Abcam, ab156712, Recombinant Human Hemoglobin subunit gamma-1 protein

Size: 50µg
Recombinant Human Hemoglobin subunit gamma-1 protein is a Human Full Length protein, in the 1 to 147 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE, Mass Spec.
Key facts
Purity:>85% SDS-PAGE,
Expression system:Escherichia coli,
Tags:His tag N-Terminus,
Applications:SDS-PAGE, Mass SpecSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:P69891,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 8Constituents: 10% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.32% Tris HCl

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Hemoglobin subunit gamma-1 also known as HBG1 or Gamma hemoglobin is a component in fetal hemoglobin. Its molecular weight is approximately 16 kDa. This protein is integral to the formation of fetal hemoglobin which consists of two alpha and two gamma chains designated as α2γ2. Expression of the gamma subunit predominates in the fetal liver spleen and bone marrow. As fetal hemoglobin it binds oxygen more efficiently than adult hemoglobin facilitating oxygen transfer from the mother to the fetus.
Biological function summary
Gamma hemoglobin forms part of the fetal hemoglobin complex. This complex is highly essential during fetal development as it helps in the transfer of oxygen through the placenta. The higher oxygen affinity of fetal hemoglobin compared to adult forms ensures adequate oxygen supply for fetal tissues. The gamma subunit is later replaced by beta or delta subunits as the individual matures transitioning to adult hemoglobin.
Pathways
Gamma hemoglobin plays an important role in the oxygen transport pathway. The transition from fetal gamma hemoglobin to adult beta hemoglobin involves a switch that is critical for proper physiological development. This switch is influenced by various signaling pathways including the erythropoietin pathway and others regulated by transcription factors such as BCL11A. Other hemoglobin proteins related in these pathways include alpha beta and delta chains which interact to form distinct hemoglobin variants.
Gamma hemoglobin is notably involved in beta-thalassemia and sickle cell disease. Gamma chain production can compensate for deficient beta chain production in beta-thalassemia ameliorating symptoms. In sickle cell disease persistent gamma globin expression often through mechanisms like BCL11A suppression can increase fetal hemoglobin levels diminishing the sickling effect. This highlights the therapeutic potential of manipulating gamma chain expression in managing these disorders.