Recombinant Human Hemoglobin Subunit a/HBA1 (N-6His)
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Amount : | 50 µg |
Content : | Lyophilized from a 0.2 µm filtered solution of 20mM PB, 150mM NaCl, pH 7.0. |
Storage condition : | Lyophilized protein should be stored at -20°C, though stable at room temperature for 3 weeks. Reconstituted protein solution can be stored at 4-7°C for 2-7 days. Aliquots of reconstituted samples are stable at -20°C for 3 months. |
AA sequence : | MNHKVHHHHHHMVLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR |
Source: E.coli.
MW :16.7kD.
Recombinant Human Hemoglobin subunit alpha is produced by our E.coli expression system and the target gene encoding Met1-Arg142 is expressed with a 6His tag at the N-terminus. Hemoglobin subunit alpha 1 (HBA1), also known as a2 beta2, is a hetero-tetramer consisting of two a and two beta subunits held together by non-covalent interactions. Each subunit contains a heme group with an iron atom in the Fe2+ state. Cooperativity of Hemoglobin (Hb) in binding with O2 and allosteric regulatory binding properties with CO2, H+, Cl-, and 2,3-DPG (2,3-bisphosphoglycerate) are based on subunit interactions. HBA1 is the most common type of Hb in adult humans, which mediates the transport of oxygen and carbon dioxide in the blood. In recent years, Hb a and beta chains have been found co-expressed in alveolar cells, mesangial cells of the kidney, retinal ganglion cells, hepatocytes and neurons. Endothelial and peripheral catecholaminergic cells express exclusively the a chain, while macrophages present the beta chain only.
MW :16.7kD.
Recombinant Human Hemoglobin subunit alpha is produced by our E.coli expression system and the target gene encoding Met1-Arg142 is expressed with a 6His tag at the N-terminus. Hemoglobin subunit alpha 1 (HBA1), also known as a2 beta2, is a hetero-tetramer consisting of two a and two beta subunits held together by non-covalent interactions. Each subunit contains a heme group with an iron atom in the Fe2+ state. Cooperativity of Hemoglobin (Hb) in binding with O2 and allosteric regulatory binding properties with CO2, H+, Cl-, and 2,3-DPG (2,3-bisphosphoglycerate) are based on subunit interactions. HBA1 is the most common type of Hb in adult humans, which mediates the transport of oxygen and carbon dioxide in the blood. In recent years, Hb a and beta chains have been found co-expressed in alveolar cells, mesangial cells of the kidney, retinal ganglion cells, hepatocytes and neurons. Endothelial and peripheral catecholaminergic cells express exclusively the a chain, while macrophages present the beta chain only.
Endotoxin : Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
Post transnational modification: | The initiator Met is not cleaved in variant Thionville and is acetylated. |
Tissue Specificity: | Red blood cells. |
BioGrid: | 109290. 45 interactions. |
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