epitope mapping within an internal region of SAHH of human origin
recommended for detection of S-adenosyl-L-homocysteine hydrolase of mouse, rat and human origin by WB, IP, IF and ELISA; also reactive with additional species, including equine, canine, bovine and porcine
SAHH Background Information SAHH (S-adenosylhomocysteine hydrolase), also known as AHCY, is a 432 amino acid cytoplasmic protein that localizes to the melanosome, a melanin-containing organelle. An essential component of amino acid biosynthesis, SAHH catalyzes the reversible hydrolysis of S-adenosylhomocysteine (SAH) to produce adenosine and L-homocysteine. Through its catalytic activity, SAHH regulates the intracellular levels of SAH and may play a key role in controlling methyltransferase reactions. SAHH exists as a homotetramer that can bind one NAD per subunit and is involved in the activated methyl cycle (a reaction in which the methyl group of methionine is activated by the formation of S-adenosylmethionine). Defects in the gene encoding SAHH result in elevated levels of methionine which cause hypermethioninemia, a disease characterized by sluggishness, muscle weakness and liver problems.
SAHH (W-20)
画像をクリックして拡大する
SAHH (W-20): sc-55759. Western blot analysis of SAHH expression in non-transfected: sc-117752 (A) and mouse SAHH transfected: sc-127505 (B) 293T whole cell lysates.
SAHH (W-20): sc-55759. Western blot analysis of SAHH expression in non-transfected 293T: sc-117752 (A), mouse SAHH transfected 293T: sc-127504 (B) and HEL 92.1.7 (C) whole cell lysates.
SAHH (W-20): sc-55759. Immunofluorescence staining of methanol-fixed HeLa cells showing cytoplasmic localization.
