Recombinant Rat Peptidyl-glycine alpha-amidating monooxygenase (Pam), partial

Code CSB-YP017417RA
MSDS
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Source Yeast
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Code CSB-EP017417RA
MSDS
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Source E.coli
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Code CSB-EP017417RA-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP017417RA
MSDS
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Source Baculovirus
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Code CSB-MP017417RA
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Pam
Uniprot No.
Alternative Names
PamPeptidylglycine 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)]
Species
Rattus norvegicus (Rat)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

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.
Gene References into Functions
  1. Disruption of AP-1-dependent late endosomal trafficking diminishes the ability of PAM to retain copper and produce amidated peptides. PMID: 26170456
  2. Data indicate that H3A mutation eliminates the ability of internalized peptidylglycine alpha-amidating monooxygenase PAM-1 to return to secretory granules. PMID: 24627494
  3. The crystal structure of the oxidized form of PHM complexed with hydrogen peroxide. PMID: 23247335
  4. the structure of the ternary complex of the peptidylglycine-alphahydroxylating monooxygenase (PHM) domain of PAM with molecular oxygen and a peptide that contains a D-amino acid designed to trap the precatalytic complex is presented PMID: 15131304
  5. Recruitment of PAM-1 to secretory vesicles depends on intact N-terminal proANP and on the lumenal domain of PAM-1. Conversely, PAM-1 participates in shaping the proANP-secretory vesicles. PMID: 15539631
  6. PAM activity was lower in cardiac atria of Cu- rats than Cu-adequate (Cu+) rats PMID: 15629125
  7. the appearance of integral membrane PAM at the plasma membrane was stimulated along with hormone secretion in anterior pituitary PMID: 15905171
  8. Data show that ubiquitin is a peptidylglycine alpha-amidating monooxygenase substrate with a (V/K)(amidation) that is similar to other known peptide substrates. PMID: 16098968
  9. expression analysis of PHM in rats and in mouse cells PMID: 16325307
  10. Data show that that thiorphan and tiopronin are substrates for peptidylglycine alpha-amidating monooxygenase. PMID: 16405966
  11. Intermittent hypoxia activates peptidylglycine alpha-amidating monooxygenase in rat brain stem via reactive oxygen species-mediated proteolytic processing. PMID: 18818385

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Subcellular Location
Cytoplasmic vesicle, secretory vesicle membrane; Single-pass membrane protein.
Protein Families
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase family; Copper type II ascorbate-dependent monooxygenase family
Database Links
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