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Hemoglobin subunit alpha Antibody

49097
Review: comment rank 5 pdf
  Catalog No. Package Size Price
49097-1 50ul $260.00
49097-2 100ul $390.00

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Description
  • Product Name Hemoglobin subunit alpha Antibody
  • Clone No. SN70-09
  • Purification ProA affinity purified
  • Applications WB, IHC, IP
  • Species Reactivity Hu, Ms, Rt
  • Immunogen Description recombinant protein
  • Alternative Names Alpha 1 globin antibody
    Alpha globin antibody
    Alpha one globin antibody
    Alpha-globin antibody
    HBA_HUMAN antibody
    HBA1 antibody
    HBA2 antibody
    Hemoglobin alpha 1 antibody
    Hemoglobin alpha 1 chain antibody
    Hemoglobin alpha 1 globin chain antibody
    Hemoglobin alpha 2 antibody
    Hemoglobin alpha chain antibody
    Hemoglobin subunit alpha antibody
    MGC126895 antibody
    MGC126897 antibody
  • Accession No. Swiss-Prot#:P69905
  • Calculated MW 15 kDa
  • Formulation 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.
  • Storage Store at -20˚C
Application Details

WB: 1:1,000
IHC: 1:10-1:50
 

Images
  • Hemoglobin subunit alpha Antibody - SAB | Signalway Antibody

    Immunohistochemical analysis of paraffin-embedded human lung tissue using anti-Hemoglobin subunit alpha antibody. Counter stained with hematoxylin.

  • Hemoglobin subunit alpha Antibody - SAB | Signalway Antibody

    Immunohistochemical analysis of paraffin-embedded human spleen tissue using anti-Hemoglobin subunit alpha antibody. Counter stained with hematoxylin.

  • Hemoglobin subunit alpha Antibody - SAB | Signalway Antibody

    Immunohistochemical analysis of paraffin-embedded mouse embryo tissue using anti-Hemoglobin subunit alpha antibody. Counter stained with hematoxylin.

Background

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.

Regerences

1. Banerjee S et al. Haptoglobin alters oxygenation and oxidation of hemoglobin and decreases propagation of peroxide-induced oxidative reactions. Free Radic Biol Med 53:1317-26 (2012).
2. Shephard F et al. A mitochondrial location for haemoglobins--dynamic distribution in ageing and Parkinson's disease. Mitochondrion 14:64-72 (2014).

    Please let us know if you have published research using #49097 so that we can cite your reference.
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    Protocol
    Browsing historyclear
    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 
    • Dm Drosophila melanogaster
    • C Caenorhabditis elegans
    • MkMonkey
    • RbRabbit
    • B Bovine 
    • D Dog
    • PPig
    • HmHamster
    • ChHm Chinese Hamster 
    • ChkChicken  
    • ShpSheep  
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