Recombinant Proteins

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AHSP Human

Alpha Hemoglobin Stabilizing Protein Human Recombinant

AHSP Human Recombinant, produced in E. coli bacteria, is a single-chain protein that is not modified by the addition of sugar molecules. It consists of 102 amino acids (specifically, amino acids 1 through 102) and has a molecular weight of 11.8 kDa. The purification of AHSP is achieved through specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT19696
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

HbA1c Human

Human Hemoglobin A1c

This product consists of Human Hemoglobin A1c purified from Human Red Blood Cells.
Shipped with Ice Packs
Cat. No.
BT19764
Source
Human Erythrocytes.
Appearance
The product appears as a clear, red solution in its frozen state.

HBA2 Human

Hemoglobin, Alpha 2 Human Recombinant

Recombinantly produced in E. coli, HBA2 Human is a single polypeptide chain weighing 19.5 kDa. This protein consists of 179 amino acids, with positions 1-142 representing the HBA2 sequence. A 37 amino acid His-tag is fused at the N-terminus. Purification is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT19828
Source
E.coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

HBG1 Human

Hemoglobin Gamma A Human Recombinant

Recombinant human HBG1, expressed in E. coli, is a single polypeptide chain consisting of 170 amino acids (residues 1-147). It has a molecular weight of 18 kDa. The protein includes a 23-amino acid His-tag fused at the N-terminus to facilitate purification, which is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT19917
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

HBG2 Human

Hemoglobin Gamma G Human Recombinant

Recombinant human HBG2, produced in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 170 amino acids (with positions 1 to 147 representing the HBG2 sequence) and has a molecular weight of 18.5 kDa. The protein includes a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT19999
Source
Escherichia Coli.
Appearance
Sterile filtered solution, reddish in color.

HBQ1 Human

Hemoglobin Theta 1 Human Recombinant

Recombinant HBQ1 Human, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 165 amino acids (residues 1-142) and has a molecular weight of 17.9 kDa. The protein includes a 23 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20087
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

HBZ Human

Hemoglobin-Zeta Human Recombinant

Recombinant human HBZ, expressed in E. coli, is a non-glycosylated polypeptide chain with a single chain. It comprises 150 amino acids, including a C-terminal 8-amino acid His Tag, and has a molecular weight of 16.7 kDa. Purification is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT20205
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

HBZ Mouse

Hemoglobin-Zeta Mouse Recombinant

Recombinant HBZ Mouse protein was expressed in E. coli. It is a single, non-glycosylated polypeptide chain containing 162 amino acids (residues 1-142), with an additional 20 amino acid His-tag at the N-terminus, resulting in a molecular mass of 18.3 kDa. Purification was achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20305
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile filtered.
Definition and Classification

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.

Biological Properties

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.

Biological Functions

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.

Modes of Action

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.

Regulatory Mechanisms

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.

Applications

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.

Role in the Life Cycle

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.

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