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Human Drug Catabolic Process

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Cytochrome P450, subfamily 3A, polypeptide 4 (CYP3A4) is a mono-oxygenase enzyme (1) found in the endoplasmic reticulum membrane of liver and prostate microsomes. It is an important enzyme in drug metabolism; it catalyzes phase I oxidation reactions in approximately 50% of drugs in the modern market, as well as steroids, fatty acids, and some carcinogens (2). It is also involved in steroid and cholesterol synthesis (3,4). Expression of CYP3A4 can be induced by glucocorticoids, carcinogens, pesticides, and drugs, which can lead to drug interactions and toxicity (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Cytochrome P450 (CYP) is a family of enzymes that contain a heme group (1). These enzymes, when reduced and bound by carbon monoxide, maximally absorb light of 450 nm (1). Type I cytochrome P450s are found in mitochondria and function in the biosynthesis of essential molecules (1). Type II cytochrome P450s are found in endoplasmic reticulum (1). Some type II cytochrome P450s play a role in the biosynthesis of essential molecules whereas others metabolize xenobiotics (1). Research studies show that cytochrome P450s form various heteromeric complexes with other members of the P450 family influencing their catalytic activities (2-4). CYP1A2 is in the endoplasmic reticulum of hepatocytes and responsible for the breakdown of a variety of xenobiotic substances and bioactivation of carcinogens (2, 5). CYP1 enzymes, including CYP1A2, have been implicated in smoking-related osteoporosis (6). A meta-analysis shows that a particular polymorphism in CYP1A2 is potentially linked to increased cancer risk (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Cytochrome P450 2D6 (CYP2D6) is a member of the cytochrome P450 superfamily of enzymes. CYP2D6 is located in the endoplasmic reticulum where it oxidizes substrates such as drugs and environmental chemicals (1,2). CYP2D6 metabolizes more than 25% of current commonly used drugs including antidepressants, antipsychotics, analgesics, beta-adrenergic blocking agents, antiarrythmics, and antiemetics. The CYP2D6 gene is highly polymorphic in humans, resulting in phenotypes that vary from poor metabolizer to super metabolizer. A patient's CYP2D6 genotype was shown to be a good predictor of drug response and side effects and is thus used to guide treatments (3-5). Although abundantly expressed in liver, CYP2D6 is also expressed in other organs including brain. In brain, CYP2D6 and other CYP family members are expressed in a cell-specific, region-specific manner (6-8). CYP2D6 functions as a neuroprotective enzyme that increases with age and is induced by nicotine and alcohol (9,10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Nitric Oxide Synthase (NOS) catalyzes the formation of nitric oxide (NO) and citruline from L-arginine, oxygen and cofactors. Three family members have been characterized: neuronal NOS (nNOS), which is found primarily in neuronal tissue; inducible NOS (iNOS), which is induced by interferon gamma and lipopolysaccharides in the kidney and cardiovascular system; and endothelial NOS (eNOS), which is expressed in blood vessels (1). NO is a messenger molecule with diverse functions throughout the body including the maintenance of vascular integrity, homeostasis, synaptic plasticity, long-term potentiation, learning, and memory (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Nitric Oxide Synthase (NOS) catalyzes the formation of nitric oxide (NO) and citruline from L-arginine, oxygen and cofactors. Three family members have been characterized: neuronal NOS (nNOS), which is found primarily in neuronal tissue; inducible NOS (iNOS), which is induced by interferon gamma and lipopolysaccharides in the kidney and cardiovascular system; and endothelial NOS (eNOS), which is expressed in blood vessels (1). NO is a messenger molecule with diverse functions throughout the body including the maintenance of vascular integrity, homeostasis, synaptic plasticity, long-term potentiation, learning, and memory (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Nitric Oxide Synthase (NOS) catalyzes the formation of nitric oxide (NO) and citruline from L-arginine, oxygen and cofactors. Three family members have been characterized: neuronal NOS (nNOS), which is found primarily in neuronal tissue; inducible NOS (iNOS), which is induced by interferon gamma and lipopolysaccharides in the kidney and cardiovascular system; and endothelial NOS (eNOS), which is expressed in blood vessels (1). NO is a messenger molecule with diverse functions throughout the body including the maintenance of vascular integrity, homeostasis, synaptic plasticity, long-term potentiation, learning, and memory (2,3).

