TEK Mouse Fc

TEK Tyrosine Kinase Endothelial Fc Chimera Mouse Recombinant

Soluble TEK Mouse Recombinant, fused with the Fc region of human IgG1, is produced in CHO cells. It is a glycosylated, disulfide-linked homodimeric polypeptide encompassing amino acids 119-740, resulting in a total molecular mass of 280 kDa. Each monomer of Mouse TIE-2/Fc has a calculated molecular mass of approximately 105 kDa. Glycosylation contributes to the recombinant protein's migration as an approximately 140 kDa protein in SDS-PAGE under reducing conditions. The purification of the TEK Fc Chimera is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28612
Source
CHO Cells.
Appearance
Sterile Filtered White lyophilized powder.

TIE1 Fc Human

TIE1 Fc Human Recombinant

Recombinant human TIE-1 Fc Chimera, produced in baculovirus, is a homodimeric glycoprotein. It consists of 749 amino acids fused with the Fc region of human IgG1, resulting in a total molecular mass of 250 kDa. The monomeric form of human TIE-1/Fc has a calculated molecular mass of approximately 105 kDa. However, due to glycosylation, it migrates as an approximately 125 kDa protein on SDS-PAGE under reducing conditions. Purification of the TIE1 Fc Chimera is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28685
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

TIE1 Fc Mouse

TIE1 Fc Chimera Mouse Recombinant

Soluble TIE-1 Mouse Recombinant, fused with the Fc region of human IgG1, is produced in CHO cells. It is a glycosylated, disulfide-linked homodimeric polypeptide chain comprising amino acids 23-749, with a total molecular mass of 260 kDa. Each TIE-1/Fc monomer has a calculated molecular mass of approximately 105 kDa. Due to glycosylation, the recombinant protein migrates at approximately 130 kDa in SDS-PAGE under reducing conditions. The TIE1 Fc Chimera is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28737
Source
CHO Cells.
Appearance
Sterile Filtered White lyophilized powder.

TEK Mouse

TEK Tyrosine Kinase Endothelial Mouse Recombinant

TEK, a single glycosylated polypeptide chain produced in Sf9 Baculovirus cells, contains 730 amino acids (23-746 a.a.) and has a molecular mass of 81.6kDa. (Migrates at 70-100kDa on SDS-PAGE under reducing conditions). TEK is purified using proprietary chromatographic methods and expressed with a 6 amino acid His tag at the C-Terminus.
Shipped with Ice Packs
Cat. No.
BT28354
Source
Sf9, Baculovirus cells.
Appearance
Colorless solution that has been sterile filtered.

TEK Human

TEK Tyrosine Kinase Endothelial Human Recombinant

Recombinant human TEK, expressed in Sf9 insect cells using baculovirus, is a glycosylated polypeptide chain with a molecular weight of approximately 107.9 kDa (appears as 100-150 kDa on SDS-PAGE). It encompasses amino acids 23-748 of the TEK protein and includes a C-terminal 239 amino acid hIgG-His tag for purification.

Shipped with Ice Packs
Cat. No.
BT28441
Source
Sf9, Baculovirus cells.
Appearance
Clear, colorless solution, sterile-filtered.

TEK Human Fc

TEK Tyrosine Kinase Endothelial Fc Chimera Human Recombinant

Soluble TEK Human Recombinant, fused with the Fc portion of human IgG1, is produced in a baculovirus expression system. This monomeric, glycosylated polypeptide comprises 730 amino acids, resulting in a total molecular mass of 250 kDa. While the calculated molecular mass of the TIE-2/Fc monomer is approximately 125 kDa, glycosylation causes the recombinant protein to migrate at approximately 140 kDa in SDS-PAGE under reducing conditions. Purification of the TEK Fc Chimera is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT28524
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized powder.
Definition and Classification

TIE1 and TIE2 are receptor tyrosine kinases (RTKs) that form a distinct subfamily characterized by their unique extracellular domains. These receptors are primarily expressed in endothelial cells and play crucial roles in vascular development and homeostasis. TIE1 is often referred to as an orphan receptor due to the lack of a well-defined ligand, while TIE2 interacts with angiopoietins (ANG1, ANG2, ANG4) to mediate its functions .

Biological Properties

Key Biological Properties: TIE1 and TIE2 are integral to angiogenesis and blood vessel stability. TIE2, in particular, is activated by its ligands, leading to endothelial cell survival, migration, and vascular maturation .

Expression Patterns: Both receptors are predominantly expressed in endothelial cells. TIE1 is also found in hematopoietic cells during certain developmental stages .

Tissue Distribution: TIE1 and TIE2 are widely distributed in vascular and lymphatic endothelial cells. TIE2 is also present in circulating hematopoietic cells, including megakaryocytes and neutrophils .

Biological Functions

Primary Biological Functions: TIE1 and TIE2 are essential for vascular development and maintenance. TIE2, activated by ANG1, promotes endothelial cell survival and vascular integrity. TIE1 modulates the effects of ANG1 and ANG2 on TIE2, influencing angiogenesis and vascular remodeling .

Role in Immune Responses and Pathogen Recognition: TIE2 signaling is associated with anti-inflammatory effects, reducing leukocyte adhesion and transendothelial migration .

Modes of Action

Mechanisms with Other Molecules and Cells: TIE1 and TIE2 interact with angiopoietins to regulate endothelial cell functions. ANG1 binding to TIE2 promotes cell survival and vascular stability, while ANG2 can act as both an agonist and antagonist depending on the context .

Binding Partners and Downstream Signaling Cascades: TIE2 activation by ANG1 leads to downstream signaling involving the PI3K/Akt pathway, promoting cell survival and vascular stability. TIE1 modulates TIE2 signaling by influencing its interactions with ANG1 and ANG2 .

Regulatory Mechanisms

Transcriptional Regulation: The expression of TIE1 and TIE2 is regulated by various transcription factors that respond to developmental and environmental cues .

Post-Translational Modifications: TIE1 undergoes ectodomain cleavage in response to inflammatory signals, which modulates its interaction with TIE2 and affects downstream signaling .

Applications

Biomedical Research: TIE1 and TIE2 are studied for their roles in vascular biology and disease. Understanding their functions can lead to insights into angiogenesis and vascular disorders .

Diagnostic Tools: Alterations in TIE1 and TIE2 expression or function can serve as biomarkers for vascular diseases and cancer .

Therapeutic Strategies: Targeting the TIE1/TIE2 pathway holds potential for treating diseases characterized by vascular dysfunction, such as cancer, diabetic retinopathy, and inflammatory conditions .

Role in the Life Cycle

Development: TIE1 and TIE2 are crucial for embryonic vascular development. TIE2, activated by ANG1, supports the formation and maturation of blood vessels .

Aging and Disease: Dysregulation of TIE1 and TIE2 signaling is implicated in various age-related diseases, including atherosclerosis and cancer. Therapeutic modulation of these pathways may offer benefits in managing these conditions .

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