Analytical Data
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Gene name
HFE
- Application
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Alternative Names
HFE;HLAH;Hereditary hemochromatosis Protein
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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
Q30201
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Expression Region
23-306aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMRLLRSHSLHYLFMGASEQDLGLSLFE ALGYVDDQLFVFYDHESRRVEPRTPWVSSRISSQMWLQLSQSLKGWDHMF TVDFWTIMENHNHSKESHTLQVILGCEMQEDNSTEGYWKYGYDGQDHLEF CPDTLDWRAAEPRAWPTKLEWERHKIRARQNRAYLERDCPAQLQQLLELG RGVLDQQVPPLVKVTHHVTSSVTTLRCRALNYYPQNITMKWLKDKQPMDA KEFEPKDVLPNGDGTYQGWITLAVPPGEEQRYTCQVEHPGLDQPLIVIWE PSPSGTLV
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Molecular Weight
36 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
HFE (Human Hemochromatosis Protein) is a crucial regulatory protein involved in iron homeostasis in the human body. Mutations in the HFE gene can lead to hereditary hemochromatosis, a condition characterized by excessive iron accumulation, which can result in serious health issues such as liver cirrhosis, diabetes, and heart disease. Understanding the structure and function of HFE is essential for developing potential therapeutic strategies for iron overload disorders. The study of recombinant HFE proteins has emerged as a vital area of research, enabling scientists to explore the protein's interactions with various cellular components, including transferrin receptors and hepcidin, a key hormone regulating iron metabolism. Through techniques such as protein expression and purification, researchers can produce HFE in sufficient quantities for structural and functional analyses, paving the way for insights into its role in iron absorption and regulatory mechanisms. Additionally, elucidating the molecular basis of HFE-related diseases at the protein level can help identify biomarkers for early diagnosis and new therapeutic targets. As the understanding of HFE dynamics evolves, it holds promise for advancing clinical management of iron-related conditions and enhancing overall health outcomes in affected individuals.
