ALAD Human

Aminolevulinate Dehydratase Human Recombinant
Cat. No.
BT25458
Source
E.coli.
Synonyms
Aminolevulinate delta-dehydratase, ALADH, PBGS, Porphobilinogen synthase, delta-aminolevulinic acid dehydratase, EC 4.2.1.24.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

ALAD Human Recombinant produced in E. coli is a single polypeptide chain containing 354 amino acids (1-330) and having a molecular mass of 38.8kDa.
ALAD is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Delta-aminolevulinate dehydratase (ALAD) is responsible for the creation of porphobilinogen, a key component in the production of heme, cytochromes, and other hemoproteins. It achieves this by facilitating the condensation of two delta-aminolevulinate molecules. This enzymatic reaction, catalyzed by ALAD, represents the second step in the biosynthesis of porphyrin and heme. The enzyme's activity is dependent on zinc and is inhibited by lead. Genetic mutations affecting the ALAD structural gene can lead to increased susceptibility to lead poisoning and acute hepatic porphyria.
Description
Recombinant human ALAD, produced in E. coli, is a single polypeptide chain with a molecular weight of 38.8kDa. It consists of 354 amino acids (1-330) and includes a 24 amino acid His-tag fused at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
A sterile, colorless solution, free from particulate matter.
Formulation
The ALAD solution is provided at a concentration of 1mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0), 100mM NaCl, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the solution should be kept at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. Adding a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. Repeated freezing and thawing of the solution should be avoided.
Purity
The purity of ALAD is determined to be greater than 85% using SDS-PAGE analysis.
Synonyms
Aminolevulinate delta-dehydratase, ALADH, PBGS, Porphobilinogen synthase, delta-aminolevulinic acid dehydratase, EC 4.2.1.24.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMQPQSV LHSGYFHPLL RAWQTATTTL NASNLIYPIF VTDVPDDIQP ITSLPGVARY GVKRLEEMLR PLVEEGLRCV LIFGVPSRVP KDERGSAADS EESPAIEAIH LLRKTFPNLL VACDVCLCPY TSHGHCGLLS ENGAFRAEES RQRLAEVALA YAKAGCQVVA PSDMMDGRVE AIKEALMAHG LGNRVSVMSY SAKFASCFYG PFRDAAKSSP AFGDRRCYQL PPGARGLALR AVDRDVREGA DMLMVKPGMP YLDIVREVKD KHPDLPLAVY HVSGEFAMLW HGAQAGAFDL KAAVLEAMTA FRRAGADIII TYYTPQLLQW LKEE.

Product Science Overview

Structure and Function

Aminolevulinate Dehydratase is a zinc-dependent enzyme that binds two molecules of ALA per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen . The enzyme is encoded by the ALAD gene located on chromosome 9 in humans . The enzyme’s activity is essential for the production of heme, an important component of hemoglobin, myoglobin, and various cytochromes.

Biological Importance

The enzyme is highly active in the liver and erythroid cells, where heme synthesis is most prominent . It is involved in several biological processes, including:

  • Heme biosynthetic process: Essential for the production of heme, which is vital for oxygen transport and cellular respiration.
  • Response to metal ions: The enzyme’s activity can be affected by the presence of metal ions such as lead, zinc, and mercury .
  • Response to oxidative stress: Plays a role in the cellular response to oxidative stress and other environmental factors .
Clinical Significance

Deficiency or inhibition of ALAD can lead to various medical conditions, including:

  • Lead poisoning: Lead ions can inhibit ALAD activity, leading to a buildup of ALA and subsequent symptoms of lead poisoning .
  • Porphyria: Genetic mutations in the ALAD gene can cause a form of porphyria known as ALAD porphyria, characterized by abdominal pain, neuropathy, and other symptoms .
Recombinant ALAD

Recombinant ALAD is produced using genetic engineering techniques to express the human ALAD gene in a host organism, such as bacteria or yeast. This allows for the production of large quantities of the enzyme for research and therapeutic purposes. Recombinant ALAD is used in studies to understand the enzyme’s structure, function, and role in various diseases, as well as in the development of potential treatments for conditions related to ALAD deficiency.

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