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Conditions of optimal ALAD 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
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Introduction
ALAD form porphobilinogen (a precursor of heme, cytochromes and other hemoproteins) by catalyzing the compression of 2 molecules of delta-aminolevulinate. ALAD catalyzes the second step in the porphyrin and heme biosynthetic pathway; zinc is vital for enzymatic activity. ALAD has 8 identical subunits and its enzymatic activity is inhibited by lead. Mutations in the ALAD structural gene are the source for high sensitivity to lead poisoning and acute hepatic porphyria.
BP002539-ENZ-586: Recombinant Human Aminolevulinate Dehydratase (ALAD) Enzyme
Source: E. coli-derived.
A single polypeptide chain containing 354 amino acids (1-330) and having a molecular mass of 38.8 kDa. ALAD is fused to a 24 amino acid His-tag at N-terminus.
Purity: > 85% as determined by SDS-PAGE.
Formulation: The ALAD solution (1 mg/ml) contains 20 mM Tris-HCl buffer (pH 8.0), 100 mM NaCl and 10% 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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