Analytical Data
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Gene name
Phe
- Application
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Alternative Names
Phe；Phenylalanine-4-hydroxylase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P00439
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Expression Region
1-452aa
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AA Sequence
MSTAVLENPGLGRKLSDFGQETSYIEDNCNQNGAISLIFSLKEEVGALAKVLRLFEENDVNLTHIESRPSRLKKDEYEFFTHLDKRSLPALTNIIKILRHDIGATVHELSRDKKKDTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYCLSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRIEVLDNTQQLKILADSINSEIGILCSALQKIK
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Molecular Weight
51.8 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Phe recombinant proteins have gained significant attention in the field of biotechnology and biomedical research due to their potential applications in various therapeutic and diagnostic areas. Recombinant proteins, produced through genetic engineering techniques, allow for the expression of specific proteins in host organisms, such as bacteria, yeast, or mammalian cells, enabling the study of their structure and function. In particular, Phe, or phenylalanine, is an essential amino acid that plays a crucial role in protein synthesis and metabolic processes. Its derivatives and related proteins are studied for their involvement in several biological functions and diseases, including metabolic disorders like phenylketonuria (PKU). The manipulation of Phe-related genes and proteins has opened avenues for developing enzyme replacement therapies and other treatment modalities. Additionally, understanding the pathways involved in Phe metabolism is essential for designing effective dietary interventions for individuals with metabolic conditions. The advancement of recombinant DNA technology and protein expression systems has facilitated the efficient production of Phe-based proteins, allowing researchers to explore their therapeutic potential, characterize their mechanisms of action, and improve diagnostic assays for disease detection. Overall, the study of Phe recombinant proteins represents a promising frontier in the ongoing quest to understand complex biological systems and develop innovative solutions for health challenges.