$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

Application Methods: Western Blotting

Background: Transforming growth factor-β (TGF-β) superfamily members are critical regulators of cell proliferation and differentiation, developmental patterning and morphogenesis, and disease pathogenesis (1-4). TGF-β elicits signaling through three cell surface receptors: type I (RI), type II (RII), and type III (RIII). Type I and type II receptors are serine/threonine kinases that form a heteromeric complex. In response to ligand binding, the type II receptors form a stable complex with the type I receptors allowing phosphorylation and activation of type I receptor kinases (5). The type III receptor, also known as betaglycan, is a transmembrane proteoglycan with a large extracellular domain that binds TGF-β with high affinity but lacks a cytoplasmic signaling domain (6,7). Expression of the type III receptor can regulate TGF-β signaling through presentation of the ligand to the signaling complex. The only known direct TGF-β signaling effectors are the Smad family proteins, which transduce signals from the cell surface directly to the nucleus to regulate target gene transcription (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Transforming growth factor-β (TGF-β) superfamily members are critical regulators of cell proliferation and differentiation, developmental patterning and morphogenesis, and disease pathogenesis (1-4). TGF-β elicits signaling through three cell surface receptors: type I (RI), type II (RII), and type III (RIII). Type I and type II receptors are serine/threonine kinases that form a heteromeric complex. In response to ligand binding, the type II receptors form a stable complex with the type I receptors allowing phosphorylation and activation of type I receptor kinases (5). The type III receptor, also known as betaglycan, is a transmembrane proteoglycan with a large extracellular domain that binds TGF-β with high affinity but lacks a cytoplasmic signaling domain (6,7). Expression of the type III receptor can regulate TGF-β signaling through presentation of the ligand to the signaling complex. The only known direct TGF-β signaling effectors are the Smad family proteins, which transduce signals from the cell surface directly to the nucleus to regulate target gene transcription (8,9).

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

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

Background: The ubiquitin-conjugating (UBC) enzymes HR6A and HR6B are the mammalian orthologues of the Saccharomyces cerevisiae Rad6 gene products (1). In S. cerevisiae, Rad6 facilitates cell cycle progression and ubiquitinates histone H2B (2,3). In vivo phosphorylation of HR6A Ser120 by cyclin-dependent kinases is thought to be important for the coordination and timing of ubiquitination events involved in cell cycle progression (4). In response to DNA damage, HR6A is known to interact physically with p53 and p14ARF, but knockout mice lacking HR6A or HR6B exhibit normal DNA damage responses (5,6). HR6B knockout males exhibit defective spermatogenesis, while HR6A knockout females fail to produce viable offspring (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Adenosine deaminase (ADA) catalyzes adenosine degradation (1). Lack of this enzyme leads to the accumulation of toxic metabolites causing severe combined immunodeficiency (ADA-SCID), an autosomal recessive disorder. Differentiation and function of T cells, B cells, and natural killer cells are impaired in ADA-SCID patients leading to recurrent infections (1,2). Gene therapies for ADA-SCID were reported to correct the metabolic defect and restore the deficient immune function (1-3).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Catalase catalyzes the conversion of hydrogen peroxide to water and oxygen (1). Research studies show that overexpression of this antioxidant enzyme increases the ability of pancreatic β-cells to scavenge reactive oxygen species (ROS), thereby protecting pancreatic β-cells from oxidative stress (2). The pancreatic β-cells overexpressing this enzyme are also protected from hydrogen peroxide-mediated lipotoxicity, providing further evidence for the importance of catalase in the pathogenesis of diabetes (3).

