• Product name

    Recombinant Human TIE2 protein (Fc Chimera)
    See all TIE2 proteins and peptides
  • Purity

    > 90 % SDS-PAGE.
    Source: Insect cells. Purity: > 90%, by SDS-PAGE and visualised by silver stain. Endotoxin level: < 0.1 ng per ug sTIE-2/Fc.
  • Expression system

    Insect cells
  • Accession

  • Protein length

    Protein fragment
  • Animal free

  • Nature

    • Species

    • Sequence

    • Amino acids

      23 to 731
    • Additional sequence information

      Sequence = aa23-731 of TIE2 fused to the Fc part of human IgG1.

Associated products


Our Abpromise guarantee covers the use of ab54435 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications


    Western blot


  • Form

  • Additional notes

    The recombinant mature TIE-2/Fc is a disulfide-linked homodimeric protein. The soluble receptor protein consists of the full extracellular domain (Met1-Val730).

    Human TIE-2-Fc monomer has a calculated molecular mass of approximately 105kDa. As a result of glycosylation, the recombinant protein migrates as an approximately 125kDa protein in SDS-PAGE under reducing conditions.

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.

    Constituent: PBS

  • Reconstitution
    The lyophilised sTIE-2/Fc is soluble in water and most aqueous buffers. The lyophilised sTIE-2/Fc should be reconstituted in PBS or medium to a concentration not lower than 50 µg/ml.

General Info

  • Alternative names

    • Angiopoietin 1 receptor
    • Angiopoietin-1 receptor
    • CD202b
    • CD202b antigen
    • Endothelial tyrosine kinase
    • Endothelium specific receptor tyrosine kinase 2
    • hTIE 2
    • hTIE2
    • Hyk
    • p140 TEK
    • Soluble TIE2 variant 1
    • Soluble TIE2 variant 2
    • Tek
    • tek tyrosine kinase
    • TEK tyrosine kinase endothelial
    • tek tyrosine kinase, endothelial
    • TIE 2
    • TIE2
    • TIE2_HUMAN
    • Tunica interna endothelial cell kinase
    • Tyrosine kinase with Ig and EGF homology domains 2
    • Tyrosine kinase with Ig and EGF homology domains-2
    • Tyrosine protein kinase receptor TEK
    • Tyrosine protein kinase receptor TIE 2
    • Tyrosine-protein kinase receptor TEK
    • Tyrosine-protein kinase receptor TIE-2
    • Venous malformations multiple cutaneous and mucosal
    • VMCM
    • VMCM 1
    • VMCM1
    see all
  • Function

    Tyrosine-protein kinase that acts as cell-surface receptor for ANGPT1, ANGPT2 and ANGPT4 and regulates angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Has anti-inflammatory effects by preventing the leakage of proinflammatory plasma proteins and leukocytes from blood vessels. Required for normal angiogenesis and heart development during embryogenesis. Required for post-natal hematopoiesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. ANGPT1 signaling triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Signaling is modulated by ANGPT2 that has lower affinity for TEK, can promote TEK autophosphorylation in the absence of ANGPT1, but inhibits ANGPT1-mediated signaling by competing for the same binding site. Signaling is also modulated by formation of heterodimers with TIE1, and by proteolytic processing that gives rise to a soluble TEK extracellular domain. The soluble extracellular domain modulates signaling by functioning as decoy receptor for angiopoietins. TEK phosphorylates DOK2, GRB7, GRB14, PIK3R1; SHC1 and TIE1.
  • Tissue specificity

    Detected in umbilical vein endothelial cells. Proteolytic processing gives rise to a soluble extracellular domain that is detected in blood plasma (at protein level). Predominantly expressed in endothelial cells and their progenitors, the angioblasts. Has been directly found in placenta and lung, with a lower level in umbilical vein endothelial cells, brain and kidney.
  • Involvement in disease

    Dominantly inherited venous malformations
    May play a role in a range of diseases with a vascular component, including neovascularization of tumors, psoriasis and inflammation.
  • Sequence similarities

    Belongs to the protein kinase superfamily. Tyr protein kinase family. Tie subfamily.
    Contains 3 EGF-like domains.
    Contains 3 fibronectin type-III domains.
    Contains 2 Ig-like C2-type (immunoglobulin-like) domains.
    Contains 1 protein kinase domain.
  • Domain

    The soluble extracellular domain is functionally active in angiopoietin binding and can modulate the activity of the membrane-bound form by competing for angiopoietins.
  • Post-translational

    Proteolytic processing leads to the shedding of the extracellular domain (soluble TIE-2 alias sTIE-2).
    Autophosphorylated on tyrosine residues in response to ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Autophosphorylation occurs in a sequential manner, where Tyr-992 in the kinase activation loop is phosphorylated first, followed by autophosphorylation at Tyr-1108 and at additional tyrosine residues. ANGPT1-induced phosphorylation is impaired during hypoxia, due to increased expression of ANGPT2. Phosphorylation is important for interaction with GRB14, PIK3R1 and PTPN11. Phosphorylation at Tyr-1102 is important for interaction with SHC1, GRB2 and GRB7. Phosphorylation at Tyr-1108 is important for interaction with DOK2 and for coupling to downstream signal transduction pathways in endothelial cells. Dephosphorylated by PTPRB.
    Ubiquitinated. The phosphorylated receptor is ubiquitinated and internalized, leading to its degradation.
  • Cellular localization

    Cell membrane. Cell junction. Cell junction, focal adhesion. Cytoplasm, cytoskeleton. Secreted. Recruited to cell-cell contacts in quiescent endothelial cells. Colocalizes with the actin cytoskeleton and at actin stress fibers during cell spreading. Recruited to the lower surface of migrating cells, especially the rear end of the cell. Proteolytic processing gives rise to a soluble extracellular domain that is secreted.
  • Information by UniProt


  • SDS-PAGE of recombinant human soluble TIE-2/Fc produced from insect cells. The sample was loaded in 10% SDS-polyacrylamide gel under reducing condition and stained with Coomassie blue.

  • Anti-TIE2 antibody [Cl. 16] (ab24859) at 1 µg/ml + Recombinant Human TIE2 protein (Fc Chimera) (ab54435) at 0.01 µg

    Goat Anti-Mouse IgG H&L (HRP) preadsorbed (ab97040) at 1/5000 dilution

    Developed using the ECL technique.

    Performed under reducing conditions.

    Exposure time: 2 minutes


ab54435 has not yet been referenced specifically in any publications.

Customer reviews and Q&As


body {
margin: 0px;
margin-top: 10px;
font-family: arial, verdana, tahoma;
background-color: #F5F5EE;

padding-top: 4px;
margin: 0px;
line-height: 18px;

body table{
font-size: 12px;
line-height: 100%;

a {
text-decoration: underline;
color: #004a91;

a:visited {
color: #0096db;

a:hover {
color: #0096db;
text-decoration: underline;

.mainText {
margin-left: 0cm;
font-weight: normal;
margin-left: 10px;

.tagLine {
margin-left: 0cm;
font-weight: normal;
margin-left: 10px;
color: #FFFFFF;

.tagLine a {
margin-left: 0cm;
font-weight: normal;
text-decoration: none;
color: #FFFFFF;

.tagLink {
margin-left: 0cm;
font-weight: normal;
text-decoration: none;
color: #FFFFFF;
font-weight: bold;

Thank you for contacting Abcam.

The protein ab54435 does not havea His-tag but a C-terminal Fc-tag.

If there is anything else I can help you with, please let me know.

Read More

For licensing inquiries, please contact

Sign up