Analytical Data
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Gene name
Hba
- Application
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Alternative Names
Hba；Hba-a1；Hemoglobin subunit alpha
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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
P01942
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Expression Region
2-142aa
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AA Sequence
VLSGEDKSNIKAAWGKIGGHGAEYGAEALERMFASFPTTKTYFPHFDVSHGSAQVKGHGKKVADALASAAGHLDDLPGALSALSDLHAHKLRVDPVNFKLLSHCLLVTLASHHPADFTPAVHASLDKFLASVSTVLTSKYR
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Molecular Weight
33.1 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
The study of Hba recombinant proteins is grounded in the critical role of hemoglobin in oxygen transport and overall cellular function. Hemoglobin, particularly the adult form known as HbA, consists of two alpha and two beta globin chains, and any mutations or anomalies can lead to hemoglobinopathies such as sickle cell disease and thalassemia. The recombinant production of hemoglobin subunits allows researchers to better understand its structure-function relationships and the mechanisms underlying various blood disorders. Additionally, the generation of Hba recombinant proteins provides valuable tools for developing innovative therapeutics and blood substitutes, improving transfusion medicine, and studying blood-related diseases. This research is further propelled by advances in genetic engineering and protein expression systems, enabling the production of high-yield, functional hemoglobin for both clinical applications and fundamental biological research. Overall, the exploration of Hba recombinant proteins stands at the intersection of molecular biology, medicine, and biotechnology, presenting opportunities to enhance health outcomes for patients with hemoglobin disorders.
