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Monoclonal Antibody Male Gonad Development

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Wilms' Tumor 1 (WT1) is a transcription factor named from Wilms' Tumor 1, an embryonal malignancy of the kidneys that is caused by mutations in the WT1 gene (1). It is highly important in development, particularly of the genitourinary system, and mutations and dysregulation of expression of WT1 result in a variety of syndromes affecting the genitourinal system and other tissues (2-5).WT1 has a myriad of biological functions and a host of interacting partners and target genes (6). It can behave as a transcriptional activator, or a repressor, and can act as an oncogene or a tumor suppressor (7). It exerts influence over the epigenetic landscape, and also has post translational influence of gene expression through RNA interactions (8). The diverse biological roles of WT1 have been attributed to the existence of multiple isoforms and post translation modifications of the protein (9).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Wilms' Tumor 1 (WT1) is a transcription factor named from Wilms' Tumor 1, an embryonal malignancy of the kidneys that is caused by mutations in the WT1 gene (1). It is highly important in development, particularly of the genitourinary system, and mutations and dysregulation of expression of WT1 result in a variety of syndromes affecting the genitourinal system and other tissues (2-5).WT1 has a myriad of biological functions and a host of interacting partners and target genes (6). It can behave as a transcriptional activator, or a repressor, and can act as an oncogene or a tumor suppressor (7). It exerts influence over the epigenetic landscape, and also has post translational influence of gene expression through RNA interactions (8). The diverse biological roles of WT1 have been attributed to the existence of multiple isoforms and post translation modifications of the protein (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: DSS-AHC critical region on the X chromosome protein 1 (DAX1) is an orphan nuclear receptor encoded by the nuclear receptor subfamily 0 group B member 1 (NR0B1) gene. DAX1 possesses an atypical DNA binding domain that allows it to form heterodimeric complexes with DNA binding partners and repress transcriptional activity (1,2). During development, DAX1 is important for establishment of the hypothalamic-pituitary-adrenal gonadal axis. The receptor is essential for development of several important hormone-producing organs that determine this axis, including the adrenal glands, pituitary, hypothalamus, and the male and female reproductive organs (3,4). Research studies suggest that DAX1 plays a role in maintenance of pluripotency in embryonic stem cells (5,6). Loss of DAX1 function through deletion or mutation results in adrenal insufficiency and hypogonadotropic hypogonadism (7), while duplication of the NR0B1 gene on the X-chromosome causes dosage-sensitive sex reversal (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Fanconi anemia (FA) is an autosomal recessive genetic disorder that results in chromosomal breakage, bone marrow failure, hypersensitivity to DNA cross-linking agents (such as mitomycin C), and a predisposition to cancer (1). The ubiquitously expressed FA complementation group A protein (FANCA, FAA) is a component of the FA nuclear complex that also contains FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, and FANCM. In response to DNA damage, the FA nuclear complex induces mono-ubiquitination of FANCD2 and FANCI (2). FANCJ/BRIP1, FANCD1/BRCA2 and FANCN/PALB2 are then recruited to sites of DNA damage along with other DNA repair proteins. FA signaling is important in maintenance of chromosome stability and control of mitosis (3).DNA-damage-dependent localization and stability of FANCA protein regulates FA complex function and localization. Interaction between FANCA protein and the Hsp90 chaperone protein regulates FANCA protein stability and turnover, and may play a role in controlling the FA DNA damage pathway (4). Mutations in the corresponding FANCA gene are responsible for the majority of cases of Fanconi anemia (5).

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

Application Methods: Western Blotting

Background: Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).

$327
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-IGF-I Receptor β (Tyr1135/1136)/Insulin Receptor β (Tyr1150/1151) (19H7) Rabbit mAb #3024.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).

$122
20 µl
$307
100 µl
$719
300 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Secreted Frizzled-related proteins (SFRPs) display homology and structural similarity to the extracellular cysteine-rich Wnt-binding domain of the G protein-coupled receptor Frizzled (1,2). To date, five distinct SFRPs (SFRP1 to 5) have been found in mammalian cells. These secreted proteins typically act as antagonists to Wnt signaling by directly binding and inhibiting Wnt proteins, or by binding Frizzled to block Wnt protein interaction with the receptor (3). The various SFRPs bind and regulate Wnt proteins differentially; these proteins also display distinct expression patterns as they play important roles in regulating development (4-7). SFRP proteins appear to act as tumor suppressors, with loss of expression or function correlating with many invasive forms of cancer. Deletion of the corresponding SFRP1 gene and promoter hypermethylation leading to gene silencing has been reported in a number of cancers. Abnormal expression of SRFP1 and other Wnt signaling proteins is associated with some cases of retinitis pigmentosa (reviewed in 8).

