Render Target: SSR
Render Timestamp: 2024-10-24T19:57:05.550Z
Commit: 56767fe525c928647c8401233a175d0d607d385d
XML generation date: 2024-04-05 20:46:35.024
Product last modified at: 2024-10-18T12:30:12.000Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77

Tyrosine Hydroxylase (LNC1) Mouse mAb #45648

Filter:
  • WB
  • IP
  • IF

    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 55-60
    Source/Isotype Mouse IgG1 kappa
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    • IF-Immunofluorescence 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:100
    Immunofluorescence (Frozen) 1:100 - 1:200
    Immunofluorescence (Immunocytochemistry) 1:200 - 1:800

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. This product is stable for 36 months when stored at -20C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Tyrosine Hydroxylase (LNC1) Mouse mAb recognizes endogenous levels of total tyrosine hydroxylase protein.

    Species Reactivity:

    Human, Mouse, Rat

    Source / Purification

    Monoclonal antibody is produced by immunizing animals against human tyrosine hydroxylase protein.

    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 post-translational 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).
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