Analytical Data
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Gene name
HEPH
- Application
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Alternative Names
CPL
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9BQS7
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Expression Region
Ala24~Cys366
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Molecular Weight
42kDa
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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
HEPH (HEPH protein) is a member of the family of hephaestin-like proteins, which play crucial roles in iron homeostasis and cellular metabolism. Research into HEPH has gained momentum due to its involvement in iron transport and its implications in various diseases, including neurodegenerative disorders and anemia. Unlike its well-studied counterpart, ceruloplasmin, which is primarily synthesized in the liver, HEPH is predominantly expressed in the intestine and brain, suggesting its specialized function in local iron metabolism. Recent studies have indicated that HEPH is essential for the oxidation of ferrous iron (Fe2+), converting it to ferric iron (Fe3+) to facilitate its binding to transferrin, the major iron transport protein in blood. This biochemical process is vital for maintaining systemic iron levels and ensuring proper cellular function. Moreover, mounting evidence suggests that dysregulation of HEPH may contribute to the pathophysiology of conditions such as Alzheimer’s disease and iron overload syndromes. As such, understanding the structure and function of HEPH recombinant proteins has become a focal point for researchers aiming to elucidate the mechanisms governing iron metabolism and to develop potential therapeutic interventions for related disorders. Advances in biotechnology allow for the production of recombinant HEPH, enabling detailed studies of its enzymatic activity, interactions, and role in physiological processes. Consequently, this research not only enhances our understanding of iron biology but also opens new avenues for addressing iron-related health issues.
