Recombinant Proteins
Product List
AHSP Human
Alpha Hemoglobin Stabilizing Protein Human Recombinant
The AHSP is purified by proprietary chromatographic techniques.
HBA2 Human
Hemoglobin, Alpha 2 Human Recombinant
HBA2 is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
HBG1 Human
Hemoglobin Gamma A Human Recombinant
HBG2 Human
Hemoglobin Gamma G Human Recombinant
Sterile filtered reddish solution.
HBQ1 Human
Hemoglobin Theta 1 Human Recombinant
HBZ Human
Hemoglobin-Zeta Human Recombinant
HBZ Mouse
Hemoglobin-Zeta Mouse Recombinant
HBZ Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 162 amino acids (1-142 a.a) and having a molecular mass of 18.3kDa.
HBZ is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Introduction
Hemoglobin (Hb) is a complex protein found in red blood cells (RBCs) that is responsible for transporting oxygen from the lungs to the tissues and facilitating the return of carbon dioxide from the tissues to the lungs. Hemoglobin is classified as a metalloprotein due to its iron-containing heme groups. It is composed of four polypeptide chains, typically two alpha (α) and two beta (β) chains in adults, forming a tetrameric structure.
Key Biological Properties: Hemoglobin exhibits cooperative binding with oxygen, meaning its affinity for oxygen increases as more oxygen molecules bind. This property is crucial for efficient oxygen transport and release.
Expression Patterns: Hemoglobin is predominantly expressed in erythroid cells during their differentiation in the bone marrow.
Tissue Distribution: Hemoglobin is primarily found in red blood cells, which circulate throughout the body, delivering oxygen to various tissues and organs.
Primary Biological Functions: The main function of hemoglobin is to transport oxygen from the lungs to the tissues and return carbon dioxide from the tissues to the lungs for exhalation. Hemoglobin also plays a role in maintaining the acid-base balance in the blood.
Role in Immune Responses and Pathogen Recognition: Hemoglobin can influence immune responses indirectly by modulating oxygen levels in tissues, which can affect the activity of immune cells. Additionally, hemoglobin-derived peptides, such as hemocidins, have antimicrobial properties and can contribute to pathogen recognition and defense.
Mechanisms with Other Molecules and Cells: Hemoglobin binds oxygen in the lungs, where the partial pressure of oxygen is high, and releases it in tissues, where the partial pressure is low. This binding and release are regulated by factors such as pH, carbon dioxide levels, and 2,3-bisphosphoglycerate (2,3-BPG).
Binding Partners: Hemoglobin interacts with various molecules, including oxygen, carbon dioxide, and nitric oxide. It also binds to 2,3-BPG, which stabilizes the deoxygenated form of hemoglobin and facilitates oxygen release.
Downstream Signaling Cascades: Hemoglobin can influence cellular signaling pathways through its interactions with nitric oxide, which plays a role in vasodilation and blood flow regulation.
Transcriptional Regulation: The expression of hemoglobin genes is tightly regulated during erythropoiesis. Transcription factors such as GATA-1 and KLF1 play crucial roles in the activation of hemoglobin gene expression.
Post-Translational Modifications: Hemoglobin undergoes various post-translational modifications, including glycosylation and oxidation. These modifications can affect its stability, function, and interactions with other molecules.
Biomedical Research: Hemoglobin is extensively studied in biomedical research to understand its structure, function, and role in diseases such as sickle cell anemia and thalassemia.
Diagnostic Tools: Hemoglobin levels and variants are commonly measured in clinical diagnostics to assess conditions such as anemia, polycythemia, and hemoglobinopathies.
Therapeutic Strategies: Hemoglobin-based oxygen carriers (HBOCs) are being developed as blood substitutes for use in situations where blood transfusions are not possible or desirable. Additionally, gene therapy approaches are being explored to treat hemoglobin-related disorders.
Development: Hemoglobin expression undergoes changes during development. Fetal hemoglobin (HbF) is the predominant form in the fetus, which has a higher affinity for oxygen than adult hemoglobin (HbA). After birth, HbF is gradually replaced by HbA.
Aging and Disease: Hemoglobin function can be affected by aging and various diseases. For example, oxidative stress and glycation can impair hemoglobin function in elderly individuals. Hemoglobinopathies, such as sickle cell disease and thalassemia, result from genetic mutations that affect hemoglobin structure and function, leading to severe clinical manifestations.
