Antibody data
- Antibody Data
- Antigen structure
- References [4]
- Comments [0]
- Validations [0]
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- Product number
- ABIN155165 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-TEK Tyrosine Kinase, Endothelial (TEK) antibody (Biotin)
- Antibody type
- Monoclonal
- Description
- Protein G purified
- Reactivity
- Human
- Host
- Mouse
- Conjugate
- Biotin
- Isotype
- IgG
- Antibody clone number
- Cl-16
- Vial size
- 50 μg
- Storage
- Prior to reconstitution store at -20°C. Following reconstitution store undiluted at 2-8°C for two weeks or (in aliquots) at -20°C for longer.
- Handling
- Avoid repeated freezing and thawing.
Submitted references Identification of cell surface proteins for antibody-based selection of human embryonic stem cell-derived cardiomyocytes.
Soluble Tie2 and Flt1 extracellular domains in serum of patients with renal cancer and response to antiangiogenic therapy.
Functions of Tie1 and Tie2 receptor tyrosine kinases in vascular development.
Angiopoietin-1 and -2 coiled coil domains mediate distinct homo-oligomerization patterns, but fibrinogen-like domains mediate ligand activity.
Van Hoof D, Dormeyer W, Braam SR, Passier R, Monshouwer-Kloots J, Ward-van Oostwaard D, Heck AJ, Krijgsveld J, Mummery CL
Journal of proteome research 2010 Mar 5;9(3):1610-8
Journal of proteome research 2010 Mar 5;9(3):1610-8
Soluble Tie2 and Flt1 extracellular domains in serum of patients with renal cancer and response to antiangiogenic therapy.
Harris AL, Reusch P, Barleon B, Hang C, Dobbs N, Marme D
Clinical cancer research : an official journal of the American Association for Cancer Research 2001 Jul;7(7):1992-7
Clinical cancer research : an official journal of the American Association for Cancer Research 2001 Jul;7(7):1992-7
Functions of Tie1 and Tie2 receptor tyrosine kinases in vascular development.
Partanen J, Dumont DJ
Current topics in microbiology and immunology 1999;237:159-72
Current topics in microbiology and immunology 1999;237:159-72
Angiopoietin-1 and -2 coiled coil domains mediate distinct homo-oligomerization patterns, but fibrinogen-like domains mediate ligand activity.
Procopio WN, Pelavin PI, Lee WM, Yeilding NM
The Journal of biological chemistry 1999 Oct 15;274(42):30196-201
The Journal of biological chemistry 1999 Oct 15;274(42):30196-201
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