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

Application Methods: Western Blotting

Background: Catalase catalyzes the conversion of hydrogen peroxide to water and oxygen (1). Research studies show that overexpression of this antioxidant enzyme increases the ability of pancreatic β-cells to scavenge reactive oxygen species (ROS), thereby protecting pancreatic β-cells from oxidative stress (2). The pancreatic β-cells overexpressing this enzyme are also protected from hydrogen peroxide-mediated lipotoxicity, providing further evidence for the importance of catalase in the pathogenesis of diabetes (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Catechol-O-methyltransferase (COMT) is an intracellular enzyme that catalyzes the O-methylation and inactivation of catecholamine neurotransmitters and hormones, including dopamine, epinephrine, and norepinephrine (1). Two distinct COMT proteins are generated from separate promoters in cells, including a 28 kDa, membrane-bound protein (mb-COMT), and a soluble protein (s-COMT) of 24 kDa (2,3). The soluble s-COMT is the predominant form of COMT found in peripheral organs, while the mb-COMT protein is more abundant in the central nervous system (4,5).In addition to inactivating endogenous catecholamines, COMT can also inhibit catechol-based drugs used to treat a number of disorders, including Parkinson's disease and schizophrenia. Research studies using COMT inhibitors indicate that these reagents can prolong the bioavailability of psychoactive drugs such as levodopa by preventing O-methylation and subsequent degradation (6). A Val158Met polymorphism in the corresponding COMT gene reduces COMT enzymatic activity and leads to increased cortical dopamine levels (7). Several research studies suggest that this reduced COMT activity is associated with a large number of mental disorders, including schizophrenia, bipolar disorder, attention deficit hyperactivity disorder, obsessive-compulsive disorder, and anorexia nervosa (reviewed in 8).

$348
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Arginase-1 (D4E3M™) XP® Rabbit mAb #93668.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: L-arginine plays a critical role in regulating the immune system (1-3). In inflammation, cancer and certain other pathological conditions, myeloid cell differentiation is inhibited leading to a heterogeneous population of immature myeloid cells, known as myeloid-derived suppressor cells (MDSCs). MDSCs are recruited to sites of cancer-associated inflammation and express high levels of arginase-1 (4). Arginase-1 catalyzes the final step of the urea cycle converting L-arginine to L-ornithine and urea (5). Thus MDSCs increase the catabolism of L-arginine resulting in L-arginine depletion in the inflammatory microenvironment of cancer (4,6). The reduced availability of L-arginine suppresses T-cell proliferation and function and thus contributes to tumor progression (4,6). Arginase-1 is of great interest to researchers looking for a therapeutic target to inhibit the function of MDSCs in the context of cancer immunotherapy (7). In addition, research studies have demonstrated that Arginase-1 distinguishes primary hepatocellular carcinoma (HCC) from metastatic tumors in the liver, indicating its value as a potential biomarker in the diagnosis of HCC (8,9).

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

Application Methods: Flow Cytometry, IHC-Leica® Bond™, Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Western Blotting

Background: L-arginine plays a critical role in regulating the immune system (1-3). In inflammation, cancer and certain other pathological conditions, myeloid cell differentiation is inhibited leading to a heterogeneous population of immature myeloid cells, known as myeloid-derived suppressor cells (MDSCs). MDSCs are recruited to sites of cancer-associated inflammation and express high levels of arginase-1 (4). Arginase-1 catalyzes the final step of the urea cycle converting L-arginine to L-ornithine and urea (5). Thus MDSCs increase the catabolism of L-arginine resulting in L-arginine depletion in the inflammatory microenvironment of cancer (4,6). The reduced availability of L-arginine suppresses T-cell proliferation and function and thus contributes to tumor progression (4,6). Arginase-1 is of great interest to researchers looking for a therapeutic target to inhibit the function of MDSCs in the context of cancer immunotherapy (7). In addition, research studies have demonstrated that Arginase-1 distinguishes primary hepatocellular carcinoma (HCC) from metastatic tumors in the liver, indicating its value as a potential biomarker in the diagnosis of HCC (8,9).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Arginase-1 (D4E3M™) XP® Rabbit mAb #93668.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: L-arginine plays a critical role in regulating the immune system (1-3). In inflammation, cancer and certain other pathological conditions, myeloid cell differentiation is inhibited leading to a heterogeneous population of immature myeloid cells, known as myeloid-derived suppressor cells (MDSCs). MDSCs are recruited to sites of cancer-associated inflammation and express high levels of arginase-1 (4). Arginase-1 catalyzes the final step of the urea cycle converting L-arginine to L-ornithine and urea (5). Thus MDSCs increase the catabolism of L-arginine resulting in L-arginine depletion in the inflammatory microenvironment of cancer (4,6). The reduced availability of L-arginine suppresses T-cell proliferation and function and thus contributes to tumor progression (4,6). Arginase-1 is of great interest to researchers looking for a therapeutic target to inhibit the function of MDSCs in the context of cancer immunotherapy (7). In addition, research studies have demonstrated that Arginase-1 distinguishes primary hepatocellular carcinoma (HCC) from metastatic tumors in the liver, indicating its value as a potential biomarker in the diagnosis of HCC (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: IHC-Leica® Bond™, Immunohistochemistry (Paraffin), Western Blotting

