Render Target: STATIC
Render Timestamp: 2024-11-14T10:15:56.722Z
Commit: 3c1f305a63297e594ac8d7bb5424007d592d68be
XML generation date: 2024-09-20 06:17:42.012
Product last modified at: 2024-11-01T18:30:10.514Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Tyrosine Hydroxylase (E2L6M) Rabbit mAb #58844

Filter:
  • WB
  • IHC
  • IF
  • F

    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 55-60
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IHC-Immunohistochemistry 
    • IF-Immunofluorescence 
    • F-Flow Cytometry 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    IHC Leica Bond 1:150 - 1:600
    Immunohistochemistry (Paraffin) 1:150 - 1:600
    Immunofluorescence (Frozen) 1:50 - 1:200
    Immunofluorescence (Immunocytochemistry) 1:50 - 1:200
    Flow Cytometry (Fixed/Permeabilized) 1:400 - 1:1600

    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. Store at –20°C. Do not aliquot the antibody.

    For a carrier free (BSA and azide free) version of this product see product #81242.

    Protocol

    Specificity / Sensitivity

    Tyrosine Hydroxylase (E2L6M) Rabbit mAb recognizes endogenous levels of total tyrosine hydroxylase protein.

    Species Reactivity:

    Human, Mouse, Rat

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of 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).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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