Hemoglobin β Antibody (37-8): sc-21757

Hemoglobin β Antibody (37-8) is a mouse monoclonal IgG1 kappa light chain antibody specifically raised against human Hemoglobin beta. Hemoglobin β monoclonal antibody (37-8) detects Hemoglobin beta, also known as Hemoglobin subunit beta, β-globin, or CD113t-C, in human samples using techniques such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), immunohistochemistry with paraffin-embedded sections (IHCP), and flow cytometry (FCM). Hemoglobin beta is a vital component of hemoglobin, the oxygen-carrying protein in red blood cells that transports oxygen from the lungs to tissues and facilitates the return of carbon dioxide to the lungs. The hemoglobin molecule consists of two alpha (α) chains and two beta (β) chains arranged in pairs to form a tetramer, each associated with a heme group containing an iron ion that binds oxygen. The interactions between the α and β chains are crucial for the structural integrity and oxygen-binding properties of hemoglobin. Mutations in the Hemoglobin beta gene can lead to hemoglobinopathies such as sickle cell anemia and beta-thalassemia, highlighting the importance of studying this protein in medical research and diagnostics. Hemoglobin β (37-8) antibody is available in both unconjugated and conjugated forms, including agarose, horseradish peroxidase (HRP), phycoerythrin (PE), fluorescein isothiocyanate (FITC), and multiple Alexa Fluor® conjugates, providing versatility for various experimental applications.

Alexa Fluor^® is a trademark of Molecular Probes Inc., OR., USA

LI-COR^® and Odyssey^® are registered trademarks of LI-COR Biosciences

Hemoglobin β Antibody (37-8) References:

1. Assembly of human hemoglobin (Hb) beta- and gamma-globin chains expressed in a cell-free system with alpha-globin chains to form Hb A and Hb F.  |  Adachi, K., et al. 2002. J Biol Chem. 277: 13415-20. PMID: 11827978
2. Linkage of interactions in sickle hemoglobin fiber assembly: inhibitory effect emanating from mutations in the AB region of the alpha-chain is annulled by a mutation at its EF corner.  |  Sudha, R., et al. 2004. J Biol Chem. 279: 20018-27. PMID: 14982923
3. Transfer of human alpha- to beta-hemoglobin via its chaperone protein: evidence for a new state.  |  Baudin-Creuza, V., et al. 2004. J Biol Chem. 279: 36530-3. PMID: 15220346
4. Molecular mechanism of AHSP-mediated stabilization of alpha-hemoglobin.  |  Feng, L., et al. 2004. Cell. 119: 629-40. PMID: 15550245
5. Fetal hemoglobin regulation in β-thalassemia: heterogeneity, modifiers and therapeutic approaches.  |  Sripichai, O. and Fucharoen, S. 2016. Expert Rev Hematol. 9: 1129-1137. PMID: 27801605
6. Quadrupole-Time-of-Flight Mass Spectrometric Identification of Hemoglobin Subunits α, β, γ and δ in Unknown Peaks of High Performance Liquid Chromatography of Hemoglobin in β-Thalassemias.  |  Abdullah, UYH., et al. 2019. Hemoglobin. 43: 182-187. PMID: 31298599
7. Allosteric energy at the hemoglobin beta chain C terminus studied by hydrogen exchange.  |  Louie, G., et al. 1988. J Mol Biol. 201: 755-64. PMID: 3172203
8. Hemoglobin subunit beta protein as a novel marker for time since deposition of bloodstains at crime scenes.  |  Heo, TM., et al. 2022. Forensic Sci Int. 336: 111348. PMID: 35635979
9. Molecular basis of length polymorphism in the human zeta-globin gene complex.  |  Goodbourn, SE., et al. 1983. Proc Natl Acad Sci U S A. 80: 5022-6. PMID: 6308667
10. Homology and concerted evolution at the alpha 1 and alpha 2 loci of human alpha-globin.  |  Liebhaber, SA., et al. 1981. Nature. 290: 26-9. PMID: 7010180
11. 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
12. The multiple functions of hemoglobin.  |  Giardina, B., et al. 1995. Crit Rev Biochem Mol Biol. 30: 165-96. PMID: 7555018

Monoclonal antibodies for mammalian and non-mammalian protein targets represent essentially all targets covered by polyclonal antibodies. Over 8,300 of our antibodies are offered as ImmunoCruz^® conjugates which eliminates the need for a secondary antibody.

Santa Cruz Biotechnology antibodies have over 360,000 research citations. Anti-Hemoglobin β Antibody (37-8) has 78 citations in a variety of scientific publications.

Primary antibodies like Anti-Hemoglobin β Antibody (37-8) for mammalian target proteins are recommended for the detection of a range of mammalian species, primarily of mouse, rat and human species. Many mammalian antibodies are also ideal for veterinary research and reactive with ovine, porcine, caprine, feline, canine, bovine and equine protein targets. Santa Cruz Biotechnology primary monoclonal antibodies are suitable for laboratory research applications and are not intended for diagnostic or therapeutic use.

Hemoglobin β Antibody (37-8) Specifications

Alternate Product Name: Hemoglobin beta (HBB)

Product Clone Name: 37-8

Classification: Primary Antibody

Clonality: Monoclonal Antibody

Antibody Isotype: IgG₁ kappa light chain

Amino Acids:

Epitope Target: Hemoglobin β

Epitope Species: human

Product Reactivity/Detection: Hemoglobin β

Species Reactivity/Detection: human

Additional Mammalian Reactivity: N/A

Additional Non-Mammalian Reactivity: N/A

Applications: WB, IP, IF, IHC(P), FCM

Vialing Information: Each vial contains 200 µg IgG₁ kappa light chain in 1.0 ml of PBS with < 0.1% sodium azide and 0.1% gelatin

Research Citations: 78 citations in various scientific publications

Available Conjugates/Forms for Hemoglobin β Antibody (37-8): AC: Agarose, AF488: Alexa Fluor^® 488, AF546: Alexa Fluor^® 546, AF594: Alexa Fluor^® 594, AF647: Alexa Fluor^® 647, AF680: Alexa Fluor^® 680, AF790: Alexa Fluor^® 790, FITC: Fluoroscein, HRP: Horseradish Peroxidase, PE: Phycoerythrin, PerCP: Peridinin Chlorophyll Protein Complex