Bifunctional enzyme that catalyzes amidation of the C-terminus of proteins . Alpha-amidation is present at the C-terminus of many endocrine hormones and neuropeptides and is required for their activity . C-terminal amidation also takes place in response to protein fragmentation triggered by oxidative stress, promoting degradation of amidated protein fragments by the proteasome . Alpha-amidation involves two sequential reactions, both of which are catalyzed by separate catalytic domains of the enzyme . The first step, catalyzed by peptidyl alpha-hydroxylating monooxygenase (PHM) domain, is the copper-, ascorbate-, and O2- dependent stereospecific hydroxylation (with S stereochemistry) at the alpha-carbon (C-alpha) of the C-terminal glycine of the peptidylglycine substrate . The second step, catalyzed by the peptidylglycine amidoglycolate lyase (PAL) domain, is the zinc-dependent cleavage of the N-C-alpha bond, producing the alpha-amidated peptide and glyoxylate . Similarly, catalyzes the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate (By similarity). .

p19021

Peptidyl-glycine alpha-amidating monooxygenase (PAM) [Includes: Peptidylglycine alpha-hydroxylating monooxygenase (PHM) (EC 1.14.17.3); Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (EC 4.3.2.5) (Peptidylamidoglycolate lyase) (PAL)],PAM,PAL, PHM, PAM, Peptidylamidoglycolate lyase, Peptidyl-glycine alpha-amidating monooxygenase

Human, Mouse, Rat

WB,IHC,ELISA

WB 1:500-1:2000
IHC 1:50-1:300
ELISA 1:5000-1:20000

109kD

Rabbit

Recombinant Human PAM (Phe21-Cys288).

Polyclonal

IgG

Purified by antigen affinity column.

0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300.

Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Store at 4℃ short term (1-2 weeks). Store at -20℃ 12 months.