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Location： Home > Recombinant Rabbit Monoclonal Antibodies > Hemoglobin subunit alpha Rabbit mAb

Hemoglobin subunit alpha Rabbit mAb#49097

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Product Detail

Product NameHemoglobin subunit alpha Rabbit mAb

Clone No.SN70-09

Host SpeciesRecombinant Rabbit

ClonalityMonoclonal

PurificationProA affinity purified

ApplicationsWB, IHC, IP

Species ReactivityHu, Ms, Rt

Immunogen Descrecombinant protein

ConjugateUnconjugated

Other NamesAlpha 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 NoSwiss-Prot#:P69905

Uniprot P69905

Gene ID 3039;3040;

Calculated MW15 kDa

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

StorageStore at -20˚C

Application Details

WB: 1:1,000
IHC: 1:10-1:50
 

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

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.

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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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