Background: L-arginine plays a critical role in regulating the immune system (1-3). In inflammation, cancer and certain other pathological conditions, myeloid cell differentiation is inhibited leading to a heterogeneous population of immature myeloid cells, known as myeloid-derived suppressor cells (MDSCs). MDSCs are recruited to sites of cancer-associated inflammation and express high levels of arginase-1 (4). Arginase-1 catalyzes the final step of the urea cycle converting L-arginine to L-ornithine and urea (5). Thus MDSCs increase the catabolism of L-arginine resulting in L-arginine depletion in the inflammatory microenvironment of cancer (4,6). The reduced availability of L-arginine suppresses T-cell proliferation and function and thus contributes to tumor progression (4,6). Arginase-1 is of great interest to researchers looking for a therapeutic target to inhibit the function of MDSCs in the context of cancer immunotherapy (7). In addition, research studies have demonstrated that Arginase-1 distinguishes primary hepatocellular carcinoma (HCC) from metastatic tumors in the liver, indicating its value as a potential biomarker in the diagnosis of HCC (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: MMP-13 (collagenase 3) belongs to the matrix metalloproteinase (MMP) superfamily of enzymes that targets many extracellular proteins, including other proteases, growth factors, cell surface receptors, and adhesion molecules (1, 2). MMP-13 is a member of a subgroup of collagenases (including MMP-1, MMP-8, and MMP-18) that play an even more important function targeting fibrillar collagen. MMP-13 is synthesized as a latent proenzyme, and proteolytic removal of the inhibitory propeptide domain is required for enzyme activation. MMP-13 protein levels are regulated at the transcriptional level, via specific transcription factors and via promoter DNA methylation (3, 4). MMP-13 preferentially cleaves Type II collagen, and research studies have shown that aberrant upregulation of MMP-13 activity can lead to cartilage loss and osteoarthritis (5, 6). In addition, MMP-13 has been shown to promote cancer development, in part through enhancing tumor angiogenesis and metastases (7-9), suggesting that collagenase activity may serve as a useful marker of tumor progression (10).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Arginase-1 (D4E3M™) XP® Rabbit mAb #93668.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: L-arginine plays a critical role in regulating the immune system (1-3). In inflammation, cancer and certain other pathological conditions, myeloid cell differentiation is inhibited leading to a heterogeneous population of immature myeloid cells, known as myeloid-derived suppressor cells (MDSCs). MDSCs are recruited to sites of cancer-associated inflammation and express high levels of arginase-1 (4). Arginase-1 catalyzes the final step of the urea cycle converting L-arginine to L-ornithine and urea (5). Thus MDSCs increase the catabolism of L-arginine resulting in L-arginine depletion in the inflammatory microenvironment of cancer (4,6). The reduced availability of L-arginine suppresses T-cell proliferation and function and thus contributes to tumor progression (4,6). Arginase-1 is of great interest to researchers looking for a therapeutic target to inhibit the function of MDSCs in the context of cancer immunotherapy (7). In addition, research studies have demonstrated that Arginase-1 distinguishes primary hepatocellular carcinoma (HCC) from metastatic tumors in the liver, indicating its value as a potential biomarker in the diagnosis of HCC (8,9).