Analytical Data
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Gene name
HEBP2
- Application
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Alternative Names
HEBP2；C6orf34；SOUL；Heme-binding Protein 2
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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
Q9Y5Z4
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Expression Region
2-205aa
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AA Sequence
AEPLQPDPGAAEDAAAQAVETPGWKAPEDAGPQPGSYEIRHYGPAKWVSTSVESMDWDSAIQTGFTKLNSYIQGKNEKEMKIKMTAPVTSYVEPGSGPFSESTITISLYIPSEQQFDPPRPLESDVFIEDRAEMTVFVRSFDGFSSAQKNQEQLLTLASILREDGKVFDEKVYYTAGYNSPVKLLNRNNEVWLIQKNEPTKENE
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Molecular Weight
38.7 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
HEBP2, or Hemoglobin Expression Regulator Protein 2, is a crucial player in the regulation of hemoglobin synthesis and erythropoiesis. It has garnered significant interest in research due to its role in cellular iron metabolism and the regulation of heme synthesis, which is vital for maintaining proper cellular function and overall blood health. Dysregulation of HEBP2 has been implicated in various hematological disorders, including anemia and thalassemia, highlighting its potential as a therapeutic target. The recombinant production of HEBP2 protein allows for in-depth studies of its structure, function, and interactions with other cellular components. These studies can provide insights into the molecular mechanisms underlying hemoglobin production and offer potential avenues for therapeutic intervention. Furthermore, understanding the role of HEBP2 in the context of genetic variations that affect hemoglobin levels may pave the way for novel strategies in treating blood-related diseases. Researchers are focusing on the optimization of expression systems to facilitate the large-scale production of functional HEBP2, enabling detailed biochemical and biophysical characterization. This can lead to the identification of small molecules or biological agents that could modulate HEBP2 activity, thus providing innovative solutions for managing disorders associated with dysfunctional hemoglobin production. Overall, the investigation of HEBP2 recombinant protein is crucial for unlocking new frontiers in hematology and improving the therapeutic landscape for blood disorders.