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

Application Methods: Chromatin IP, Western Blotting

Background: There are three members of the steroid receptor co-activator (SRC) family of proteins: SRC-1 (NCoA-1), SRC-2 (TIF2/GRIP1/NCoA-2), and SRC-3 (ACTR/pCIP/RAC3/TRAM-1/AIB1). All SRC family members share significant structural homology and function to stimulate transcription mediated by nuclear hormone receptors and other transcriptional activators such as Stat3, NF-κB, E2F1, and p53 (1-4). Two SRC proteins, SRC-1 and SRC-3, function as histone acetyltransferases (5,6). In addition, all three family members can recruit other histone acetyltransferases (CBP/p300, PCAF) and histone methyltransferases (PRMT1, CARM1) to target promoters and cooperate to enhance expression of many genes (5-8). The SRC proteins play important roles in multiple physiological processes including cell proliferation, cell survival, somatic cell growth, mammary gland development, female reproductive function, and vasoprotection (9). SRC-1 and SRC-3 are conduits for kinase-mediated growth factor signaling to the estrogen receptor and other transcriptional activators. Seven SRC-1 phosphorylation sites and six SRC-3 phosphorylation sites have been identified, which are induced by steroids, cytokines, and growth factors and involve multiple kinase signaling pathways (9-11). Research has shown that all three SRC family members are associated with increased activity of nuclear receptors in breast, prostate, and ovarian carcinomas. According to the literature, SRC-3 is frequently amplified or overexpressed in a number of cancers (12), and SRC-1/PAX3 and SRC-2/MYST3 translocations are found associated with rhabdomyosarcoma and acute myeloid leukemia, respectively (13,14).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Sox9 (D8G9H) Rabbit mAb #82630.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Sox9 is a transcription factor with an HMG-box DNA binding domain that has homology to the HMG domain of the mammalian testis-determining factor, SRY (1). Sox9 regulates several important processes during embryonic development including chondrogenesis, during which it contributes to skeletal formation and digit specification (2,3). Sox9 also coordinates with steroidogenic factor-1 to direct Sertoli cell-specific expression of anti-Mullerian hormone during embryogenesis, thereby contributing to male sex determination (4). In addition, Sox9 is reportedly involved in the maintenance of adult stem cell populations, including multipotent neural stem cells (5), hair follicle stem cells (6), and mammary stem cells (7). Recent interest has focused on the role of Sox9 in tumor biology. For example, research studies have shown that Sox9 expression in lung adenocarcinoma induces a mesenchymal phenotype in tumor cells (8). Other research studies have shown that YAP1 induced upregulation of Sox9 confers cancer stem cell like properties on esophageal cancer cells (9). Moreover, Sox9 expression has been linked with several other tumor types including ovarian, prostate, and pancreatic malignancies (10-12).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct flow cytometry and immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Sox9 (D8G9H) Rabbit mAb #82630.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Sox9 is a transcription factor with an HMG-box DNA binding domain that has homology to the HMG domain of the mammalian testis-determining factor, SRY (1). Sox9 regulates several important processes during embryonic development including chondrogenesis, during which it contributes to skeletal formation and digit specification (2,3). Sox9 also coordinates with steroidogenic factor-1 to direct Sertoli cell-specific expression of anti-Mullerian hormone during embryogenesis, thereby contributing to male sex determination (4). In addition, Sox9 is reportedly involved in the maintenance of adult stem cell populations, including multipotent neural stem cells (5), hair follicle stem cells (6), and mammary stem cells (7). Recent interest has focused on the role of Sox9 in tumor biology. For example, research studies have shown that Sox9 expression in lung adenocarcinoma induces a mesenchymal phenotype in tumor cells (8). Other research studies have shown that YAP1 induced upregulation of Sox9 confers cancer stem cell like properties on esophageal cancer cells (9). Moreover, Sox9 expression has been linked with several other tumor types including ovarian, prostate, and pancreatic malignancies (10-12).

$115
20 µl
$269
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Western Blotting

Background: Sox9 is a transcription factor with an HMG-box DNA binding domain that has homology to the HMG domain of the mammalian testis-determining factor, SRY (1). Sox9 regulates several important processes during embryonic development including chondrogenesis, during which it contributes to skeletal formation and digit specification (2,3). Sox9 also coordinates with steroidogenic factor-1 to direct Sertoli cell-specific expression of anti-Mullerian hormone during embryogenesis, thereby contributing to male sex determination (4). In addition, Sox9 is reportedly involved in the maintenance of adult stem cell populations, including multipotent neural stem cells (5), hair follicle stem cells (6), and mammary stem cells (7). Recent interest has focused on the role of Sox9 in tumor biology. For example, research studies have shown that Sox9 expression in lung adenocarcinoma induces a mesenchymal phenotype in tumor cells (8). Other research studies have shown that YAP1 induced upregulation of Sox9 confers cancer stem cell like properties on esophageal cancer cells (9). Moreover, Sox9 expression has been linked with several other tumor types including ovarian, prostate, and pancreatic malignancies (10-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Insulin receptor (InsR) is a heterodimeric membrane receptor tyrosine kinase. It is comprised of an extracellular α-subunit, containing the ligand binding domain, and a β-subunit containing an extracellular domain, a transmembrane domain and a cytoplasmic tyrosine kinase domain (1). Binding of insulin to InsR results in receptor autophosphorylation, and subsequent tyrosine kinase activation (2). This provides a docking site for various adaptor molecules, including insulin-receptor substrate (IRS), Gab and Shc, phosphorylation of which promotes subsequent activation of multiple downstream signaling pathways including MAPK, PI3K and TC10 (3,4). These events lead to increased glucose uptake and metabolism, and can promote cell growth. Loss of function mutation or desensitization of the InsR are two major contributors to insulin resistance and Type 2 diabetes (5).

