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BRAND / VENDOR: Abcam

Abcam, ab214049, Anti-Hemoglobin subunit beta antibody [EPR20614]

CATALOG NUMBER: ab214049
Regular price$0.99
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Product Description

Size: 100µL / 1mL
Rabbit Recombinant Monoclonal HBB antibody. Suitable for IP, WB and reacts with Human, Mouse, Rat samples. Cited in 7 publications.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:EPR20614,
Isotype:IgG,
Carrier free:No,
Reacts with:Mouse, Rat, Human,
Applications:WB, IPSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.

Product details:
Patented technology
Our RabMAb
technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to
RabMAb® patents
What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:
- High batch-to-batch consistency and reproducibility
- Improved sensitivity and specificity
- Long-term security of supply
- Animal-free batch production
For more information, read more on
recombinant antibodies

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.2 - 7.4Preservative: 0.01% Sodium azideConstituents: PBS, 40% Glycerol (glycerin, glycerine), 0.05% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
The hemoglobin subunit beta also known as beta hemoglobin or hemoglobin beta subunit is a component of the larger hemoglobin molecule important for transporting oxygen in red blood cells. This protein has a molecular weight of approximately 16 kDa. Hemoglobin subunit beta joins with alpha hemoglobin subunit to form hemoglobin A the most common form in adult humans. Expression of this protein happens in the erythroid cells of the bone marrow where it plays an important role in the production of hemoglobin during red blood cell formation.
Biological function summary
The hemoglobin beta subunit is essential for binding and releasing oxygen to tissues throughout the body. As part of the hemoglobin complex it helps stabilize the oxygen binding affinity through cooperative interactions with the alpha subunits. When oxygen binds to the heme groups in these subunits a conformational change occurs enhancing the efficiency of oxygen transport. This dynamic action allows hemoglobin to carry oxygen from the lungs to tissues and return carbon dioxide for expulsion.
Pathways
Hemoglobin beta subunit significantly participates in the oxygen transport and carbon dioxide exchange pathways. It interacts closely with carbonic anhydrase in the process of carbon dioxide transport converting it to bicarbonate for efficient clearance from the body. In this capacity the protein stands as a central component of the erythrocyte function and blood gas transport system partnering physiologically with proteins such as cytochrome b5 reductase in electron transfer-related pathways.
Hemoglobin subunit beta is prominently associated with hemoglobinopathies like sickle cell disease and beta-thalassemia. Mutations in its gene can lead to abnormal hemoglobin function or structure causing red blood cell disorders that impact oxygen delivery. In sickle cell disease an amino acid substitution causes hemoglobin to polymerize under low oxygen resulting in sickle-shaped cells. In beta-thalassemia reduced or absent beta-globin chain production leads to anemia. These hemoglobin-related disorders are tightly connected to genetic mutations influencing other proteins such as alpha-globin complicating the clinical picture.


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Collaboration

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