Analytical Data
-
Gene name
AHSP
- Application
-
Alternative Names
AHSP；EDRF；ERAF；Alpha-hemoglobin-stabilizing Protein
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9NZD4
-
Expression Region
1-102aa
-
AA Sequence
MALLKANKDL ISAGLKEFSV LLNQQVFNDP LVSEEDMVTV VEDWMNFYIN YYRQQVTGEP QERDKALQEL RQELNTLANP FLAKYRDFLK SHELPSHPPP SS
-
Molecular Weight
38.8kDa
-
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
AHSP (alpha-hemoglobin-stabilizing protein) is a crucial protein involved in the stabilization of unbound alpha-globin chains, which are often prone to misfolding and aggregation, particularly under oxidative stress conditions. Research on AHSP has gained prominence due to its significant role in erythropoiesis and its potential implications in various hemoglobinopathies, such as sickle cell disease and beta-thalassemia. These disorders are characterized by abnormal hemoglobin synthesis, leading to anemia and other severe complications. Understanding the structure and function of AHSP can provide insights into its mechanism of action in maintaining cellular homeostasis and preventing the toxic effects of free alpha-globin chains. Moreover, studies have highlighted the potential of AHSP as a therapeutic target, aiming to enhance erythrocyte production and alleviate symptoms in patients suffering from hemoglobin-related disorders. Recent advancements in recombinant protein technology have enabled the production of AHSP in a laboratory setting, paving the way for further investigation into its biological functions and therapeutic applications. Overall, AHSP represents an important molecular chaperone that could offer valuable avenues for innovative treatments in the realm of hematological diseases.
