Product List

Endoglin (27-581) Mouse

Endoglin (27-581) Mouse Recombinant

Endoglin Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 563 amino acids (27-581 a.a.) and having a molecular mass of 60.9kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions).
Endoglin is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21639
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered colorless solution.

Endoglin Human

Endoglin Human Recombinant

Endoglin Human Recombinant extracellular domain produced in E.Coli is a single, glycosylated, Polypeptide containing 151 amino acids (26-176) and having a molecular mass of 43 kDa.
The Endoglin is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21737
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless liquid formulation.

Endoglin Human, His

Endoglin Human Recombinant, His-Tag

Endoglin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 594 amino acids (26-586) and having a molecular mass of 64.9 kDa. Endoglin is fused to a 36 amino acid His-tag at N-terminus.
Shipped with Ice Packs
Cat. No.
BT21843
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

Endoglin Human, Sf9

Endoglin Human Recombinant, Sf9

CD105 Human Recombinant extracellular domain produced in baculovirus is a homodimeric, glycosylated, Polypeptide containing 586 amino acids and having a molecular mass of 61 kDa but as a result of glycosylation, migrates at 90 kDa under reducing conditions in SDS-PAGE. The CD105 is fused to a C-terminal His-tag (6xHis) and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21925
Source
Sf9 Insect Cells.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Endoglin Mouse

Endoglin Mouse Recombinant

CD105 Mouse Recombinant extracellular domain produced in baculovirus is a homodimeric, glycosylated, Polypeptide containing 581 amino acids and having a molecular mass of 61 kDa but as a result of glycosylation, migrates at 75-85 kDa under reducing conditions in SDS-PAGE. Based on N-terminal sequence analysis, the primary structure of recombinant mature Endoglin starts at Glu 26. The CD105 is fused to a C-terminal His-tag (6xHis) and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21993
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Introduction

Definition and Classification

Endoglin (ENG), also known as CD105, is a type I membrane glycoprotein located on cell surfaces and is part of the TGF-beta receptor complex . It is classified as an accessory receptor for the transforming growth factor beta (TGF-β) family, playing a crucial role in angiogenesis .

Biological Properties

Key Biological Properties: Endoglin is a transmembrane glycoprotein with a large extracellular domain, a hydrophobic transmembrane domain, and a short cytoplasmic tail . It exists in two isoforms, L-endoglin and S-endoglin, created by alternative splicing .

Expression Patterns: Endoglin expression is usually low in resting endothelial cells but increases significantly during neoangiogenesis, inflammation, and tissue repair . It is highly expressed in vascular endothelial cells, activated macrophages, and fibroblasts .

Tissue Distribution: Endoglin is found in all tissues with endothelial cells, particularly in tumor vessels, inflamed tissues, and during embryogenesis . It is also present in monocytes, vascular smooth muscle cells, and tissues undergoing fibrosis .

Biological Functions

Primary Biological Functions: Endoglin is essential for angiogenesis, the process of new blood vessel formation . It acts as a co-receptor for TGF-β family ligands, modulating cellular responses to these growth factors .

Role in Immune Responses and Pathogen Recognition: Endoglin plays a role in leukocyte trafficking and extravasation by binding to leukocyte integrins . It is involved in the immune response by regulating the adhesion and migration of immune cells .

Modes of Action

Mechanisms with Other Molecules and Cells: Endoglin interacts with various molecules, including TGF-β receptors, integrins, and metalloproteinases . It can be cleaved by metalloproteinase MMP-14, producing a soluble form that acts as a ligand trap .

Binding Partners and Downstream Signaling Cascades: Endoglin binds to TGF-β1, TGF-β3, BMP-2, BMP-7, and BMP-9, modulating their signaling pathways . It also interacts with zyxin, ZRP-1, beta-arrestin, and Tctex2beta, influencing cytoskeletal dynamics and cell migration .

Regulatory Mechanisms

Control of Expression and Activity: Endoglin expression is regulated by hypoxia, oxidative stress, and signaling molecules like TGF-β1 and BMP-9 . Its activity is modulated by post-translational modifications, including phosphorylation and cleavage by metalloproteinases .

Transcriptional Regulation and Post-Translational Modifications: Endoglin expression is upregulated by transcription factors such as Fli-1 and Erg . Post-translational modifications, including glycosylation and phosphorylation, affect its stability and function .

Applications

Biomedical Research: Endoglin is a marker for angiogenesis and is used in research on vascular diseases and cancer .

Diagnostic Tools: Elevated endoglin levels are associated with tumor angiogenesis, making it a potential diagnostic marker for cancer .

Therapeutic Strategies: Targeting endoglin with antibodies or inhibitors is being explored as a therapeutic strategy for cancer and other angiogenesis-related diseases .

Role in the Life Cycle

Development: Endoglin is crucial for cardiovascular development and vascular remodeling during embryogenesis .

Aging and Disease: Endoglin expression is associated with various diseases, including hereditary hemorrhagic telangiectasia (HHT), preeclampsia, and cancer . Its role in angiogenesis and immune responses makes it a key player in aging and disease progression .

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