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Mouse Anti-PAM Recombinant Antibody (CBYC-P152) (CBMAB-P0719-YC)

Provided herein is a Mouse monoclonal antibody against Human Peptidylglycine Alpha-Amidating Monooxygenase. The antibody can be used for immunoassay techniques, such as ELISA.
See all PAM antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBYC-P152
Antibody Isotype
IgG2a, κ
Application
ELISA

Basic Information

Specificity
Human
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at-20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Peptidylglycine Alpha-Amidating Monooxygenase
Introduction
PAM is a multifunctional protein. The encoded preproprotein is proteolytically processed to generate the mature enzyme. This enzyme includes two domains with distinct catalytic activities, a peptidylglycine alpha-hydroxylating monooxygenase (PHM) domain and a peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) domain. These catalytic domains work sequentially to catalyze the conversion of neuroendocrine peptides to active alpha-amidated products. Alternative splicing results in multiple transcript variants, at least one of which encodes an isoform that is proteolytically processed.
Entrez Gene ID
5066
UniProt ID
P19021
Alternative Names
Peptidylglycine Alpha-Amidating Monooxygenase; Peptidyl-Alpha-Hydroxyglycine Alpha-Amidating Lyase; Peptidylglycine Alpha-Hydroxylating Monooxygenase; Pancreatic Peptidylglycine Alpha-Amidating Monooxygenase; Peptidyl-Glycine Alpha-Amidating Monooxygenase; Peptidyl Alpha-Amidating Enzyme;
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 (PubMed:12699694).
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 (PubMed:12699694).
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 (PubMed:12699694).
Similarly, catalyzes the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate (By similarity).
Biological Process
Central nervous system developmentIEA:Ensembl
Fatty acid primary amide biosynthetic processISS:UniProtKB
Heart developmentIEA:Ensembl
LactationIEA:Ensembl
Limb developmentIEA:Ensembl
Long-chain fatty acid metabolic processIEA:Ensembl
Maternal process involved in female pregnancyIEA:Ensembl
OdontogenesisIEA:Ensembl
Ovulation cycle processIEA:Ensembl
Peptide amidationManual Assertion Based On ExperimentIDA:UniProtKB
Protein amidationIEA:Ensembl
Regulation of actin cytoskeleton organizationIEA:Ensembl
Regulation of protein secretionIEA:Ensembl
Regulation of transcription by RNA polymerase IIIEA:Ensembl
Response to copper ionIEA:Ensembl
Response to estradiolIEA:Ensembl
Response to glucocorticoidIEA:Ensembl
Response to hypoxiaIEA:Ensembl
Response to pHIEA:Ensembl
Response to xenobiotic stimulusIEA:Ensembl
Response to zinc ionManual Assertion Based On ExperimentIDA:UniProtKB
Toxin metabolic processIEA:Ensembl
Cellular Location
Cytoplasmic vesicle, secretory vesicle membrane
Secretory granules.
Isoform 1
Membrane
Isoform 2
Membrane
Isoform 3
Secreted
Secreted from secretory granules.
Isoform 4
Secreted
Secreted from secretory granules.
Topology
Intragranular: 31-863
Helical: 864-887
Cytoplasmic: 888-973

Ilina, Y., Kaufmann, P., Melander, O., Press, M., Thuene, K., & Bergmann, A. (2023). Immunoassay-based quantification of full-length peptidylglycine alpha-amidating monooxygenase in human plasma. Scientific Reports, 13(1), 10827.

Umapathysivam, M. M., Araldi, E., Hastoy, B., Dawed, A. Y., Vatandaslar, H., Sengupta, S., ... & Gloyn, A. L. (2023). Type 2 diabetes risk alleles in peptidyl-glycine alpha-amidating monooxygenase influence GLP-1 levels and response to GLP-1 receptor agonists. medRxiv.

Morrison, D. G. (2022). Heterologous production of recombinant peptidylglycine α-amidating monooxygenase for the production of biosimilar α-amidated peptides.

Sim, J., Marginean, H., Jirovec, A., Vickers, M. M., Marginean, E. C., Asmis, T. R., ... & Goodwin, R. A. (2022). 895P Correlating peptidylglycine alpha-amidating monooxygenase (PAM) expression with clinicopathologic variables in gastrointestinal (GI) neuroendocrine tumors (NETs). Annals of Oncology, 33, S957.

Merkler, D., Hawley, A., Eipper, B., & Mains, R. (2021). Peptidylglycine α-amidating monooxygenase as a therapeutic target or biomarker. Authorea Preprints.

Mamoor, S. (2020). The peptidylglycine alpha-amidating monooxygenase, PAM, is differentially expressed in viral co-infections.

Bäck, N., Luxmi, R., Powers, K. G., Mains, R. E., & Eipper, B. A. (2020). Peptidylglycine α-amidating monooxygenase is required for atrial secretory granule formation. Proceedings of the National Academy of Sciences, 117(30), 17820-17831.

Donlon, J., & Ryan, P. (2019). Peptidylglycine monooxygenase activity of monomeric species of growth hormone. Heliyon, 5(9).

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For research use only. Not intended for any clinical use.

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