Hemoglobin subunit alpha Rabbit Recombinant mAb Datasheet

生物描述

特异性	Hemoglobin subunit alpha Rabbit Recombinant mAb detects endogenous level of total Hemoglobin subunit alpha.
背景	Hemoglobin is the major oxygen carrying component in blood and is vital to the survival of most multicellular animals. In higher order vertebrates, this essential protein is a tetramer composed of two related though distinct globin chains: alpha-globin and beta-globin. It is crucial to erythrocyte formation that the two globin chains are produced at balanced levels. Any disruptions resulting in an excess of either chain has significant, deleterious effects on red cell survival. haem binding stabilizes the globin chains and promote proper folding of the polypeptide. haem is essential to the function of Hemoglobin. α-globin has a ten-fold greater ability to bind haem compared to β-globin and may actually facilitate haem integration into apo-β-globin (and γ-globin) chains. As free α-globin is an unstable, reactive molecule capable of destroying erythroid progenitor cells, this small pool of excess α-globin chains must be stabilized to limit its reactivity. This is achieved by the binding of an abundant erythroid-expressed protein known as α-hemoglobin stabilizing protein (AHSP). AHSP is able to interact with multiple forms of α-globin including apo-, ferrous and ferric states bound to a variety of ligands and reduces oxidant-induced precipitation of α-globin in solution. AHSP binds α-globin at the α1β1 dimer interface, opposite the haem binding pocket, with lower affinity than β-globin and is easily displaced by β-globin binding.

特异性

Hemoglobin subunit alpha Rabbit Recombinant mAb detects endogenous level of total Hemoglobin subunit alpha.

背景

Hemoglobin is the major oxygen carrying component in blood and is vital to the survival of most multicellular animals. In higher order vertebrates, this essential protein is a tetramer composed of two related though distinct globin chains: alpha-globin and beta-globin. It is crucial to erythrocyte formation that the two globin chains are produced at balanced levels. Any disruptions resulting in an excess of either chain has significant, deleterious effects on red cell survival. haem binding stabilizes the globin chains and promote proper folding of the polypeptide. haem is essential to the function of Hemoglobin. α-globin has a ten-fold greater ability to bind haem compared to β-globin and may actually facilitate haem integration into apo-β-globin (and γ-globin) chains. As free α-globin is an unstable, reactive molecule capable of destroying erythroid progenitor cells, this small pool of excess α-globin chains must be stabilized to limit its reactivity. This is achieved by the binding of an abundant erythroid-expressed protein known as α-hemoglobin stabilizing protein (AHSP). AHSP is able to interact with multiple forms of α-globin including apo-, ferrous and ferric states bound to a variety of ligands and reduces oxidant-induced precipitation of α-globin in solution. AHSP binds α-globin at the α1β1 dimer interface, opposite the haem binding pocket, with lower affinity than β-globin and is easily displaced by β-globin binding.

使用信息

抗体应用

WB ,ELISA,ELISA

稀释比例

WB

1:1000

反应性

Human Mouse Rat

MW (kDa)

15kDa

抗体类型

Rabbit

储存液配方

10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide.

储存条件
(自收到货起)

Store at –20°C.

文献参考

[1] Voon HP, et al. Haematologica. 2008, 93(12):1868-76.

Application Data

WB

Validated by Selleck