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Recombinant Human Hemoglobin Subunit α/HBA1

Recombinant Human Hemoglobin Subunit α/HBA1 Recombinant Human Hemoglobin Subunit α/HBA1

Instruction Manual!

Product name: Recombinant Human Hemoglobin Subunit α/HBA1
Source:E.coli
Purity:Greater than 95% as determined by reducing SDS-PAGE.
Buffer Formulation:Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.0.
Applications:Applications:SDS-PAGE; WB; ELISA; IP.
Storage:Avoid repeated freeze/thaw cycles. Store at 2-8 oC for one month. Aliquot and store at -80 oC for 12 months.
UOM:100ug/50ug/200ug/1mg/1g
Source E.coli
Description 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.
Names Hemoglobin subunit alpha, Alpha-globin, Hemoglobin alpha chain, HBA1,HBH, HBA-T3
Accession # P69905
Formulation Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.0.
Shipping The product is shipped at ambient temperature.
Reconstitution Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100 μg/ml.
Dissolve the lyophilized protein in ddH2O.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage 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.
Purity Greater than 95% as determined by reducing SDS-PAGE.
Endotoxin Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.
Amino Acid Sequence
MNHKVHHHHHHMVLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSA QVKGHGKKVADALTNAVAHVDDMPNALSALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFT PAVHASLDKFLASVSTVLTSKYR
Background Hemoglobin subunit alpha 1 (HBA1), also known as α2β2, is a hetero-tetramer consisting of two α and two β 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 α and β 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 α chain, while macrophages present the β chain only.

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