anti-Hemoglobin, mAb (7E1F)

CHF 315.00
In stock
YIF-LF-MA0277100 µlCHF 315.00
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Product Details
Synonyms HBB
Product Type Monoclonal Antibody
Clone 7E1F
Isotype Mouse IgG1 κ
Immunogen/Antigen Human plasma.

Western Blot (1:1,000)

Crossreactivity Human
Purity Detail Ammonium sulfate precipitation.
Formulation Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol.
Isotype Negative Control

Mouse IgG1 Isotype Control

Other Product Data

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Our product description may differ slightly from the original manufacturers product datasheet.

Declaration Manufactured by AbFrontier
Shipping and Handling
Shipping BLUE ICE
Short Term Storage +4°C
Long Term Storage -20°C
Use/Stability Stable for at least 1 year after receipt when stored at -20°C.
MSDS Inquire
Product Specification Sheet
Datasheet Download PDF

Hemoglobin (haemoglobin, Hb) is the iron-containing oxygen-transport protein in the red blood cells of vertebrates. Its chief physiological function is to transport oxygen from the lungs or gills to the tissues where it releases the oxygen for the cellular respiration. Hb A (most of adult hemoglobin) is a tetrameric protein with a molecular weight of 64,500 Da, consisting of two identical α-chains of 141 amino acids each, and two identical β-chains of 146 amino acids each. Each subunit or chain of Hb A adopts a three dimensional structure, called the globin fold, similar to that of the related, monomeric protein myoglobin (Mb). This fold is an arrangement of the helices which forms a pocket that encloses and binds a heme prosthetic group which consists of an iron (Fe) ion held in a heterocyclic ring, known as a porphyrin. The binding of oxygen is a cooperative process. The binding affinity of hemoglobin for oxygen is increased by the oxygen saturation of the molecule. the oxygen binding curve of hemoglobin is sigmoidal, or S-shaped, as opposed to the normal hyperbolic curve associated with noncooperative binding. Hemoglobin's oxygen-binding capacity is decreased in the presence of carbon monoxide because both gases compete for the same binding sites on hemoglobin. Carbon dioxide occupies a different binding site on the hemoglobin. Some mutations in the globin chain are associated with the hemoglobinopathies, such as sickle-cell disease and thalassemia. Hemoglobin (Hb)-based O2 carriers (HBOCs) such as hemoglobin vesicle (HbV) have been investigated as a transfusion alternative and other clinical applications. Involved in oxygen transport from the lung to the various peripheral tissues. LVV-hemorphin-7 potentiates the activity of bradykinin, causing a decrease in blood pressure.

Product References

1) Sakai H et al. (2008) J Intern Med. 263(1):4-15. (General)
2) Lukin JA and Ho C, (2004) Chem Rev. 104(3):1219-1230. (General)

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