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TH Rabbit anti-Human, Mouse, Rat, Polyclonal, Proteintech

Rabbit Polyclonal Antibody

145.00 € - 410.00 €

Specifications

Antigen TH
Concentration 0.21 mg/mL
Applications Western Blot, Immunofluorescence, Immunocytochemistry, Immunohistochemistry (Paraffin), Immunoprecipitation
Classification Polyclonal
Conjugate Unconjugated
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Products 2
Product Code Brand Quantity Price Quantity & Availability  
Product Code Brand Quantity Price Quantity & Availability  
16804425
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Proteintech
25859-1-AP-20UL
20 μL
145.00 €
20µL
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16894415
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Proteintech
25859-1-AP-150UL
150 μL
410.00 €
150µL
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Description

Description

Tyrosine hydroxylase (TH) is an enzyme involved in the synthesis of catecholamine neurotransmitters dopamine, epinephrine, and norepinephrine. In all species, catecholamine synthesis is regulated by the interaction of TH with a cofactor, tetrahydrobiopterin (BH4). BH4 binds to the TH catalytic domain, resulting in enzymatic activity. Unlike TH in non-primate species, four human TH mRNA splice variants (hTH1-hTH4) have been isolated. These variants are identical in their catalytic domain, but differ in their N-terminal, regulatory domains. TH is also responsible for the conversion of L-tyrosine to L-dopa. TH plays a key role in the physiology of adrenergic neurons. The role of TH in the synthesis of catecholamine neurotransmitters suggests a correlation between the enzyme and a number of neuropathogenic diseases including: Parkinson′s disease, schizophrenia, Segawa syndrome, and dystonia, as well as a variety of cardiovascular diseases.
Specifications

Specifications

TH
Western Blot, Immunofluorescence, Immunocytochemistry, Immunohistochemistry (Paraffin), Immunoprecipitation
Unconjugated
Rabbit
Human, Mouse, Rat
P04177, P07101, P24529
21823, 25085, 7054
TH Fusion Protein Ag23075
Primary
-20°C
TH
0.21 mg/mL
Polyclonal
Liquid
RUO
PBS with 50% glycerol and 0.1% sodium azide; pH 7.3
TH, TYH, Tyrosine 3 hydroxylase, Tyrosine 3 monooxygenase, tyrosine hydroxylase
TH
IgG
Antigen Affinity Chromatography
Antibody
Videos
SDS
Documents

Documents

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