Recombinant Human PAM Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 4837-AM

R&D Systems, part of Bio-Techne
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4837-AM-010
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Key Product Details

Source

NS0

Accession #

P19021

Conjugate

Unconjugated

Applications

Enzyme Activity

View all PAM Proteins and Enzymes »

Product Specifications

Source

Mouse myeloma cell line, NS0-derived human PAM protein
Met1-Val817, with a C-terminal 10-His tag

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain at 5 μg per lane.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Phe21

Predicted Molecular Mass

90 kDa

SDS-PAGE

79-92 kDa, reducing conditions

Activity

Measured by its ability to convert Hippurate to Benzamide and Glyoxylate.
The specific activity is >1000 pmol/min/μg, as measured under the described conditions.

Formulation, Preparation and Storage

4837-AM
Formulation Supplied as a 0.2 μm filtered solution in Tris and NaCl.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.

Background: PAM

Pedptidylglycine alpha-Amidating Monooxygenase (PAM) catalyzes the C-terminal amidation that is required for the function of a number of peptide hormones (1). PAM possesses two enzymatic activities on a single polypeptide chain (2), due to the presence of a peptidylglycine alpha‑hydroxylating monooxygenase (PHM) domain and a peptidyl‑ alpha‑hydroxyglycine alpha‑amidating lyase (PAL) domain. The C-terminal glycines of precursor peptides are hydroxylated at the glycine  alpha carbon by the PHM activity in a reaction that requires ascorbate, then the PAL activity completes the amidation, releasing glyoxylate in the process. PAM is required for the biosynthesis of peptides such as Substance P, neuropeptide Y, oxytocin, vasopressin, and calcitonin (3). PAM is highly expressed in tissues that synthesize bioactive peptides, such as the thyroid and pituitary glands. The enzyme is generally stored in secretory granules, but soluble secreted forms have been observed (3). Recombinant human PAM was expressed as a C-terminally truncated protein lacking its transmembrane and cytosolic domains to facilitate its secretion.

References

  1. Kizer J.S. et al. (1986) Endocrinol. 118:2262.
  2. Perkins S.N. et al. (1990) Biochem. Biophys. Res. Commun. 171:926.
  3. Eipper B.A. et al. (1993) Protein Sci. 2:489.

Long Name

Peptidylglycine Alpha-Amidating Monooxygenase

Alternate Names

PAL, PHM

Entrez Gene IDs

5066 (Human); 18484 (Mouse); 25508 (Rat)

Gene Symbol

PAM

UniProt

P19021

Additional PAM Products

Product Documents for Recombinant Human PAM Protein, CF

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Product Specific Notices for Recombinant Human PAM Protein, CF

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