PMVK is a peroxisomal enzyme that catalyzes the conversion of mevalonate 5-phosphate into mevalonate 5-diphosphate as the fifth reaction of the cholesterol biosynthetic pathway. The deduced 192-amino acid PMVK protein has a calculated molecular mass of about 22 kD. It contains a C-terminal peroxisomal targeting sequence, and a single methionine is removed from the N terminus upon maturation of the protein. Expression is highest in heart and skeletal muscle, with slightly lower levels in liver, kidney, and pancreas, and low but detectable levels in brain, lung, and placenta.
Immunogen
PMVK (167-202) This antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide selected from the C-terminal region of human PMVK.
Physical form
Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide.
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