protein

AHSP Protein, Human

HY-P76136

5 μg;10 μg;50 μg;100 μg

50;85;230;390 USD

AHSP Protein, Human

proteins

E. coli

5 μg;10 μg;50 μg;100 μg

50;85;230;390 USD

AHSP proteins are chaperones in developing red blood cells that protect alpha-hemoglobin from harmful aggregation and precipitation. It is essential for alpha-hemoglobin stability, and it regulates conditions associated with excess alpha-hemoglobin, such as beta-thalassemia. AHSP Protein, Human is the recombinant human-derived AHSP protein, expressed by E. coli , with tag free. The total length of AHSP Protein, Human is 102 a.a., with molecular weight of ~12 KDa.

Human

AHSP protein serves as a chaperone during normal erythroid cell development, safeguarding alpha-hemoglobin from harmful aggregation by preventing its precipitation. This protective function is crucial for maintaining the stability of free alpha-hemoglobin and is particularly relevant in modulating pathological conditions associated with an excess of alpha-hemoglobin, such as beta-thalassemia. AHSP exists as a monomer and forms a specific heterodimeric complex with free alpha-hemoglobin, exhibiting selectivity as it does not bind to beta-hemoglobin or the alpha(2)beta(2) hemoglobin A complex. This interaction underscores AHSP's role in preventing detrimental interactions and maintaining the proper balance of hemoglobin components during erythropoiesis.

Alpha-hemoglobin-stabilizing protein; Erythroid-associated factor; AHSP; EDRF; ERAF

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

Room temperature in continental US; may vary elsewhere.