Hemoglobin subunit gamma 1and2 Recombinant Rabbit monoclonal Antibody IgG
Fig1: Western blot analysis of HBG1/2 on human placenta (1) and human brain (2) tissue lysates using anti-HBG1/2 antibody at 1/500 dilution.
Fig2: ICC staining HBG1/2 in D3 cells (red). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.
Fig3: ICC staining HBG1/2 in MCF-7 cells (red). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.
Host Species; Species ReactivityRabbit; Human
Application SummaryWB, ICC/IF, IHC
Purification; FormulationProA affinity purified; 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.; Liquid form.
ALTnamesHemoglobin subunit gamma-1, Gamma-1-globin, Hb F Agamma, Hemoglobin gamma-1 chain, Hemoglobin gamma-A chain
BackgroundHemoglobin (Hgb) is coupled to four iron-binding, methene-linked tetrapyrrole rings (heme). The α (16p13.3; 5′-ζ-pseudoz-pseudo α2-pseudo α1-α2-α1-1-3′) and β (11p15.5) globin loci determine the basic hemoglobin structure. The globin portion of hemoglobin consists of two α chains and two β chains arranged in pairs forming a tetramer. Each of the four globin chains covalently associates with a heme group. The bonds between α and β chains are weaker than between similar globin chains, thereby forming a cleavage plane that is important for oxygen binding and release. High affinity for oxygen occurs upon relaxation of the α1-β2 cleavage plane. When the two α1-β2 interfaces are closely bound, hemoglobin has a low affinity for oxygen. Hb A, which contains two α chains plus two β chains, comprises 97% of total circulating hemoglobin. The remaining 3% of total circulating hemoglobin is comprised of Hb A-2, which consists of two α chains plus two δ chains, and fetal hemoglobin (Hb F), which consists of two α chains together with two γ chains.(ET1703-46)