Product Pathways - Metabolism
Hemoglobin γ (D4K7X) Rabbit mAb #39386
|39386S||100 µl ( 10 western blots )||￥3,250.00 现货查询||购买询价|
|39386||carrier free & custom formulation / quantity||email request|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, F=Flow Cytometry,
Specificity / Sensitivity
Hemoglobin γ (D4K7X) Rabbit mAb recognizes endogenous levels of the hemoglobin γ subunit. This antibody recognizes both HBG1 and HBG2 isoforms, but does not cross-react with the hemoglobin β subunit.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val21 of human hemoglobin γ (HBG1) protein.
Western blot analysis of extracts from various cell lines using Hemoglobin γ (D4K7X) Rabbit mAb (upper) and β-Actin (D6A8) Rabbit mAb #8457 (lower).
Western blot analysis of extracts from 293T cells, mock-transfected (-) or transfected with a construct expressing Myc-tagged full-length human hemoglobin γ (hHbγ, +) or hemoglobin β (hHbβ, +), using Hemoglobin γ (D4K7X) Rabbit mAb (upper), Myc-Tag (71D10) Rabbit mAb #2278 (middle), and β-Actin (D6A8) Rabbit mAb #8457 (lower).
Hemoglobin (Hb, Hgb) is a heme-containing transport protein found primarily in the red blood cells of humans and most other vertebrates. The primary function of hemoglobin is to transport oxygen from the external environment to the body tissues. Hemoglobin also facilitates metabolic waste removal by assisting in the transport of carbon dioxide from tissues back to the respiratory organs (1). Mature hemoglobin is a tetrameric protein complex, with each subunit containing an oxygen-binding heme group (2). Multiple isoforms of hemoglobin exist, which vary in relative abundance depending on developmental stage. Adult hemoglobin (HbA) is comprised of two α subunits and two β subunits and is the predominant hemoglobin found in red blood cells of children and adults. Fetal hemoglobin (HbF) contains two α subunits and two γ subunits and is the predominant isoform found during fetal and early postnatal development (2,3). Mutations that alter the structure or abundance of specific globin subunits can result in pathological conditions known as hemoglobinopathies (4). One such disorder is sickle cell disease, which is characterized by structural abnormalities that limit the oxygen carrying capacity of red blood cells. By contrast, thalassemia disorders are characterized by deficiencies in the abundance of specific hemoglobin subunits (4). Clinical treatments that are designed to alter the expression of specific hemoglobin subunits can be used to treat hemoglobinopathies (5).
- Hardison, R. (1998) J Exp Biol 201, 1099-117.
- Sankaran, V.G. et al. (2010) Br J Haematol 149, 181-94.
- Bank, A. (2006) Blood 107, 435-43.
- Thein, S.L. (2013) Cold Spring Harb Perspect Med 3, a011700.
- Fucharoen, S. et al. (1996) Blood 87, 887-92.
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