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Hemopexin Human

Hemopexin Human Recombinant

Hemopexin Human Recombinant produced in E. coli is. a single polypeptide chain containing 462 amino acids (24-462) and having a molecular mass of 51.7kDa.
Hemopexin is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20413
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

Hemopexin Human, Sf9

Hemopexin Human Recombinant, Sf9

Hemopexin produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 448 amino acids (24-462a.a.) and having a molecular mass of 50.4kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).
Hemopexin is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT20480
Source

Sf9, Baculovirus cells.

Appearance
Sterile filtered colorless solution.

Introduction

Definition and Classification

Hemopexin (HPX), also known as beta-1B-glycoprotein, is a glycoprotein encoded by the HPX gene in humans . It belongs to the hemopexin family of proteins and is the plasma protein with the highest binding affinity for heme .

Biological Properties

Key Biological Properties: Hemopexin is a 60-kDa plasma glycoprotein with a high binding affinity to heme in an equimolar ratio . It plays a major protective role against oxidative stress through its heme-scavenging activities .

Expression Patterns and Tissue Distribution: Hemopexin is primarily expressed in the liver but is also found in other tissues such as the nervous system, skeletal muscle, retina, and kidney . It is an acute-phase protein whose synthesis is induced after an inflammatory event .

Biological Functions

Primary Biological Functions: Hemopexin’s main function is to scavenge heme released or lost by the turnover of heme proteins such as hemoglobin, thus protecting the body from oxidative damage . It also plays a role in recycling the iron bound to heme molecules .

Role in Immune Responses and Pathogen Recognition: Hemopexin is pivotal in the immune defense against hemolytic stress. It serves as an effective antagonist against heme toxicity resulting from severe acute or chronic hemolysis .

Modes of Action

Mechanisms with Other Molecules and Cells: Hemopexin binds free heme and forms a complex that is transported to hepatocytes and macrophages via receptors such as CD91 . This binding prevents heme’s pro-oxidant and pro-inflammatory effects and promotes its detoxification .

Binding Partners and Downstream Signaling Cascades: Hemopexin interacts with CD91 to release its bound ligand for internalization . The heme-HPX complex is phagocytosed by macrophages and broken down inside the cells, leading to the formation of bilirubin, carbon monoxide, and iron .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: The expression of hemopexin is regulated at multiple levels, including developmental control, tissue-specific control, and modulation during the acute phase reaction . Post-translational modifications also play a role in regulating its activity .

Applications

Biomedical Research: Hemopexin is used in research to understand its role in hemolytic diseases and its potential as a biomarker for assessing disease progression and prognosis .

Diagnostic Tools and Therapeutic Strategies: Hemopexin-based therapies are being developed to mitigate toxic heme exposure in conditions such as sickle cell disease, transfusion-induced hemolysis, and sepsis . It is also being explored as a diagnostic tool for various hematological disorders .

Role in the Life Cycle

Role Throughout the Life Cycle: Hemopexin plays a crucial role in protecting the body from oxidative damage throughout the life cycle, from development to aging and disease . Its levels and activity can be indicative of various pathological conditions, making it a valuable marker in clinical settings .

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