Human Recombinant PAM protein, His Tag (V2LY-0526-LY5960)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant PAM protein, His Tag consist of Amino Acid: 1-710 and predicts a molecular mass of 78.68 kDa.
Molecule Mass
78.68 kDa
Verified
HPLC
Sequence
Amino Acid: 1-710
Species
Human

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

Purity
≥90% as determined by SDS-PAGE. ≥90% as determined by SEC-HPLC.
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Peptidylglycine Alpha-Amidating Monooxygenase
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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