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Monoclonal Antibody Immunoprecipitation Androgen Metabolic Process

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Aromatase is a member of the cytochrome P450 superfamily of enzymes, which are monooxygenases that catalyze reactions involved in drug metabolism and cholesterol and steroid synthesis (1,2). Aromatase is responsible for the conversion of testosterone into 17-β estradiol (2). Aromatase is mainly expressed in the brain (3), ovaries (4), and placenta (5). Aromatase plays an important role in development of the central nervous system during ontogenesis (6,7), gonadal development, and sex differentiation (8,9). Research studies have suggested that inhibition of aromatase may be an effective therapeutic strategy for postmenopausal breast cancers that are estrogen receptor positive (6,10). Mutations in the corresponding aromatase gene are associated with cases of aromatase excess syndrome (AEXS) and aromatase deficiency (AROD) disorders (11-14).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Estrogen receptor α (ERα), a member of the steroid receptor superfamily, contains highly conserved DNA binding and ligand binding domains (1). Through its estrogen-independent and estrogen-dependent activation domains (AF-1 and AF-2, respectively), ERα regulates transcription by recruiting coactivator proteins and interacting with general transcriptional machinery (2). Phosphorylation at multiple sites provides an important mechanism to regulate ERα activity (3-5). Ser104, 106, 118, and 167 are located in the amino-terminal transcription activation function domain AF-1, and phosphorylation of these serine residues plays an important role in regulating ERα activity. Ser118 may be the substrate of the transcription regulatory kinase CDK7 (5). Ser167 may be phosphorylated by p90RSK and Akt (4,6). According to the research literature, phosphorylation at Ser167 may confer tamoxifen resistance in breast cancer patients (4).

$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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The breast cancer susceptibility proteins BRCA1 and BRCA2 are frequently mutated in cases of hereditary breast and ovarian cancers and have roles in multiple processes related to DNA damage, repair, cell cycle progression, transcription, ubiquitination, and apoptosis (1-4). BRCA2 has been shown to be required for localization of Rad51 to sites of double stranded breaks (DSBs) in DNA, and cells lacking BRCA1 and BRCA2 cannot repair DSBs through the Rad51-dependent process of homologous recombination (HR) (5). Numerous DNA damage-induced phosphorylation sites on BRCA1 have been identified, including Ser988, 1189, 1387, 1423, 1457, 1524, and 1542, and kinases activated in a cell cycle-dependent manner, including Aurora A and CDK2, can also phosphorylate BRCA1 at Ser308 and Ser1497, respectively (6-10). Cell cycle-dependent phosphorylation of BRCA2 at Ser3291 by CDKs has been proposed as a mechanism to switch off HR as cells progress beyond S-phase by blocking the carboxy terminal Rad51 binding site (11).

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: CYP17A1, also known as cytochrome P450C17, is a steroidogenic enzyme belonging to the P450 cytochrome superfamily of monooxygenases (1, 2). In humans, CYP17A1 expression is abundantly expressed in the adrenal cortex, where it plays a central role in the androgen synthesis pathway (2). CYP17A1 is the primary target of abiraterone, a synthetic steroid used in the treatment of castration-resistant prostate cancer (CRPC) (3, 4). Abiraterone is converted to the more active form D4A, which antagonizes androgen receptor signaling by inhibiting CYP17A1 and other steroidogenic enzymes (3, 4). This suppresses the synthesis of 5α-dihydrotestosterone (DHT), which is a driver of castration-resistant prostate cancer cell growth (3, 4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: CYP17A1, also known as cytochrome P450C17, is a steroidogenic enzyme belonging to the P450 cytochrome superfamily of monooxygenases (1, 2). In humans, CYP17A1 expression is abundantly expressed in the adrenal cortex, where it plays a central role in the androgen synthesis pathway (2). CYP17A1 is the primary target of abiraterone, a synthetic steroid used in the treatment of castration-resistant prostate cancer (CRPC) (3, 4). Abiraterone is converted to the more active form D4A, which antagonizes androgen receptor signaling by inhibiting CYP17A1 and other steroidogenic enzymes (3, 4). This suppresses the synthesis of 5α-dihydrotestosterone (DHT), which is a driver of castration-resistant prostate cancer cell growth (3, 4).