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The antibody against PAM was raised in rabbit using the Recombinant Human Peptidyl-glycine alpha-amidating monooxygenase protein (338-497AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA, WB, IHC, IF.
The antibody against PAM was raised in rabbit using the Recombinant Human Peptidyl-glycine alpha-amidating monooxygenase protein (338-497AA) as the immunogen. This antibody exists as a non-conjugated isotype IgG, purified by protein G with a purity greater than 95%. This antibody has been validated on ELISA, WB, IHC, IF.
$299.00
| Cat.No | ADC-06824A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | PAM |
| Form | Liquid | Species Reactivity | Human |
| Isotype | IgG | Storage Buffer | 0.01M PBS, 0.03% Proclin 300; Constituents: 50% Glycerol, PH 7.4 |
| Purification Method | >95%, Protein G purified | Conjugate | Non-conjugated |
| Application | ELISA, IF, IHC, WB | Storage | Upon receipt |
| Immunogen Description | Recombinant Human Peptidyl-glycine alpha-amidating monooxygenase protein (338-497AA) | Target Species | Human |
|---|---|---|---|
| Immunogen Sequence | Complete sequences for the immunogen, target protein, and peptides are available upon request. | Uniprot ID | P19021 |
Uniprot Id
P19021
Target Species
Human
Target Name
PAM
Target Full Name
Peptidyl-glycine alpha-amidating monooxygenase
Target Function
Bifunctional enzyme that catalyzes the post-translational modification of inactive peptidylglycine precursors to the corresponding bioactive alpha-amidated peptides, a terminal modification in biosynthesis of many neural and endocrine peptides. 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 monoxygenase (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.
Target Subcellular Location
Cytoplasmic vesicle, secretory vesicle membrane; Single-pass membrane protein.; [Isoform 1]: Membrane; Single-pass type I membrane protein.; [Isoform 2]: Membrane; Single-pass type I membrane protein.; [Isoform 3]: Secreted. Note=Secreted from secretory granules.; [Isoform 4]: Secreted. Note=Secreted from secretory granules.
Target Protein Families
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase family; Copper type II ascorbate-dependent monooxygenase family
Target Synonyms
AMD_HUMAN; PAL; PAM; Pancreatic peptidylglycine alpha amidating monooxygenase; Peptidyl alpha amidating enzyme; Peptidyl alpha hydroxyglycine alpha amidating lyase; Peptidyl-alpha-hydroxyglycine alpha-amidating lyase; Peptidylamidoglycolate lyase; Peptidylglycine 2 hydroxylase; Peptidylglycine alpha amidating monooxygenase; Peptidylglycine alpha hydroxylating monooxygenase; PHM
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