Peptidylglycine α-amidating monooxygenase (PAM) is expressed in endocrine cells and neurons. It consists of two enzyme activities- peptidyl-glycine α-hydroxylating monoxygenase (PHM) and peptidyl-α-hydroxyglycine amidating lyase (PAL). The PAM gene is localized on human chromosome 5q21.1.
Immunogen
Peptide with sequence C-DQEKEDDGSESEE from the C Terminus of the protein sequence according to NP_000910.2; NP_620121.1; NP_620176.1; NP_620177.1.
Biochem/physiol Actions
Peptidylglycine α-amidating monooxygenase (PAM) has a role in the biosynthesis of bioactive peptides. It is involved in C-terminal α-amidation, which influences the activity of regulatory peptides of the respiratory tract.
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Physical form
Supplied at 0.5 mg/mL in Tris saline with 0.02% sodium azide and 0.5% bovine serum albumin.
The endocytic pathways of a secretory granule membrane protein in HEK293 cells: PAM and EGF traverse a dynamic multivesicular body network together.
Back N, et al.
European Journal of Cell Biology, 96(5), 407-417 (2017)
Peptidylglycine alpha-amidating monooxygenase: a multifunctional protein with catalytic, processing, and routing domains.
Eipper BA, et al.
Protein Science, 2(4), 489-497 (1993)
Distribution of peptidyl-glycine alpha-amidating mono-oxygenase (PAM) enzymes in normal human lung and in lung epithelial tumors.
Saldise L, et al.
The Journal of Histochemistry and Cytochemistry, 44(1), 3-12 (1996)
Localization of the gene encoding peptidylglycine alpha-amidating monooxygenase (PAM) to human chromosome 5q14-5q21.
Ouafik LH, et al.
Genomics, 18(2), 319-321 (1993)
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