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Conditions of optimal AMD1 Enzyme performance should be determined experimentally by the investigator.
Price/availability/specifications subject to change without notice. Unless otherwise indicated, our catalog and customized products are for research use only and not intended for human or animal diagnostic or therapeutic use.
Phone: 1-617-401-8149
Fax: 1-617-606-5019
Email: message@sydlabs.com
Or leave a message with a formal purchase
order (PO) Or credit card.
Introduction
Adenosylmethionine decarboxylase proenzyme (AMD1) is synthesized originally as an inactive proenzyme. Putrescine stimulates both the proenzyme processing and the catalytic activity. The catalytic activity is inhibited by iodoacetic acid. The active enzyme formation entails a self-maturation process in which the active site pyruvoyl group is produced from an internal serine residue using an autocatalytic post-translational modification.
BP002508-ENZ-624: Recombinant Human Adenosylmethionine Decarboxylase 1 (AMD1) Enzyme
Source: E. coli-derived.
A single polypeptide chain containing 292 amino acids (68-334) and having a molecular mass of 33.4 kDa. AMD1 is fused to a 25 amino acid His-tag at N-terminus.
Purity: > 80% as determined by SDS-PAGE.
Formulation: The AMD1 solution (0.5 mg/ml) contains 20 mM Tris-HCl buffer (pH 8.0), 100 mM NaCl, 1 mM DTT and 20% glycerol.
Shipping: The product is shipped with ice pack. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70°C as supplied.
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