Analytical Data
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Gene name
Hemoglobin subunit alpha/HBA1
- Application
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Alternative Names
Alpha-globin
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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
P69905
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Expression Region
Met1~Arg142
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Molecular Weight
19kDa
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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
Hemoglobin subunit alpha, commonly referred to as HBA1, is a crucial component of hemoglobin, the protein responsible for oxygen transport in red blood cells. Research on HBA1 is vital due to its significant role in various blood disorders, including alpha-thalassemia and sickle cell disease, which impact millions globally. Mutations in the HBA1 gene can lead to insufficient production of alpha globin chains, resulting in imbalanced hemoglobin levels and compromised oxygen delivery to tissues. The study of recombinant HBA1 protein has gained traction as it enables researchers to investigate the functional implications of specific mutations, elucidate the molecular mechanisms underlying hemoglobinopathies, and explore new therapeutic strategies. Moreover, recombinant HBA1 is instrumental in developing biosensors and diagnostic tools for detecting hemoglobin levels and identifying related disorders. The production of HBA1 in various expression systems, such as bacteria and mammalian cells, allows for the generation of large quantities of the protein, facilitating detailed biochemical and biophysical analyses. Understanding HBA1's structure and function not only enhances our grasp of oxygen transport physiology but also paves the way for innovative treatments aimed at correcting hemoglobin deficiencies and improving patient outcomes in hemoglobin-related diseases. Overall, research on recombinant HBA1 remains a dynamic and essential field within biomedical science, promising advancements in both basic research and clinical applications.
