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.
Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
Target:
The synthetic peptide sequence used to generate the antibody AP7092b was selected from the C-term region of human PMVK. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
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