Hemoglobin α Antibody (B-9): sc-514906

Hemoglobin α Antibody (B-9) is a mouse monoclonal IgG1 antibody that detects Hemoglobin α in human samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). Hemoglobin α plays a crucial role in oxygen transport within the bloodstream, as one of the two types of globin chains that form the tetrameric structure of hemoglobin, consisting of two α and two β chains. The proper functioning of Hemoglobin α is vital for maintaining adequate oxygen levels in tissues, as Hemoglobin α binds oxygen in the lungs and releases it in peripheral tissues, a process influenced by structural dynamics. The α chains are encoded by the HBA1 and HBA2 genes located on chromosome 16, and mutations in these genes can lead to various hemoglobinopathies, such as alpha-thalassemia, which can result in anemia and other health complications. Hemoglobin α′s interaction with heme groups is significant, as each α chain binds to a heme, allowing for reversible binding of oxygen. The structural integrity and functionality of Hemoglobin α are essential for effective respiratory gas exchange, making Hemoglobin α a critical component of the circulatory system. Anti-Hemoglobin α antibody (B-9) is an invaluable tool for researchers studying hemoglobin-related disorders and physiological mechanisms of oxygen transport.

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Hemoglobin α Antibody (B-9) References:

1. Substitution of the heme binding module in hemoglobin alpha- and beta-subunits. Implication for different regulation mechanisms of the heme proximal structure between hemoglobin and myoglobin.  |  Inaba, K., et al. 2000. J Biol Chem. 275: 12438-45. PMID: 10777528
2. Development of a high-resolution melting method for the detection of hemoglobin alpha variants.  |  Shih, HC., et al. 2010. Clin Biochem. 43: 671-6. PMID: 20144601
3. Hemoglobin α and β are ubiquitous in the human lung, decline in idiopathic pulmonary fibrosis but not in COPD.  |  Ishikawa, N., et al. 2010. Respir Res. 11: 123. PMID: 20836851
4. Implications of the colonic deposition of free hemoglobin-α chain: a previously unknown tissue by-product in inflammatory bowel disease.  |  Myers, JN., et al. 2014. Inflamm Bowel Dis. 20: 1530-47. PMID: 25078150
5. Expression of hemoglobin-α and β subunits in human vaginal epithelial cells and their functional significance.  |  Saha, D., et al. 2017. PLoS One. 12: e0171084. PMID: 28178273
6. Resolution of products of the duplicated hemoglobin alpha-chain loci by isoelectric focusing.  |  Whitney, JB., et al. 1979. Proc Natl Acad Sci U S A. 76: 867-71. PMID: 284410
7. Inflammatory Bowel Disease-Associated Colorectal Cancer: Translational and Transformational Risks Posed by Exogenous Free Hemoglobin Alpha Chain, A By-Product of Extravasated Erythrocyte Macrophage Erythrophagocytosis.  |  Bragg, MA., et al. 2023. Medicina (Kaunas). 59: PMID: 37476546
8. Turnover of excess hemoglobin alpha chains in beta-thalassemic cells is ATP-dependent.  |  Shaeffer, JR. 1983. J Biol Chem. 258: 13172-7. PMID: 6195159
9. Ubiquitin aldehyde increases adenosine triphosphate-dependent proteolysis of hemoglobin alpha-subunits in beta-thalassemic hemolysates.  |  Shaeffer, JR. and Cohen, RE. 1997. Blood. 90: 1300-8. PMID: 9242565
10. Hemoglobin A0 and alpha-crosslinked hemoglobin (alpha-DBBF) potentiate agonist-induced platelet aggregation through the platelet thromboxane receptor.  |  Mondoro, TH., et al. 1998. Artif Cells Blood Substit Immobil Biotechnol. 26: 1-16. PMID: 9507752

The preferred Hemoglobin α antibody is Hemoglobin α Antibody (D-4): sc-514378.