Analytical Data
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Gene name
phhA
- Application
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Alternative Names
phhA；p-hydroxybenzoate-m-hydroxylase A
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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
P30967
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Expression Region
1-297aa
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AA Sequence
MNDRADFVVPDITTRKNVGLSHDANDFTLPQPLDRYSAEDHATWATLYQRQCKLLPGRACDEFMEGLERLEVDADRVPDFNKLNQKLMAATGWKIVAVPGLIPDDVFFEHLANRRFPVTWWLREPHQLDYLQEPDVFHDLFGHVPLLINPVFADYLEAYGKGGVKAKALGALPMLARLYWYTVEFGLINTPAGMRIYGAGILSSKSESIYCLDSASPNRVGFDLMRIMNTRYRIDTFQKTYFVIDSFKQLFDATAPDFAPLYLQLADAQPWGAGDVAPDDLVLNAGDRQGWADTEDV
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Molecular Weight
35.1 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
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Protein Description
The study of phhA recombinant protein focuses on the gene encoding phenylalanine hydroxylase, an enzyme crucial for the conversion of phenylalanine to tyrosine, an important amino acid for neurotransmitter synthesis. Abnormalities or deficiencies in this enzyme can lead to phenylketonuria (PKU), a metabolic disorder that can cause severe neurological damage if not managed properly. With the increasing prevalence of PKU and related metabolic disorders, understanding the structure, function, and mechanism of phhA becomes vital for developing effective diagnostic and therapeutic strategies. Research on phhA recombinant protein allows for the investigation of its enzymatic properties and potential applications in gene therapy, enzyme replacement strategies, and the design of inhibitors that could modulate its activity. Additionally, the recombinant form of the protein can be utilized in biochemical assays to elucidate its role in metabolic pathways and understand the consequences of its dysregulation in human health. By employing techniques such as molecular cloning, expression in suitable host systems, and characterization of the recombinant protein, researchers aim to garner insights into its biochemical function and its implications for treating metabolic diseases associated with phenylalanine metabolism. This area of research not only provides a deeper understanding of metabolic disorders like PKU but also sheds light on the potential for innovative therapeutic interventions that can improve patient outcomes in the future.
