|IP||4-6 μL/mg of lysate|
**********Please Note: Optimal concentrations/dilutions should be determined by the end user.**********
Mouse THOP1 was immunoprecipitated using:
Lane A:0.5 mg K562 Whole Cell Lysate2 µL anti-Mouse THOP1 rabbit polyclonal antibody and 15 μl of 50 % Protein G agarose.Primary antibody:
Anti-Mouse THOP1 rabbit polyclonal antibody,at 1:200 dilutionSecondary antibody:
Dylight 800-labeled antibody to rabbit IgG (H+L), at 1:5000 dilutionDeveloped using the odssey technique.
Performed under reducing conditions.Predicted band size: 80 kDa
Observed band size: 80 kDa
Anti-THOP1 rabbit polyclonal antibody at 1:500 dilution
Lane A: HCT116 Whole Cell Lysate
Lane B: HELA Whole Cell Lysate
Lane C: K562 Whole Cell Lysate
Lane D: 293T Whole Cell LysateLysates/proteins at 30 μg per lane.
Goat Anti-Rabbit IgG H&L (Dylight800) at 1/10000 dilution.Developed using the Odyssey technique.
Performed under reducing conditions.Predicted band size:79 kDa
Observed band size:72 kDa
THOP1, also known as Thimet oligopeptidase 1, Thimet oligopeptidase, EC 220.127.116.11, or EP24.15, is a zinc(II) endopeptidase implicated in the processing of numerous physiological peptides. As an intracellular enzyme, highly expressed in the brain, kidneys and neuroendocrine tissue, THOP1 has been proposed to metabolize peptides within cells, thereby affecting antigen presentation and G protein-coupled receptor signal transduction. Its substrates is gonadotrophin-releasing hormone (GnRH), an important hypothalamic hormone that regulates the synthesis and release of oestradiol and facilitates female sexual behaviour. THOP1 against toxic effects of Abeta in the early stages of Alzheimer disease (AD) pathology, and suggest that the observed increase in THOP1 expression might be part of a compensatory defense mechanism of the brain against an increased Abeta load.