Endoglin (27-581) Mouse

Endoglin (27-581) Mouse Recombinant

Recombinant Mouse Endoglin, produced in Sf9 Baculovirus cells, is a single glycosylated polypeptide chain comprising 563 amino acids (residues 27-581). It has a molecular weight of 60.9 kDa and migrates at 50-70 kDa on SDS-PAGE under reducing conditions. The protein includes an 8 amino acid His tag at the C-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21639
Source
Sf9, Baculovirus cells.
Appearance
A clear, colorless solution that has been sterilized by filtration.

Endoglin Human

Endoglin Human Recombinant

This product consists of the extracellular domain of human Endoglin, recombinantly produced in E.Coli. It is a single, glycosylated polypeptide chain comprising 151 amino acids (residues 26-176), resulting in a molecular weight of 43 kDa. The purification process involves proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT21737
Source
Escherichia Coli.
Appearance
The product is a clear, colorless liquid solution that has been sterilized by filtration.

Endoglin Human, His

Endoglin Human Recombinant, His-Tag

Recombinant Human Endoglin, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It contains 594 amino acids (26-586), including a 36 amino acid His-tag at the N-terminus, and has a molecular mass of 64.9 kDa.
Shipped with Ice Packs
Cat. No.
BT21843
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

Endoglin Human, Sf9

Endoglin Human Recombinant, Sf9

Recombinant human CD105, expressed in baculovirus, is a glycosylated homodimeric polypeptide. It consists of 586 amino acids, with a predicted molecular weight of 61 kDa. Due to glycosylation, it migrates at approximately 90 kDa under reducing conditions in SDS-PAGE. The CD105 protein is engineered with a C-terminal His-tag (6xHis) for purification using specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT21925
Source
Sf9 Insect Cells.
Appearance
White, sterile-filtered powder obtained by lyophilization (freeze-drying).

Endoglin Mouse

Endoglin Mouse Recombinant

Recombinant Mouse Endoglin, encompassing the extracellular domain, is produced in a baculovirus expression system. This homodimeric glycoprotein consists of 581 amino acids, resulting in a molecular mass of 61 kDa. However, due to glycosylation, it migrates at 75-85 kDa under reducing conditions in SDS-PAGE. The primary structure of the mature recombinant Endoglin, as determined by N-terminal sequence analysis, commences at Glu 26. This protein is engineered with a C-terminal His-tag (6xHis) and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21993
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized powder.
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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