Analytical Data
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Gene name
HPD
- Application
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Alternative Names
HPD;PPD;4-hydroxyphenylpyruvate dioxygenase
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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
P32754
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Expression Region
1-393aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMTTYSDKGAKPERGRFLHFHSVTFWVGNAK QAASFYCSKMGFEPLAYRGLETGSREVVSHVIKQGKIVFVLSSALNPWNK EMGDHLVKHGDGVKDIAFEVEDCDYIVQKARERGAKIMREPWVEQDKFGK VKFAVLQTYGDTTHTLVEKMNYIGQFLPGYEAPAFMDPLLPKLPKCSLEM IDHIVGNQPDQEMVSASEWYLKNLQFHRFWSVDDTQVHTEYSSLRSIVVA NYEESIKMPINEPAPGKKKSQIQEYVDYNGGAGVQHIALKTEDIITAIRH LRERGLEFLSVPSTYYKQLREKLKTAKIKVKENIDALEELKILVDYDEKG YLLQIFTKPVQDRPTLFLEVIQRHNHQGFGAGNFNSLFKAFEEEQNLRGN LTNMETNGVVPGM
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Molecular Weight
47 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
HPD (4-hydroxyphenylpyruvate dioxygenase) is an enzyme crucial in the catabolic pathway of the amino acid tyrosine, playing a significant role in the biosynthesis of important metabolites such as melanin and neurotransmitters. The study of HPD recombinant proteins has gained traction due to its potential implications in various biological processes and diseases, including metabolic disorders and certain neurodegenerative diseases. The importance of HPD is underscored by the fact that mutations in the HPD gene are associated with hereditary tyrosinemia type III, a rare genetic disorder that can lead to serious health complications. By producing recombinant HPD proteins, researchers aim to investigate the enzyme's structure-function relationships, understand the molecular mechanisms underlying tyrosine catabolism, and explore potential therapeutic interventions. Furthermore, the recombinant forms of HPD can be used as valuable tools for drug discovery and the development of targeted therapies, paving the way for novel approaches to tackle disorders linked to tyrosine metabolism. Overall, the research on HPD recombinant proteins not only enhances the understanding of fundamental biochemical pathways but also holds promise for advancing medical science in treating related diseases.
