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Mouse Phytoalexin Metabolic Process

Also showing Mouse Catecholamine Biosynthetic Process

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: 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: Immunoprecipitation, Western Blotting

Background: L-DOPA decarboxylase (DDC) is a pyridoxal 5-phosphate (PLP)-dependent enzyme that catalyzes the decarboxylation of L-DOPA to dopamine (1) and L-5HTP to serotonin (2). By catalyzing the reaction to produce dopamine, DDC is involved in many important metabolic processes and plays a central role in the complex neuroendocrine-immune regulatory network (1). DDC is expressed in the central nervous system (3), but has also been detected in some peripheral organs such as the liver and adrenal gland, as well as leukocytes of rat and human (1). DDC is thought to be the sole enzyme responsible for the synthesis of the trace amines 2-phenylethylamine, p-tyramine, and tryptamine, which are considered to act as neuromodulators (2,4). DDC is also regarded as a general biomarker for neuroendocrine tumors (3).

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), 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).

$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: Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), 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).