Render Target: STATIC
Render Timestamp: 2024-11-05T11:12:36.367Z
Commit: 57f6e368eba1a427377652f2ad915d45d7f340a4
XML generation date: 2024-08-01 15:24:02.499
Product last modified at: 2024-05-30T07:05:06.259Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

Phospho-Tyrosine Hydroxylase (Ser31) Antibody #3370

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY R
    SENSITIVITY Endogenous
    MW (kDa) 55-60
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:50

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Phospho-Tyrosine Hydroxylase (Ser31) Antibody detects endogenous levels of tyrosine hydroxylase only when phosphorylated at Ser31.

    Species Reactivity:

    Rat

    The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

    Species predicted to react based on 100% sequence homology:

    Mouse

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to the sequence surrounding Ser31 of mouse tyrosine hydroxylase. Antibodies are purified by protein A and peptide affinity chromatography.

    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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