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Location： Home > Recombinant Rabbit Monoclonal Antibodies > Hemoglobin subunit gamma 1and2 Rabbit mAb

Hemoglobin subunit gamma 1and2 Rabbit mAb#49459

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Product Detail

Product NameHemoglobin subunit gamma 1and2 Rabbit mAb

Clone No.JM84-10

Host SpeciesRecombinant Rabbit

Clonality Monoclonal

PurificationProA affinity purified

ApplicationsWB, ICC/IF, IHC

Species ReactivityHu

Immunogen Descrecombinant protein

ConjugateUnconjugated

Accession NoSwiss-Prot#:P69891

Uniprot P69891

Gene ID 3047;

Calculated MW16 kDa

Formulation1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.

StorageStore at -20˚C

Application Details
WB: 1:1,000-5,000
IHC: 1:50-1:200
ICC: 1:50-1:200

FC:150-1100
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.

Immunohistochemical analysis of paraffin-embedded human tonsil tissue using anti-HBG1/2 antibody. Counter stained with hematoxylin.
Immunohistochemical analysis of paraffin-embedded human spleen tissue using anti-HBG1/2 antibody. Counter stained with hematoxylin.
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.
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.
ICC staining HBG1/2 in PC-12 cells (red). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.
Hemoglobin (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.

If you have published an article using product 49459, please notify us so that we can cite your literature.

NOTE

Application

  • WBWestern Blotting
  • IHCImmunohistochemistry
  • IFImmunofluorescence
  • ICCImmunocytochemistry
  • FCFlow Cytometry
  • IPImmunoprecipitation
  • EELISA
  • DBDot Blotting
  • ChIPChromatin Immunoprecipitation
  • GICAGold Immunochromatography Assay
  • NCNegative Control

Species Reactivity

  • HuHuman
  • MsMouse
  • RtRat
  • DmDrosophila melanogaster
  • CCaenorhabditis elegans
  • MkMonkey
  • RbRabbit
  • BBovine
  • DDog
  • PPig
  • HmHamster
  • ChHmChinese Hamster
  • ChkChicken
  • ShpSheep
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