Hemoglobin beta Antibody (21): sc-130321

Hemoglobin β Antibody (21) is a mouse monoclonal IgG1 kappa light chain antibody specifically raised against recombinant human Hemoglobin β. Hemoglobin β, also known as Hemoglobin subunit beta or β-globin, is a vital component of adult hemoglobin (HbA), which comprises two alpha (α) and two beta (β) globin chains forming a tetramer essential for oxygen transport in the bloodstream. Each β-globin chain binds a heme group containing an iron ion, enabling the efficient binding and release of oxygen molecules. Post-translational modifications (PTMs) of Hemoglobin β, such as glycation, the non-enzymatic attachment of glucose molecules, can significantly impact function. Elevated levels of glycated hemoglobin (HbA1c) are clinically significant in conditions like diabetes mellitus, where they serve as indicators of poor glucose control. These modifications can alter structure and function, affecting oxygen delivery and contributing to disease pathogenesis. Anti-Hemoglobin β antibody (21) has been validated for use in western blotting (WB), immunoprecipitation (IP), and enzyme-linked immunosorbent assay (ELISA), making this tool invaluable for studying Hemoglobin β expression and post-translational modifications. By detecting alterations in Hemoglobin β, researchers can gain insights into oxygen delivery mechanisms and the impact of metabolic disorders on hemoglobin functionality. Hemoglobin β monoclonal antibody (21) facilitates advanced research in hematology and related biomedical fields.

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Hemoglobin beta Antibody (21) References:

1. An additional H-bond in the alpha 1 beta 2 interface as the structural basis for the low oxygen affinity and high cooperativity of a novel recombinant hemoglobin (beta L105W).  |  Fang, TY., et al. 2000. Biochemistry. 39: 13708-18. PMID: 11076510
2. Thrombocytopenia and erythrocytosis in mice with a mutation in the gene encoding the hemoglobin β minor chain.  |  Kauppi, M., et al. 2012. Proc Natl Acad Sci U S A. 109: 576-81. PMID: 22203977
3. Dynamical footprint of falcipain-2 catalytic triad in hemoglobin-β-bound state.  |  Omotuyi, IO. and Hamada, T. 2015. J Biomol Struct Dyn. 33: 1027-36. PMID: 24943200
4. Salt, phosphate and the Bohr effect at the hemoglobin beta chain C terminus studied by hydrogen exchange.  |  Louie, G., et al. 1988. J Mol Biol. 201: 765-72. PMID: 3172204
5. Regulation of hemoglobin beta-chain synthesis in bone marrow erythroid cells by alpha chains.  |  Wolf, JL., et al. 1973. Proc Natl Acad Sci U S A. 70: 3405-9. PMID: 4519634
6. The solubility of hemoglobin beta 4 S, the mutant subunits of sickle cell hemoglobin.  |  Benesch, R., et al. 1973. Biochem Biophys Res Commun. 55: 261-5. PMID: 4767302
7. Folding domains as functional tools in allosteric systems: a heme-dependent domain in hemoglobin beta subunits.  |  Franchi, D., et al. 1982. Biochemistry. 21: 6181-7. PMID: 7150550
8. Evidence for a difference in affinities of human hemoglobin beta A and beta S chains for alpha chains.  |  Shaeffer, JR. 1980. J Biol Chem. 255: 2322-4. PMID: 7358673
9. Chloride ion independence of the Bohr effect in a mutant human hemoglobin beta (V1M+H2deleted).  |  Fronticelli, C., et al. 1994. J Biol Chem. 269: 23965-9. PMID: 7929044
10. The NH2-terminal region of the sickle hemoglobin beta chain. II. Characterization of monospecific antibodies.  |  Young, NS., et al. 1976. J Biol Chem. 251: 6431-8. PMID: 977582

The preferred Hemoglobin β antibody is Hemoglobin β Antibody (37-8): sc-21757.