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  • Pfu Aminopeptidase I
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Edman degradation and protein sequencing: Pfu N-acetyl Deblocking Aminopeptidase (Ac-DAP)

Pfu N-acetyl Deblocking Aminopeptidase (Ac-DAP) is a unique exo-type aminopeptidase that liberates blocking groups (formyl, acetyl, and myristyl) from proteins and peptides, releasing amino acids until it reaches the first X-Pro bond. This enzyme has a wide range of substrate specificity and is used to determine short stretches of amino acid sequence in blocked proteins and peptides via mass spectrometry. An additional advantage of using Pfu Ac-DAP is that, since its amino terminus is acetylated, the enzyme itself is not subject to Edman degradation.

Pfu N-acetyl Deblocking Aminopeptidase (Ac-DAP) is a unique exo-type aminopeptidase that liberates blocking groups (formyl, acetyl, and myristyl) from proteins and peptides, releasing amino acids until it reaches the first X-Pro bond. This enzyme has a wide range of substrate specificity and is used to determine short stretches of amino acid sequence in blocked proteins and peptides via mass spectrometry. An additional advantage of using Pfu Ac-DAP is that, since its amino terminus is acetylated, the enzyme itself is not subject to Edman degradation. Therefore, even if a high enzyme to substrate (E/S) ratio is used (e.g., E/S = 0.5–1), protein sequencing can follow Edman degradation without the need for an extra purification step.

NOTE: Pfu Ac-DAP cannot act on non-denatured proteins; therefore, the protein sample must be completely denatured by carboxymethylation for Pfu Ac-DAP digestion.

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Cat. # Product Size License Quantity Details
7340 Pfu N-acetyl Deblocking Aminopeptidase (Ac-DAP) 50 ug USD $235.00

Pfu N-acetyl Deblocking Aminopeptidase (Ac-DAP) is a unique exo-type aminopeptidase that liberates blocking groups (formyl, acetyl, and myristyl), and then releases the subsequent amino acids from proteins and peptides until it reaches the first X-Pro bond. This enzyme has a wide range of substrate specificities and is used to determine short stretches of amino acid sequence of blocked proteins and peptides whose sequence can be determined by Mass Spectrometry. In addition, since the amino terminus of Ac-DAP is acetylated, its amino acid sequence cannot be determined by Edman degradation. Therefore, even if a high E/S ratio is used (for example, E/S = 0.5-1), the amino acid sequence of the target protein or peptide can still be determined by Edman Degradation without requiring separation from the enzyme.

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Our products are to be used for Research Use Only. They may not be used for any other purpose, including, but not limited to, use in humans, therapeutic or diagnostic use, or commercial use of any kind. Our products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without our prior written approval.

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7340: Pfu N-acetyl Deblocking Aminopeptidase (Ac-DAP)

7340: Pfu N-acetyl Deblocking Aminopeptidase (Ac-DAP)

More Information

Used for the liberation of N-terminal formyl, acetyl, and myristyl blocking groups from proteins

Components

  • Buffer (5X)
    Once thawed, the buffer should be stored at 4°C. Avoid additional freeze-thaw cycles.

    Volume: 1 ml
    Components: 250 mM N-Ethylmorpholine-AcOH buffer (pH 8.0, 0.5 mM CoCl2)
    Once thawed, the buffer should be stored at 4°C. Avoid additional freeze-thaw cycles.

  

Source

Recombinant yeast containing the gene encoding Pyrococcus furiosus Ac-DAP.

Storage

−20°C. Once thawed, the enzyme solution should be stored at 4°C. The thawed enzyme and buffer are stable for at least 3 months at 4°C.

Notes

This enzyme cannot react with proteins containing higher order structures; protein samples should be denatured by chemical procedures such as carboxymethylation. This enzyme cannot react with proteins blotted onto PVDF membranes.

Properties

  • Specific activity: >8 units/mg
  • Protein concentration: 1 mg/ml
  • Molecular weight: 38,639 Da (mass spectrometry), ~451 kDa (sedimentation equilibrium method)
  • Activator: CoCl2
  • Inhibitor: Amastatin, EDTA
  • Optimum pH: 6.5–9.0
  • Optimum Temperature: 85–95°C
  • Thermal stability: Enzyme retains 100% activity after 48 hr at 50°C in the supplied buffer (pH 8.0, 0.1 mM Co2+)
  • N-terminal amino acid sequence: Ac-MDDYELLKKVVEADGV...

Form

In a solution of 50 mM N-Ethylmorpholine-AcOH buffer (pH 8.0)

Definition of activity

One unit of activity corresponds to the amount of enzyme required to hydrolyze 1 µmol of leucine-p-nitroanilide at 75°C and pH 8.0 in one minute.

Additional product information

Please see the product's Certificate of Analysis for information about storage conditions, product components, and technical specifications. Please see the Kit Components List to determine kit components. Certificates of Analysis and Kit Components Lists are located under the Documents tab.

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  • Baculovirus titration kits early access program
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