Delta-Aminolevulinic Acid Dehydratase (ALAD) Antibody
292.5€ (80 µl)
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935106861
info@markelab.com
name
Delta-Aminolevulinic Acid Dehydratase (ALAD) Antibody
category
Primary Antibodies
provider
Abbexa
reference
abx033007
tested applications
ELISA, WB, IHC, FCM
Description
The ALAD enzyme is composed of 8 identical subunits and catalyzes the condensation of 2 molecules of delta-aminolevulinate to form porphobilinogen (a precursor of heme, cytochromes and other hemoproteins). ALAD catalyzes the second step in the porphyrin and heme biosynthetic pathway; zinc is essential for enzymatic activity. ALAD enzymatic activity is inhibited by lead and a defect in the ALAD structural gene can cause increased sensitivity to lead poisoning and acute hepatic porphyria.
Documents del producto
Instrucciones
Data sheet
Product specifications
| Category | Primary Antibodies |
| Immunogen Target | Delta-Aminolevulinic Acid Dehydratase (ALAD) |
| Host | Rabbit |
| Reactivity | Human |
| Recommended Dilution | WB: 1/1000, IHC-P: 1/50 - 1/100, FCM: 1/10 - 1/50. Not tested in IHC-F. Optimal dilutions/concentrations should be determined by the end user. |
| Clonality | Polyclonal |
| Conjugation | Unconjugated |
| Isotype | IgG |
| Purification | Purified Rabbit Polyclonal Antibody. |
| Size 1 | 80 µl |
| Size 2 | 400 µl |
| Form | Liquid |
| Tested Applications | ELISA, WB, IHC, FCM |
| Buffer | PBS containing 0.09% sodium azide. |
| Availability | Shipped within 5-10 working days. |
| Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | P13716 |
| Alias | ALADH,Porphobilinogen synthase,ALA dehydratase |
| Background | Antibody anti-ALAD |
| Status | RUO |
Descripción
Aminolevulinate Delta Dehydratase (ALAD) is a key enzyme in the heme biosynthesis pathway, catalyzing the condensation of two molecules of aminolevulinic acid (ALA) into porphobilinogen (PBG), a precursor to heme. ALAD is predominantly expressed in the liver and bone marrow, where heme production is critical for hemoglobin synthesis in red blood cells and for cytochrome function in metabolic processes. The enzyme requires zinc as a cofactor for its activity, and mutations or environmental inhibitors, such as lead, can impair ALAD function, leading to disorders such as porphyria or anemia. Lead poisoning inhibits ALAD by displacing zinc, resulting in the accumulation of ALA and associated neurotoxic effects. ALAD mutations can also cause ALAD porphyria, a rare genetic disorder marked by abdominal pain, neuropsychiatric symptoms, and photosensitivity. ALAD is a target of interest for understanding and mitigating lead toxicity and heme-related metabolic disorders.
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