCR and provide important positive and negative controls that can be used to confirm a successful ChIP experiment.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Glucuronidation is a major pathway that enhances the elimination of lipophilic xenobiotics and endobiotics to more more water soluble compounds for excretion (1,2). The UDP-glucuronosyltransferase (UGT) superfamily catalyzes the glucuronidation of the glycosyl group of a nucleotide sugar to a variety of endogenous and exogenous compounds. Over 100 UGT mammalian gene products have been described and have been divided into subfamilies based on sequence identities (3). The UGT1 subfamily consists of a number of gene products resulting from alternative splicing. These UGT products can differ in tissue expression and substrate specificity. Also, marked differences in the individual expression of UGT isoforms can account for differences in drug metabolism.

$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: Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Pro-Opio-Melano-Cortin (POMC) is a precursor protein expressed in the pituitary and the brain where it is processed into several peptide hormones and neuropeptides. Among these peptides are ACTH, α- and β-MSH, β-and γ-LPH, CLIP, β-endorphin, and N-POMC (1). POMC is involved in hypothalamic circuits regulating feeding behavior and POMC-producing neurons promote satiety (2). POMC neurons are also the target of leptin and insulin for the promotion of the browning of white fat (3).

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

Application Methods: Western Blotting

Background: Adiponectin, also termed AdipoQ, Acrp30, apM1 and GBP28, is an adipokine expressed exclusively in brown and white adipocytes (1). It is secreted into the blood and exists in three major forms: a low molecular weight trimer, a medium molecular weight hexamer and a high molecular weight multimer (1). Adiponectin levels are decreased in obese and insulin-resistant mice and humans (2), suggesting that this adipokine is critical to maintain insulin sensitivity. Adiponectin stimulates the phosphorylation of AMPKα at Thr172 and activates AMPK in skeletal muscle (3). It also stimulates glucose uptake in myocytes (3). The block of AMPK activation by a dominant-negative AMPKα2 isoform inhibits the effect of adiponectin on glucose uptake, indicating that adiponectin stimulates glucose uptake and increases insulin sensitivity through its action on AMPK (3). Adiponectin mutants that are not able to form oligomers larger than trimers have no effect on the AMPK pathway (4). Mutations that render adiponectin unable to form high molecular weight multimers are associated with human diabetes (4), indicating the importance of multimerization for adiponectin activity.

$303
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

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

Background: Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the synthesis of the neurotransmitter dopamine and other catecholamines. TH functions as a tetramer, with each subunit composed of a regulatory and catalytic domain, and exists in several different isoforms (1,2). This enzyme is required for embryonic development since TH knockout mice die before or at birth (3). Levels of transcription, translation and posttranslational modification regulate TH activity. The amino-terminal regulatory domain contains three serine residues: Ser9, Ser31 and Ser40. Phosphorylation at Ser40 by PKA positively regulates the catalytic activity of TH (4-6). Phosphorylation at Ser31 by CDK5 also increases the catalytic activity of TH through stabilization of TH protein levels (7-9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Reverse orientation c-erbA gene α (Rev-erbα, EAR-1, or NR1D1) is a widely expressed member of the orphan nuclear receptor family of proteins (1). Rev-erbα is highly expressed in adipose tissue, skeletal muscle, brain and liver, and regulates cellular proliferation and differentiation. Expression increases during differentiation in adipocytes and ectopic expression of Rev-erbα potentiates the adipocyte differentiation of 3T3-L1 cells (2). In addition, expression oscillates with circadian rhythm in liver cells and Rev-erbα regulates expression of BMAL1, ApoA-I and ApoC-III, all key regulators of circadian rhythm (3-7). Phosphorylation of Rev-erbα Ser55 and Ser59 by GSK-3β appears to stabilize Rev-erbα protein levels and is important for synchronizing and maintaining the circadian clock (8). Rev-erbα also regulates inflammation by targeting the NF-κB responsive genes IL-6 and COX-2 (9). Rev-erbα lacks the activation function 2 domain required for ligand-dependent activation of transcription by other members of the nuclear receptor family; thus it behaves as a constitutive repressor protein, recruiting the nuclear receptor co-repressor (N-CoR)/HDAC3 complex to target genes to repress transcription (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Peroxisome proliferator-activated receptor γ (PPARγ) is a member of the ligand-activated nuclear receptor superfamily and functions as a transcriptional activator (1). PPARγ is preferentially expressed in adipocytes as well as in vascular smooth muscle cells and macrophage (2). Besides its role in mediating adipogenesis and lipid metabolism (2), PPARγ also modulates insulin sensitivity, cell proliferation and inflammation (3). PPARγ transcriptional activity is inhibited by MAP kinase phosphorylation of PPARγ at Ser84 (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: Peroxisome proliferator-activated receptor γ (PPARγ) is a member of the ligand-activated nuclear receptor superfamily and functions as a transcriptional activator (1). PPARγ is preferentially expressed in adipocytes as well as in vascular smooth muscle cells and macrophage (2). Besides its role in mediating adipogenesis and lipid metabolism (2), PPARγ also modulates insulin sensitivity, cell proliferation and inflammation (3). PPARγ transcriptional activity is inhibited by MAP kinase phosphorylation of PPARγ at Ser84 (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: The human retinoid X receptors (RXRs) are encoded by three distinct genes (RXRα, RXRβ, and RXRγ) and bind selectively and with high affinity to the vitamin A derivative, 9-cis-retinoic acid. RXRs are type-II nuclear hormone receptors that are largely localized to the nuclear compartment independent of ligand binding. Nuclear RXRs form heterodimers with nuclear hormone receptor subfamily 1 proteins, including thyroid hormone receptor, retinoic acid receptors, vitamin D receptor, peroxisome proliferator-activated receptors, liver X receptors, and farnesoid X receptor (1). Since RXRs heterodimerize with multiple nuclear hormone receptors, they play a central role in transcriptional control of numerous hormonal signaling pathways by binding to cis-acting response elements in the promoter/enhancer region of target genes (2).