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.

Specificity:

HBG1 polyclonal antibody detects endogenous levels of HBG1 protein.

Alternative names:

HBG1,

Species reactivity:

Human

Host:

Rabbit

Ig type:

Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2

Immunogen:

recombinant protein

Purification & Purity:

ProA affinity purified

Molecular weight:

16 kDa

Applications:

WB ICC/IF IHC

Usage:

WB:1:1,000-1:5,000 ICC:1:50-1:200 IHC:1:50-1:200 FC:1：50-1：100

Storage:

Store at +4°C after thawing. Aliquot store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.

Precautions:

For research use only, not for use in diagnostic procedure.

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