Recombinant Rat Peptidylglycine alpha-amidating monooxygenase (Pam), partial

Code CSB-MP017417RA
Abbreviation Recombinant Rat Pam protein, partial
MSDS
Size $138
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity
Greater than 95% as determined by SDS-PAGE.
Activity
Not Test
Target Names
Pam
Uniprot No.
Research Area
Others
Alternative Names
PAM
Species
Rattus norvegicus (Rat)
Source
Mammalian cell
Expression Region
36-820aa
Target Protein Sequence
FKETTRSFSNECLGTIGPVTPLDASDFALDIRMPGVTPKESDTYFCMSMRLPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWFCDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNHKDCSGVSVHLTRVPQPLIAGMYLMMSVDTVIPPGEKVVNADISCQYKMYPMHVFAYRVHTHHLGKVVSGYRVRNGQWTLIGRQNPQLPQAFYPVEHPVDVTFGDILAARCVFTGEGRTEATHIGGTSSDEMCNLYIMYYMEAKYALSFMTCTKNVAPDMFRTIPAEANIPIPVKPDMVMMHGHHKEAENKEKSALMQQPKQGEEEVLEQGDFYSLLSKLLGEREDVHVHKYNPTEKTESGSDLVAEIANVVQKKDLGRSDAREGAEHEEWGNAILVRDRIHRFHQLESTLRPAESRAFSFQQPGEGPWEPEPSGDFHVEEELDWPGVYLLPGQVSGVALDSKNNLVIFHRGDHVWDGNSFDSKFVYQQRGLGPIEEDTILVIDPNNAEILQSSGKNLFYLPHGLSIDTDGNYWVTDVALHQVFKLDPHSKEGPLLILGRSMQPGSDQNHFCQPTDVAVEPSTGAVFVSDGYCNSRIVQFSPSGKFVTQWGEESSGSSPRPGQFSVPHSLALVPHLDQLCVADRENGRIQCFKTDTKEFVREIKHASFGRNVFAISYIPGFLFAVNGKPYFGDQEPVQGFVMNFSSGEIIDVFKPVRKHFDMPHDIVASEDGTVYIGDAHTNTVWKFTLTEKMEHRSV
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
Mol. Weight
90.4 kDa
Protein Length
Partial
Tag Info
C-terminal 8xHis-tagged
Form
Liquid or 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
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is 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°C/-80°C. 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.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
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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