Human Delta-Aminolevulinic Acid Dehydratase (ALAD) Protein
234€ (2 µg)
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935106861
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name
Human Delta-Aminolevulinic Acid Dehydratase (ALAD) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx073793
tested applications
SDS-PAGE
Description
Aminolevulinate Dehydratase is a recombinant enzyme.
Documents del producto
Instrucciones
Data sheet
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Delta-Aminolevulinic Acid Dehydratase (ALAD) |
| Host | E. coli |
| Recommended Dilution | Optimal dilutions/concentrations should be determined by the end user. |
| Origin | Human |
| Expression | Recombinant |
| Purity | > 85% (SDS-PAGE) |
| Size 1 | 2 µg |
| Size 2 | 10 µg |
| Size 3 | 1 mg |
| Form | Liquid |
| Tested Applications | SDS-PAGE |
| Availability | Shipped within 5-10 working days. |
| Storage | Store at 4 °C if the entire vial will be used within 2-4 weeks. Store at -20 °C for long term storage. For long term storage, it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | P13716 |
| Alias | ALADH,Porphobilinogen synthase,ALA dehydratase |
| Background | Protein ALAD |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
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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