Human Aminolevulinate Delta Dehydratase (ALAD) Protein
221€ (10 µg)
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935106861
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name
Human Aminolevulinate Delta Dehydratase (ALAD) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx166533
tested applications
WB, SDS-PAGE
Description
Aminolevulinate Delta Dehydratase Protein is a recombinant Human protein expressed in E. coli.
Documents del producto
Instrucciones
Data sheet
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Aminolevulinate Delta Dehydratase (ALAD) |
| Host | E. coli |
| Origin | Human |
| Conjugation | Unconjugated |
| Observed MW | Molecular Weight: Calculated MW: 40.0 kDa Concentration: Prior to lyophilization: 200 µg/ml Sequence Fragment: Met1-Glu330 Tag: N-terminal His tag |
| Expression | Recombinant |
| Purity | > 95% |
| Size 1 | 10 µg |
| Size 2 | 50 µg |
| Size 3 | 100 µg |
| Size 4 | 200 µg |
| Size 5 | 500 µg |
| Form | Lyophilized To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex. |
| Tested Applications | WB, SDS-PAGE |
| Buffer | Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300. |
| Availability | Shipped within 5-7 working days. |
| Storage | Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| 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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