Analytical Data
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Gene name
HBG1
- Application
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Alternative Names
HBG1;Hemoglobin subunit gamma-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
P69891
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Expression Region
2-147aa
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AA Sequence
GHFTEEDKATITSLWGKVNVEDAGGETLGRLLVVYPWTQRFFDSFGNLSSASAIMGNPKVKAHGKKVLTSLGDAIKHLDDLKGTFAQLSELHCDKLHVDPENFKLLGNVLVTVLAIHFGKEFTPEVQASWQKMVTAVASALSSRYH
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Molecular Weight
23.0 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
HBG1, or hemoglobin gamma 1 gene, is part of the globin gene family and plays a crucial role in fetal hemoglobin production. The study of HBG1 recombinant protein has gained significant attention due to its potential implications in treating hemoglobinopathies, particularly sickle cell disease and beta-thalassemia. These conditions result from mutations in the beta-globin gene, leading to ineffective erythropoiesis and severe anemia. By understanding the mechanisms of HBG1, researchers aim to induce fetal hemoglobin production in patients, which can compensate for the defective adult hemoglobin. Advances in molecular biology techniques, such as CRISPR/Cas9 gene editing and lentiviral vector systems, have facilitated the exploration of HBG1 expression and its regulation. Furthermore, the recombinant HBG1 protein enables researchers to investigate its structure, function, and interaction with other hemoglobin subunits. The identification of small molecules or genetic modifiers that can enhance HBG1 expression represents a promising therapeutic avenue. Overall, the research into HBG1 recombinant protein not only contributes to fundamental knowledge of hemoglobin biology but also holds the promise for innovative treatments for patients suffering from debilitating hemoglobin disorders.
