Human Hemoglobin zeta Antibody Summary
Accession # P02008
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of Human Hemoglobin zeta by Western Blot. Western blot shows lysates of TF-1 human erythroleukemic cell line and K562 human chronic myelogenous leukemia cell line. PVDF membrane was probed with 0.2 µg/mL of Mouse Anti-Human Hemoglobin zeta Monoclonal Antibody (Catalog # MAB7708) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for Hemoglobin zeta at approximately 13 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Hemoglobin zeta in K562 Human Cell Line. Hemoglobin zeta was detected in immersion fixed K562 human chronic myelogenous leukemia cell line using Mouse Anti-Human Hemoglobin zeta Monoclonal Antibody (Catalog # MAB7708) at 10 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Mouse IgG Secondary Antibody (red; Catalog # NL007) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm. View our protocol for Fluorescent ICC Staining of Non-adherent Cells.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Hemoglobin zeta
Hemoglobin is a tetrameric heme-containing protein that is responsible for the transport of oxygen by red blood cells in the circulation. For most of fetal development and adulthood, hemoglobin consists of two alpha chains and two beta chains. Hemoglobin zeta (HBZ) is an approximately 15 kDa alpha chain-like protein that is produced during the first few weeks of embryogenesis until the onset of alpha chain expression. Its expression is prolonged in a0-thalassemia which is characterized by deficient alpha chain production. The Gower-1, Portland-1, and Portland-2 forms of hemoglobin consist of two zeta chains in association with either two epsilon, gamma, or beta chains, respectively. Human Hemoglobin zeta shares 79% amino acid sequence identity with mouse and rat Hemoglobin zeta.
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