Analytical Data
-
Gene name
HBA1
- Application
-
Alternative Names
HBA1；HBA2；Hemoglobin subunit alpha
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P69905
-
Expression Region
1-142aa
-
AA Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMVL SPADKTNVKA AWGKVGAHAG EYGAEALERM FLSFPTTKTY FPHFDLSHGS AQVKGHGKKV ADALTNAVAH VDDMPNALSA LSDLHAHKLR VDPVNFKLLS HCLLVTLAAH LPAEFTPAVH ASLDKFLASV STVLTSKYR
-
Molecular Weight
20 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
HBA1, the human alpha-globin gene, plays a critical role in the synthesis of hemoglobin, which is essential for oxygen transport in the blood. Abnormalities in HBA1 can lead to various disorders, including alpha-thalassemia and other hemoglobinopathies, which significantly impact human health. The study of HBA1 recombinant protein has gained traction due to its potential applications in therapeutic interventions and genetic studies. By producing and characterizing HBA1 as a recombinant protein, researchers can better understand the structure-function relationships essential for proper hemoglobin function. These studies provide insights into the molecular mechanisms underlying hemoglobinopathies, enabling the development of improved diagnostic tools and potential treatments, such as gene therapy. Additionally, recombinant HBA1 can serve as a valuable model for the investigation of protein folding, stability, and interaction with other hemoglobin subunits. The recombinant approach also facilitates large-scale protein production, which is important for further research and potential clinical applications. Overall, HBA1 recombinant protein research is crucial for advancing our understanding of hemoglobin disorders and developing innovative strategies for their management.
