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Monoclonal Antibody Immunofluorescence Immunocytochemistry Drug Binding

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: The methylation of deoxyuridine monophosphate (dUMP) to deoxythymidine monophosphate (dTMP) is an essential step in the formation of thymine nucleotides (1,2, reviewed in 3). This process is catalyzed by thymidylate synthase (TS or TYMS), a homodimer composed of two 30 kDa subunits. TS is an intracellular enzyme that provides the sole de novo source of thymidylate, making it a required enzyme in DNA biosynthesis with activity highest in proliferating cells (1). Being the exclusive source of dTMP, investigators have concluded that TS is also an important target for anticancer agents such as 5-fluorouracil (5-FU) (1-5). 5-FU acts as a TS inhibitor and is active against solid tumors such as colon, breast, head, and neck. Research studies have demonstrated that patients with metastases expressing lower levels of TS have a higher response rate to treatment with 5-FU than patients with tumors that have increased levels of TS (5). Researchers continue to investigate TS expression in different types of cancers (6-10).

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

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

Background: Fatty acid synthase (FASN) catalyzes the synthesis of long-chain fatty acids from acetyl-CoA and malonyl-CoA. FASN is active as a homodimer with seven different catalytic activities and produces lipids in the liver for export to metabolically active tissues or storage in adipose tissue. In most other human tissues, FASN is minimally expressed since they rely on circulating fatty acids for new structural lipid synthesis (1).According to the research literature, increased expression of FASN has emerged as a phenotype common to most human carcinomas. For example in breast cancer, immunohistochemical staining showed that the levels of FASN are directly related to the size of breast tumors (2). Research studies also showed that FASN is highly expressed in lung and prostate cancers and that FASN expression is an indicator of poor prognosis in breast and prostate cancer (3-5). Furthermore, inhibition of FASN is selectively cytotoxic to human cancer cells (5). Thus, increased interest has focused on FASN as a potential target for the diagnosis and treatment of cancer as well as metabolic syndrome (6,7).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Fascin is a monomeric, globular protein that plays a central role in regulating the structure and function of the cortical actin cytoskeleton (1). Fascin promotes cross-linkage of parallel actin filaments during the formation of cell protrusions (lamellipodia and filopodia), and therefore plays an important role in regulating cell migration (2). It has been reported that fascin may also regulate filopodia formation by a mechanism independent of its actin-bundling functions (3), though less is known about this mechanism of action. Research studies have shown that increased fascin expression is associated with increased motility and invasiveness of neoplastic cells, including breast, colon, prostate, and esophageal squamous cell carcinomas (4-6). Fascin binds to the armadillo-repeat domain of β-catenin in vitro and in vivo, and has been shown to co-localize with β-catenin and cadherins at the leading edge of migratory cells (7).

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

Application Methods: Chromatin IP, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), 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).

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

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

Background: Fatty acid binding proteins (FABPs) bind to fatty acids and other lipids to function as cytoplasmic lipid chaperones (1,2). They participate in the transport of fatty acids and other lipids to various cellular pathways (2). Research studies have shown that common variants of the human liver fatty acid binding protein gene FABP1 play a role in the development of type 2 diabetes and insulin resistance (3).

$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).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: DNA topoisomerases I and II are nuclear enzymes; type II consists of two highly homologous isoforms: topoisomerase IIα and IIβ. These enzymes regulate the topology of DNA, maintain genomic integrity, and are essential for processes such as DNA replication, recombination, transcription, and chromosome segregation by allowing DNA strands to pass through each other (1). Topoisomerase I nicks and rejoins one strand of the duplex DNA, while topoisomerase II transiently breaks and closes double-stranded DNA (2). Topoisomerases are very susceptible to various stresses. Acidic pH or oxidative stress can convert topoisomerases to DNA-breaking nucleases, causing genomic instability and cell death. DNA-damaging topoisomerase targeting drugs (e.g., etoposide) also convert topoisomerases to nucleases, with the enzyme usually trapped as an intermediate that is covalently bound to the 5+ end of the cleaved DNA strand(s). Research studies have shown that this intermediate leads to genomic instability and cell death. Thus, agents that target topoisomerases are highly sought after cancer chemotherapeutic drugs (3). Ca2+-regulated phosphorylation of topoisomerase IIα at Ser1106 modulates the activity of this enzyme and its sensitivity to targeting drugs (4).

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

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

Background: The mammalian target of rapamycin (mTOR, FRAP, RAFT) is a Ser/Thr protein kinase (1-3) that functions as an ATP and amino acid sensor to balance nutrient availability and cell growth (4,5). When sufficient nutrients are available, mTOR responds to a phosphatidic acid-mediated signal to transmit a positive signal to p70 S6 kinase and participate in the inactivation of the eIF4E inhibitor, 4E-BP1 (6). These events result in the translation of specific mRNA subpopulations. mTOR is phosphorylated at Ser2448 via the PI3 kinase/Akt signaling pathway and autophosphorylated at Ser2481 (7,8). mTOR plays a key role in cell growth and homeostasis and may be abnormally regulated in tumors. For these reasons, mTOR is currently under investigation as a potential target for anti-cancer therapy (9).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: DNA topoisomerases I and II are nuclear enzymes; type II consists of two highly homologous isoforms: topoisomerase IIα and IIβ. These enzymes regulate the topology of DNA, maintain genomic integrity, and are essential for processes such as DNA replication, recombination, transcription, and chromosome segregation by allowing DNA strands to pass through each other (1). Topoisomerase I nicks and rejoins one strand of the duplex DNA, while topoisomerase II transiently breaks and closes double-stranded DNA (2). Topoisomerases are very susceptible to various stresses. Acidic pH or oxidative stress can convert topoisomerases to DNA-breaking nucleases, causing genomic instability and cell death. DNA-damaging topoisomerase targeting drugs (e.g., etoposide) also convert topoisomerases to nucleases, with the enzyme usually trapped as an intermediate that is covalently bound to the 5+ end of the cleaved DNA strand(s). Research studies have shown that this intermediate leads to genomic instability and cell death. Thus, agents that target topoisomerases are highly sought after cancer chemotherapeutic drugs (3). Ca2+-regulated phosphorylation of topoisomerase IIα at Ser1106 modulates the activity of this enzyme and its sensitivity to targeting drugs (4).

$134
20 µl
$336
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: The mammalian target of rapamycin (mTOR, FRAP, RAFT) is a Ser/Thr protein kinase (1-3) that functions as an ATP and amino acid sensor to balance nutrient availability and cell growth (4,5). When sufficient nutrients are available, mTOR responds to a phosphatidic acid-mediated signal to transmit a positive signal to p70 S6 kinase and participate in the inactivation of the eIF4E inhibitor, 4E-BP1 (6). These events result in the translation of specific mRNA subpopulations. mTOR is phosphorylated at Ser2448 via the PI3 kinase/Akt signaling pathway and autophosphorylated at Ser2481 (7,8). mTOR plays a key role in cell growth and homeostasis and may be abnormally regulated in tumors. For these reasons, mTOR is currently under investigation as a potential target for anti-cancer therapy (9).