Analytical Data
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Gene name
Hemoglobin subunit theta-1/HBQ1
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简介
Hemoglobin subunit theta-1 (HBQ1) is a protein belonging to the globin family. Globulin is a group of proteins involved in oxygen transport and storage. Hemoglobin subunit theta-1/HBQ1 Protein, Human (His) is the recombinant human-derived Hemoglobin subunit theta-1/HBQ1 protein, expressed by E. coli , with N-6*His labeled tag.
- Application
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Alternative Names
rHuHemoglobin subunit theta-1, His; Hemoglobin subunit theta-1; Hemoglobin theta-1 chain; Theta-1-globin; HBQ1
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Species
Human
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Source
E. coli
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P09105
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Expression Region
M1-R142
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Protein Length
Full Length
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Molecular Weight
15 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
Hemoglobin subunit theta-1 (HBQ1), a member of the globin family, plays a crucial role in the transport and storage of oxygen in various organisms. Its distinct expression pattern and structural characteristics have garnered interest in both physiological and pathological studies. Notably, HBQ1 has been implicated in various biological processes, including oxygen sensing and cellular response to hypoxia. Research into recombinant HBQ1 protein has expanded our understanding of its function, potential applications in therapeutics, and integration in synthetic biology. The production of recombinant HBQ1 enables detailed functional assays, structural investigations, and exploration of its interactions with other biomolecules. Additionally, understanding HBQ1's role in diseases, such as anemia and other hemoglobinopathies, presents opportunities for novel diagnostic and therapeutic strategies. Given the increasing prevalence of such conditions globally, elucidating the functional mechanisms of HBQ1 through recombinant approaches is essential for advancing medical research and potential therapeutic interventions. These investigations not only highlight the significance of HBQ1 in fundamental biology but also pave the way for innovative applications in biotechnology and medicine.
