Analytical Data
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Gene name
HEBP1
- Application
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Alternative Names
HEBP1;HBP;Heme-binding Protein 1
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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
Q9NRV9
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Expression Region
1-189aa
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AA Sequence
MLGMIKNSLFGSVETWPWQVLSKGDKEEVAYEERACEGGKFATVEVTDKPVDEALREAMPKVAKYAGGTNDKGIGMGMTVPISFAVFPNEDGSLQKKLKVWFRIPNQFQSDPPAPSDKSVKIEEREGITVYSMQFGGYAKEADYVAQATRLRAALEGTATYRGDIYFCTGYDPPMKPYGRRNEIWLLKT
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Molecular Weight
48.6 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
HEBP1 (Heme-binding protein 1) is a crucial protein involved in heme metabolism and cellular responses to oxidative stress. Its role has garnered increasing attention due to its association with various physiological and pathological processes, including erythropoiesis, apoptosis, and cancer progression. The recombinant expression of HEBP1 in different models allows researchers to explore its function at a molecular level and assess its potential as a therapeutic target. Studies have shown that HEBP1 interacts with key proteins involved in the regulation of heme synthesis and catabolism, suggesting its importance in maintaining heme homeostasis. Additionally, its ability to bind heme indicates a potential role in cellular signaling pathways related to oxidative stress and inflammation. Understanding the structure-function relationship of HEBP1 through recombinant protein studies will aid in elucidating its mechanisms of action and provide insights into its potential implications in human diseases. Overall, the research on HEBP1 recombinant protein not only enhances our comprehension of heme biology but also opens new avenues for therapeutic interventions in disorders linked to heme dysregulation.
