Human Phenylalanine Hydroxylase (PAH) Protein
247€ (10 µg)
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935106861
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name
Human Phenylalanine Hydroxylase (PAH) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx068508
tested applications
WB, SDS-PAGE
Description
Human Phenylalanine Hydroxylase (PAH) is a recombinant Human protein produced in a Prokaryotic expression system (E. coli).
Documents del producto
Instrucciones
Data sheet
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Phenylalanine Hydroxylase (PAH) |
| Host | E. coli |
| Origin | Human |
| Conjugation | Unconjugated |
| Observed MW | Molecular Weight: Calculated MW: 27.6 kDa Observed MW (SDS-PAGE): 28 kDa Concentration: Prior to lyophilization: 200 µg/ml Sequence Fragment: Met1-Gln226 Tag: N-terminal His tag |
| Expression | Recombinant |
| Purity | > 97% |
| 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 20 mM Tris, 150 mM NaCl, pH 8.0. If a higher concentration is required, the product can be reconstituted directly in 20 mM Tris, 150 mM NaCl, pH 8.0, 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: 20 mM Tris, 150 mM NaCl, pH 8.0, containing 1 mM EDTA, 1 mM DTT, 0.01% Sarcosyl, 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 |
| UniProt ID | P00439 |
| Gene ID | 5053 |
| OMIM | 261600 |
| Background | Protein PAH |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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