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

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

Background: There are three members of the steroid receptor co-activator (SRC) family of proteins: SRC-1 (NCoA-1), SRC-2 (TIF2/GRIP1/NCoA-2), and SRC-3 (ACTR/pCIP/RAC3/TRAM-1/AIB1). All SRC family members share significant structural homology and function to stimulate transcription mediated by nuclear hormone receptors and other transcriptional activators such as Stat3, NF-κB, E2F1, and p53 (1-4). Two SRC proteins, SRC-1 and SRC-3, function as histone acetyltransferases (5,6). In addition, all three family members can recruit other histone acetyltransferases (CBP/p300, PCAF) and histone methyltransferases (PRMT1, CARM1) to target promoters and cooperate to enhance expression of many genes (5-8). The SRC proteins play important roles in multiple physiological processes including cell proliferation, cell survival, somatic cell growth, mammary gland development, female reproductive function, and vasoprotection (9). SRC-1 and SRC-3 are conduits for kinase-mediated growth factor signaling to the estrogen receptor and other transcriptional activators. Seven SRC-1 phosphorylation sites and six SRC-3 phosphorylation sites have been identified, which are induced by steroids, cytokines, and growth factors and involve multiple kinase signaling pathways (9-11). Research has shown that all three SRC family members are associated with increased activity of nuclear receptors in breast, prostate, and ovarian carcinomas. According to the literature, SRC-3 is frequently amplified or overexpressed in a number of cancers (12), and SRC-1/PAX3 and SRC-2/MYST3 translocations are found associated with rhabdomyosarcoma and acute myeloid leukemia, respectively (13,14).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).

$305
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. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Sox9 (D8G9H) Rabbit mAb #82630.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: Sox9 is a transcription factor with an HMG-box DNA binding domain that has homology to the HMG domain of the mammalian testis-determining factor, SRY (1). Sox9 regulates several important processes during embryonic development including chondrogenesis, during which it contributes to skeletal formation and digit specification (2,3). Sox9 also coordinates with steroidogenic factor-1 to direct Sertoli cell-specific expression of anti-Mullerian hormone during embryogenesis, thereby contributing to male sex determination (4). In addition, Sox9 is reportedly involved in the maintenance of adult stem cell populations, including multipotent neural stem cells (5), hair follicle stem cells (6), and mammary stem cells (7). Recent interest has focused on the role of Sox9 in tumor biology. For example, research studies have shown that Sox9 expression in lung adenocarcinoma induces a mesenchymal phenotype in tumor cells (8). Other research studies have shown that YAP1 induced upregulation of Sox9 confers cancer stem cell like properties on esophageal cancer cells (9). Moreover, Sox9 expression has been linked with several other tumor types including ovarian, prostate, and pancreatic malignancies (10-12).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometry and immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Sox9 (D8G8H) Rabbit mAb #82630.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Sox9 is a transcription factor with an HMG-box DNA binding domain that has homology to the HMG domain of the mammalian testis-determining factor, SRY (1). Sox9 regulates several important processes during embryonic development including chondrogenesis, during which it contributes to skeletal formation and digit specification (2,3). Sox9 also coordinates with steroidogenic factor-1 to direct Sertoli cell-specific expression of anti-Mullerian hormone during embryogenesis, thereby contributing to male sex determination (4). In addition, Sox9 is reportedly involved in the maintenance of adult stem cell populations, including multipotent neural stem cells (5), hair follicle stem cells (6), and mammary stem cells (7). Recent interest has focused on the role of Sox9 in tumor biology. For example, research studies have shown that Sox9 expression in lung adenocarcinoma induces a mesenchymal phenotype in tumor cells (8). Other research studies have shown that YAP1 induced upregulation of Sox9 confers cancer stem cell like properties on esophageal cancer cells (9). Moreover, Sox9 expression has been linked with several other tumor types including ovarian, prostate, and pancreatic malignancies (10-12).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Type I insulin-like growth factor receptor (IGF-IR) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell lines and cell types within fetal and postnatal tissues (1-3). Receptor autophosphorylation follows binding of the IGF-I and IGF-II ligands. Three tyrosine residues within the kinase domain (Tyr1131, Tyr1135, and Tyr1136) are the earliest major autophosphorylation sites (4). Phosphorylation of these three tyrosine residues is necessary for kinase activation (5,6). Insulin receptors (IRs) share significant structural and functional similarity with IGF-I receptors, including the presence of an equivalent tyrosine cluster (Tyr1146/1150/1151) within the kinase domain activation loop. Tyrosine autophosphorylation of IRs is one of the earliest cellular responses to insulin stimulation (7). Autophosphorylation begins with phosphorylation at Tyr1146 and either Tyr1150 or Tyr1151, while full kinase activation requires triple tyrosine phosphorylation (8).